{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T14:06:58Z","timestamp":1787062018614,"version":"build-2736575974"},"reference-count":245,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2025,1,13]],"date-time":"2025-01-13T00:00:00Z","timestamp":1736726400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"University of Hawaii Cancer Center"},{"name":"Regucalcin Biomedical Institute in Shizuoka, Japan"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cancers"],"abstract":"<jats:p>The regucalcin gene is located on the X chromosome, comprising seven exons and six introns. This gene and protein are expressed in various tissues and cells and is predominantly expressed in human liver, kidney, and adrenal tissues. Regucalcin gene expression is enhanced via a mechanism mediated by several signaling molecules and transcription factors. Regucalcin plays a multifunctional role in cellular regulation in maintaining cell homeostasis. In addition, regucalcin has been implicated in several metabolic disorders and diseases. In particular, regucalcin plays a role as a novel suppressor in several types of cancer patients. Increased expression of regucalcin suppresses the growth of human cancer cells, suggesting its pivotal role in suppressing tumor development. The survival time of cancer patients is prolonged with increased expression of regucalcin in the tumor tissues. The adhesion, migration, invasion, and bone metastatic activity of cancer cells are blocked by the overexpression of regucalcin, promoting dormancy in cancer patients. Interestingly, regucalcin is also found in human serum, suggesting its character as a novel biomarker in various diseases. This extracellular regucalcin has been shown to suppress human cancer cells\u2019 growth and bone metastatic activity. Thus, extracellular regucalcin may play a vital role as a suppressor of human cancer activity. Alteration of the serum regucalcin levels in physiological and pathophysiological conditions may influence the activity of cancer cells in the microenvironment. This review will discuss the potential role of extracellular regucalcin in cancer cell activity as a critical suppressor in the cancer microenvironment.<\/jats:p>","DOI":"10.3390\/cancers17020240","type":"journal-article","created":{"date-parts":[[2025,1,13]],"date-time":"2025-01-13T07:40:08Z","timestamp":1736754008000},"page":"240","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Extracellular Regucalcin: A Potent Suppressor in the Cancer Cell Microenvironment"],"prefix":"10.3390","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8511-110X","authenticated-orcid":false,"given":"Masayoshi","family":"Yamaguchi","sequence":"first","affiliation":[{"name":"Cancer Biology Program, University of Hawaii Cancer Center, University of Hawaii at Manoa, 701 Ilalo Street, Honolulu, HI 96813, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,1,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1126\/science.170.3956.404","article-title":"Cell communication, calcium ion, and cyclic adenosine monophosphate","volume":"170","author":"Rasmussen","year":"1970","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1126\/science.6243188","article-title":"Calmodulin plays a pivotal role in cellular regulation","volume":"202","author":"Cheung","year":"1980","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1126\/science.3014651","article-title":"Studies and perspectives of protein kinase C","volume":"233","author":"Nishizuka","year":"1986","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1146\/annurev.ph.51.030189.000543","article-title":"Hormonal effects on cellular Ca2+ fluxes","volume":"51","author":"Williamson","year":"1989","journal-title":"Annu. Rev. Physiol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Li, W., Ye, C., He, M., Ko, W.K.W., Cheng, C.H.K., Chan, Y.W., and Wong, A.O.L. (2024). Differential involvement of cAMP\/PKA-, PLC\/PKC- and Ca2+\/calmodulin-dependent pathways in GnRH-induced prolactin secretion and gene expression in grass carp pituitary cells. Front. Endocrinol., 15.","DOI":"10.3389\/fendo.2024.1399274"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/978-3-030-12457-1_8","article-title":"An update to calcium binding proteins","volume":"1131","author":"Elies","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1915","DOI":"10.1248\/cpb.26.1915","article-title":"Purification of calcium binding substance from soluble fraction of normal rat liver","volume":"26","author":"Yamaguchi","year":"1978","journal-title":"Chem. Pharm. Bull."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1016\/S0024-3205(99)00602-5","article-title":"Role of regucalcin in calcium signaling","volume":"66","author":"Yamaguchi","year":"2000","journal-title":"Life Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/0014-5793(93)80998-A","article-title":"Molecular cloning and sequencing of the cDNA coding for a calcium-binding protein regucalcin from rat liver","volume":"327","author":"Shimokawa","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/0167-4781(92)90164-U","article-title":"Isolation of cDNA clone encoding rat senescence marker protein-30 (SMP30) and its tissue distribution","volume":"1132","author":"Fujita","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_11","first-page":"191","article-title":"The gene of Ca2+-binding protein regucalcin is highly conserved in vertebrate species","volume":"6","author":"Misawa","year":"2000","journal-title":"Int. J. Mol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/BF01322338","article-title":"Genomic cloning and chromosomal assignment of rat regucalcin gene","volume":"151","author":"Shimokawa","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/BF00229476","article-title":"The 5\u2019end seguences and exon organization in rat regucalcin gene","volume":"165","author":"Yamaguchi","year":"1996","journal-title":"Mol. Cell. Biochem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1006\/geno.2002.6733","article-title":"An integrated, functionally annotated gene map of the DXS8026-ELK1 internal on human Xp11.3-Xp11.23: Potential hotspot for neurogenetic disorders","volume":"79","author":"Thiselton","year":"2002","journal-title":"Genomics"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1042\/bj3290157","article-title":"Ca2+ administration stimulates the binding of AP-1 factor to the 5\u2032-flanking region of the rat gene for the Ca2+-binding protein regucalcin","volume":"329","author":"Murata","year":"1998","journal-title":"Biochem. J."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1074\/jbc.274.3.1277","article-title":"Promoter characterization of the rat gene for Ca2+- binding protein regucalcin. Transcriptional regulation by signaling factors","volume":"274","author":"Murata","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_17","first-page":"513","article-title":"Molecular cloning and sequencing of the cDNA coding for a novel regucalcin gene promoter region-related protein in rat, mouse and human liver","volume":"8","author":"Misawa","year":"2001","journal-title":"Int. J. Mol. Med."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/s11010-009-0042-4","article-title":"Novel protein RGPR-p117: Its role as the regucalcin gene transcription factor","volume":"327","author":"Yamaguchi","year":"2009","journal-title":"Mol. Cell. Biochem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"28115","DOI":"10.1074\/jbc.M109.047258","article-title":"\u03b2-Catenin regulates vitamic C biosynthesis and cell survival in murine liver","volume":"284","author":"Zeng","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/s11010-010-0601-8","article-title":"The transcriptional regulation of regucalcin gene expression","volume":"346","author":"Yamaguchi","year":"2011","journal-title":"Mol. Cell. Biochem."},{"key":"ref_21","first-page":"371","article-title":"Role of regucalcin in maintaining cell homeostasis and function (Review)","volume":"15","author":"Yamaguchi","year":"2005","journal-title":"Int. J. Mol. Med."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s11010-011-0779-4","article-title":"Regucalcin and cell regulation: Role as a suppressor in cell signaling","volume":"353","author":"Yamaguchi","year":"2011","journal-title":"Mol. Cell. Biochem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/s00018-013-1323-3","article-title":"The diverse roles of calcium-binding protein regucalcin in cell biology: From tissue expression and signalling to disease","volume":"71","author":"Marques","year":"2014","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/s00441-013-1665-z","article-title":"Role of regucalcin in cell nuclear regulation: Involvement as a transcription factor","volume":"354","author":"Yamaguchi","year":"2013","journal-title":"Cell Tissue Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1111\/cpr.12036","article-title":"Suppressive role of regucalcin in liver cell proliferation: Involvement in carcinogenesis","volume":"46","author":"Yamaguchi","year":"2013","journal-title":"Cell Prolif."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1007\/s10495-013-0859-x","article-title":"The anti-apoptotic effect of regucalcin is mediated through multisignaling pathways","volume":"18","author":"Yamaguchi","year":"2013","journal-title":"Apoptosis"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/s11010-010-0443-4","article-title":"Regucalcin and metabolic disorder: Osteoporosis and hyperlipidemia are induced in regucalcin transgenic rats","volume":"341","author":"Yamaguchi","year":"2010","journal-title":"Mol. Cell. Biochem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1093\/molehr\/gar075","article-title":"Regucalcin, a calcium-binding protein with a role in male reproduction","volume":"18","author":"Laurentino","year":"2012","journal-title":"Mol. Hum. Reprod."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1016\/j.metabol.2013.01.023","article-title":"Involvement of regucalcin in lipid metabolism and diabetes","volume":"62","author":"Yamaguchi","year":"2013","journal-title":"Metabolism"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"110533","DOI":"10.1016\/j.cellsig.2022.110533","article-title":"Functional pleiotropy of calcium binding protein Regucalcin in signaling and diseases","volume":"102","author":"Danish","year":"2023","journal-title":"Cell Signal."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"303","DOI":"10.3892\/br.2014.245","article-title":"Regulatory role of regucalcin in heart calcium signaling: Insight into cardiac failure (Review)","volume":"2","author":"Yamaguchi","year":"2014","journal-title":"Biomed Rep."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"607","DOI":"10.2174\/1566524016666160714124550","article-title":"The emerging role of regucalcin as a tumor suppressor: Facts and view","volume":"16","author":"Vaz","year":"2016","journal-title":"Curr. Mol. Med."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1007\/s00432-014-1831-z","article-title":"Involvement of regucalcin as a suppressor protein in human carcinogenesis: Insight into the gene therapy","volume":"141","author":"Yamaguchi","year":"2015","journal-title":"J. Cancer Res. Clin. Oncol."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Yamaguchi, M. (2023). Regucalcin is a potential regulator in human cancer: Aiming to expand into cancer therapy. Cancers, 15.","DOI":"10.3390\/cancers15225489"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.3892\/ijo.2016.3669","article-title":"Prolonged survival in hepatocarcinoma patients with increased regucalcin. gene expression: HepG2 cell proliferation is suppressed by overexpression of. regucalcin in vitro","volume":"49","author":"Yamaguchi","year":"2016","journal-title":"Int. J. Oncol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.3892\/ijo.2016.3409","article-title":"Prolonged. survival in pancreatic cancer patients with increased regucalcin gene expression: Overexpression of regucalcin suppresses the proliferation in human pancreatic cancer MIA PaCa-2 cells in vitro","volume":"48","author":"Yamaguchi","year":"2016","journal-title":"Int. J. Oncol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"812","DOI":"10.3892\/ijo.2016.3538","article-title":"Increased regucalcin gene expression extends survival in breast cancer patients: Overexpression of regucalcin suppresses the proliferation and metastatic bone activity in MDA-MB-231 human breast cancer cells in vitro","volume":"49","author":"Yamaguchi","year":"2016","journal-title":"Int. J. Oncol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/s11010-017-2952-x","article-title":"Survival of lung cancer patients is prolonged with higher regucalcin gene expression: Suppressed proliferation of lung adenocarcinoma A549 cells in vitro","volume":"430","author":"Yamaguchi","year":"2017","journal-title":"Mol. Cell. Biochem."},{"key":"ref_39","first-page":"1313","article-title":"Prolonged survival of colorectal cancer patients is associated with higher regucalcin gene expression: Overexpressed regucalcin suppresses growth of human colorectal carcinoma cells in vitro","volume":"53","author":"Yamaguchi","year":"2018","journal-title":"Int. J. Oncol."},{"key":"ref_40","first-page":"188","article-title":"Prolonged survival of renal cancer patients are concomitant with a higher regucalcin gene expression in the tumor tissues: Overexpression of regucalcin depresses the growth of human renal cell carcinoma cells in vitro","volume":"54","author":"Yamaguchi","year":"2019","journal-title":"Int. J. Oncol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"100955","DOI":"10.1016\/j.tranon.2020.100955","article-title":"Progression-free survival of prostate cancer patients are prolonged with a higher regucalcin expression in the tumor tissues: Overexpressed regucalcin suppresses the growth and bone metastatic activity of PC-3 cells in vitro","volume":"14","author":"Yamaguchi","year":"2021","journal-title":"Transl. Oncol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"122448","DOI":"10.1016\/j.lfs.2024.122448","article-title":"Regucalcin downregulation in human cancer tissue","volume":"340","author":"Ghanem","year":"2024","journal-title":"Life Sci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/BF00928911","article-title":"Expression of hepatic calcium-binding protein regucalcin mRNA is elevated by refeeding of fasted rats: Involvement of glucose, insulin and calcium as stimulating factors","volume":"142","author":"Yamaguchi","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1007\/BF00925954","article-title":"Hepatic calcium-binding protein regucalcin is released into the serum of rats administered orally carbon tetrachloride","volume":"131","author":"Isogai","year":"1994","journal-title":"Mol. Cell. Biochem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/s11010-014-1998-2","article-title":"Regucalcin as a potential biomarker for metabolic and neuronal diseases","volume":"391","author":"Yamaguchi","year":"2014","journal-title":"Mol. Cell. Biochem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"e14085","DOI":"10.1111\/apha.14085","article-title":"Hyperpolarization-activated cyclic nucleotide-gated channel inhibitor in myocardial infarction: Potential benefits beyond heart rate modulation","volume":"240","author":"Sripusanapan","year":"2024","journal-title":"Acta Physiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"122309","DOI":"10.1016\/j.lfs.2023.122309","article-title":"Vascular calcification and cellular signaling pathways as potential therapeutic targets","volume":"336","author":"Kang","year":"2024","journal-title":"Life Sci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.phrs.2019.01.008","article-title":"Debating the \u201cbidirectional link\u201d between diabetes and depression through the Ca2+\/cAMP signalling: Off-label effects of Ca2+ channel blockers","volume":"141","author":"Bergantin","year":"2019","journal-title":"Pharmacol. Res."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Haynes, V., and Giulivi, C. (2023). Calcium-dependent interaction of nitric oxide synthase with cytochrome c oxidase: Implications for brain bioenergetics. Brain Sci., 13.","DOI":"10.3390\/brainsci13111534"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Semenikhina, M., Stefanenko, M., Spires, D.R., Ilatovskaya, D.V., and Palygin, O. (2022). Nitric-oxide-mediated signaling in podocyte pathophysiology. Biomolecules, 12.","DOI":"10.3390\/biom12060745"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Takata, T., Araki, S., Tsuchiya, Y., and Watanabe, Y. (2020). Oxidative stress orchestrates MAPK and nitric oxide synthase signal. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21228750"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Sun, Y., Dinenno, F.A., Tang, P., and Kontaridis, M.I. (2024). Protein tyrosine phosphatase 1B in metabolic and cardiovascular diseases: From mechanisms to therapeutics. Front. Cardiovasc. Med., 11.","DOI":"10.3389\/fcvm.2024.1445739"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"214199","DOI":"10.1111\/apha.14199","article-title":"Cardiovascular toxicities by calcineurin inhibitors: Cellular mechanisms behind clinical manifesttations","volume":"240","author":"Attachaipanich","year":"2024","journal-title":"Acta Physiol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1002\/(SICI)1097-4644(19981001)71:1<140::AID-JCB14>3.0.CO;2-R","article-title":"Inhibition of Ca2+\/calmodulin-dependent phosphatase activity by regucalcin in rat liver cytosol: Involvement of calmodulin binding","volume":"71","author":"Omura","year":"1998","journal-title":"J. Cell. Biochem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/BF01261390","article-title":"Effect of calcium-binding protein regucalcin on hepatic protein synthesis: Inhibition of aminoacyl-tRNA synthetase activity","volume":"99","author":"Yamaguchi","year":"1990","journal-title":"Mol. Cell. Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/BF00929504","article-title":"Characterization of regucalcin effect on proteolytic activity in rat liver cytosol: Relation to cysteinyl-proteases","volume":"148","author":"Yamaguchi","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1023\/A:1007007626813","article-title":"Stimulatory effect of regucalcin on proteolytic activity is impaired in the kidney cortex cytosol of rats with saline ingestion","volume":"206","author":"Baba","year":"2000","journal-title":"Mol. Cell. Biochem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1002\/(SICI)1097-4644(19991201)75:3<437::AID-JCB9>3.0.CO;2-W","article-title":"Regulation of protein phosphatase activity by regucalcin localization in rat liver nuclei","volume":"75","author":"Omura","year":"1999","journal-title":"J. Cell. Biochem."},{"key":"ref_59","first-page":"655","article-title":"Translocation of regucalcin to rat liver nucleus: Involvement of nuclear protein kinase and protein phosphatase regulation","volume":"6","author":"Tsurusaki","year":"2000","journal-title":"Int. J. Mol. Med."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/0006-291X(80)90849-9","article-title":"Calmodulin stimulates DNA synthesis by rat liver cells","volume":"95","author":"Boynton","year":"1980","journal-title":"Biochem. Biophys Res. Commun."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"18863","DOI":"10.1016\/S0021-9258(19)47234-7","article-title":"Effect of alpha-adrenergic blockers on calmodulin associate with the nuclear matrix of rat liver cells during proliferative activation","volume":"264","author":"Pujol","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_62","first-page":"605","article-title":"Nuclear localization of regucalcin is enhanced in culture with protein kinase C activation in cloned normal rat kidney proximal tubular epithelial NRK52E cells","volume":"21","author":"Nakagawa","year":"2008","journal-title":"Int. J. Mol. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"6398","DOI":"10.1016\/S0021-9258(18)83363-4","article-title":"Calcium activated DNA fragmentation in rat liver nuclei","volume":"264","author":"Jones","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/0014-5793(91)80168-3","article-title":"Inhibitory effect of calcium-binding protein regucalcin on Ca2+-activated DNA fragmentation in rat liver nuclei","volume":"279","author":"Yamaguchi","year":"1991","journal-title":"FEBS Lett."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/BF00227538","article-title":"Calcium-binding protein regucalcin inhibits deoxyribonucleic acid synthesis in the nuclei of regenerating rat liver","volume":"162","author":"Yamaguchi","year":"1996","journal-title":"Mol. Cell. Biochem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1002\/jcb.10153","article-title":"Suppressive role of endogenous regucalcin in the enhancement of deoxyribonucleic acid synthesis activity in the nucleus of regenerating rat liver","volume":"85","author":"Tsurusaki","year":"2002","journal-title":"J. Cell. Biochem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1023\/A:1006833111236","article-title":"Inhibitory effect of calcium-binding protein regucalcin on ribonucleic acid synthesis in isolated rat liver nuclei","volume":"173","author":"Yamaguchi","year":"1997","journal-title":"Mol. Cell. Biochem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1002\/jcb.10325","article-title":"Role of endogenous regucalcin in nuclear regulation of regenerating rat liver: Suppression of the enhanced ribonucleic acid synthesis activity","volume":"87","author":"Tsurusaki","year":"2002","journal-title":"J. Cell. Biochem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1023\/A:1006996506238","article-title":"Expression of calcium-binding protein regucalcin mRNA in the cloned rat hepatoma cells (H4-II-E) is stimulated through Ca2+ signaling factors: Involvement of protein kinase C","volume":"198","author":"Nakajima","year":"1999","journal-title":"Mol. Cell. Biochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1023\/A:1006844815743","article-title":"Expression of calcium-binding protein regucalcin mRNA in the cloned human hepatoma cells (Hep G2): Stimulation by insulin","volume":"175","author":"Murata","year":"1997","journal-title":"Mol. Cell. Biochem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1002\/jcb.20056","article-title":"Overexpression of regucalcin suppresses cell death in cloned rat hepatoma H4-II-E cells induced by tumor necrosis factor-\u03b1 or thapsigargin","volume":"92","author":"Izumi","year":"2004","journal-title":"J. Cell. Biochem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1002\/jcb.20214","article-title":"Overexpression of regucalcin suppresses cell death and apoptosis in cloned rat hepatoma H4-II-E cells induced by lipopolysaccharide, PD98059, dibucaine, or Bay K 8644","volume":"93","author":"Izumi","year":"2004","journal-title":"J. Cell. Biochem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1002\/jcb.20617","article-title":"Over expression of regucalcin suppresses apoptotic cell death in cloned normal rat kidney proximal tubular epithelial NRK52E cells: Change in apoptosis-related gene expression","volume":"96","author":"Nakagawa","year":"2005","journal-title":"J. Cell. Biochem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1002\/jcb.1080","article-title":"Suppressive role of endogenous regucalcin in the enhancement of protein kinase activity with proliferation of cloned rat hepatoma cells (H4-II-E)","volume":"36","author":"Inagaki","year":"2001","journal-title":"J. Cell. Biochem."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1002\/jcb.1193","article-title":"Regulatory role of endogenous regucalcin in the enhancement of nuclear deoxyribonucleic acid synthesis with proliferation of cloned rat hepatoma cells (H4-II-E)","volume":"82","author":"Inagaki","year":"2001","journal-title":"J. Cell. Biochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1023\/A:1007100631753","article-title":"Role of endogenous regucalcin in protein tyrosine phosphatase regulation in the cloned rat hepatoma cells (H4-II-E)","volume":"213","author":"Inagaki","year":"2000","journal-title":"Mol. Cell. Biochem."},{"key":"ref_77","first-page":"323","article-title":"Enhancement of protein tyrosine phosphatase activity in the proliferation of cloned rat hepatoma H4-II-E cells: Suppressive role of endogenous regucalcin","volume":"6","author":"Inagaki","year":"2000","journal-title":"Int. J. Mol. Med."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1002\/jcb.1274","article-title":"Suppression of cell proliferation and deoxyribonucleic acid synthesis in cloned rat hepatoma H4-II-E cells overexpressing regucalcin","volume":"84","author":"Misawa","year":"2002","journal-title":"J. Cell. Biochem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1002\/jcb.20490","article-title":"Overexpression of regucalcin suppresses cell proliferation in cloned rat hepatoma H4-II-E cells: Involvement of intracellular signaling factors and cell cycle-related genes","volume":"95","author":"Yamaguchi","year":"2005","journal-title":"J. Cell. Biochem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1111\/j.1432-1033.1997.t01-2-00527.x","article-title":"Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5","volume":"243","author":"Meijer","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"25813","DOI":"10.1074\/jbc.M313538200","article-title":"Sulforaphane-induced G2\/M phase cell cycle arrest involves checkpoint kinase 2-mediated phosphorylation of cell division cycle 25C","volume":"279","author":"Singh","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1002\/jcp.1041450108","article-title":"Butyrate blocks the accumulation of CDC2 mRNA in late G1 phase but inhibits both early and late G1 progression in chemically transformed mouse fibroblasts BP-A31","volume":"145","author":"Charollais","year":"1990","journal-title":"J. Cell. Physiol."},{"key":"ref_83","unstructured":"Cohen, P., and Foulkes, J.G. (1991). Fos and June: Intermediary transcription factors. The Hormonal Control of Gene Transcription, Elsevier."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1093\/nar\/21.3.713","article-title":"Structure of the rat p53 tumor suppressor gene","volume":"21","author":"Hulla","year":"1993","journal-title":"Nucleic Acids Res."},{"key":"ref_85","first-page":"637","article-title":"Overexpression of regucalcin suppresses cell proliferation of cloned normal rat kidney proximal tubular epithelial NRK52E cells","volume":"16","author":"Nakagawa","year":"2005","journal-title":"Int. J. Mol. Med."},{"key":"ref_86","first-page":"186","article-title":"Experimental pathology of the liver. Restoration of the liver of the white rat following partial surgical removal","volume":"12","author":"Higgins","year":"1931","journal-title":"Arch. Pathol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/S0006-291X(05)80226-8","article-title":"Identification and change in the receptor for hepatocyte growth factor in rat liver after partial hepatectomy or induced hepatitis","volume":"176","author":"Higuchi","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1002\/jcp.1041530213","article-title":"Hepatocyte growth factor induces calcium mobilization and inositol phosphate production in rat hepatocytes","volume":"153","author":"Baffy","year":"1992","journal-title":"J. Cell. Physiol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/0014-5793(88)80868-8","article-title":"Increased calmodulin synthesis in the pre-replicative phase of rat liver regeneration","volume":"231","author":"Pinol","year":"1988","journal-title":"FEBS Lett."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1007\/BF00944611","article-title":"Enhancement of nuclear Ca2+-ATPase activity in regenerating rat liver: Involvement of nuclear DNA increase","volume":"146","author":"Kanayama","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/BF00230886","article-title":"Effect of calcium-binding protein regucalcin on Ca2+ transport system in rat liver nuclei: Stimulation of Ca2+ release","volume":"113","author":"Yamaguchi","year":"1992","journal-title":"Mol. Cell. Biochem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1002\/jcb.240570203","article-title":"Enhanced expression of calcium-binding protein regucalcin mRNA in regenerating rat liver","volume":"57","author":"Yamaguchi","year":"1995","journal-title":"J. Cell. Biochem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1002\/(SICI)1097-4644(19981215)71:4<569::AID-JCB11>3.0.CO;2-Z","article-title":"Inhibitory effect of calcium-binding protein regucalcin on protein kinase activity in the nuclei of regenerating rat liver","volume":"71","author":"Katsumata","year":"1998","journal-title":"J. Cell. Biochem."},{"key":"ref_94","first-page":"505","article-title":"Enhancement of protein kinase activity in the cytosol of regenerating rat liver: Regulatory role of endogenous regucalcin","volume":"3","author":"Yamaguchi","year":"1999","journal-title":"Int. J. Mol. Med."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1002\/(SICI)1097-4644(19990601)73:3<332::AID-JCB5>3.0.CO;2-U","article-title":"Enhancement of neutral phosphatase activity in the cytosol and nuclei of regenerating rat liver: Role of endogenous regucalcin","volume":"73","author":"Omura","year":"1999","journal-title":"J. Cell. Biochem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/bbrc.2000.3359","article-title":"The role of regucalcin in nuclear regulation of regenerating liver","volume":"276","author":"Yamaguchi","year":"2000","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"ref_97","first-page":"295","article-title":"Suppressive effect of endogenous regucalcin on the enhancement of protein synthesis and aminoacyl-tRNA synthetase activity in regenerating rat liver","volume":"6","author":"Tsurusaki","year":"2000","journal-title":"Int. J. Mol. Med."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1080\/07357907.2019.1708924","article-title":"Overexpression of regucalcin suppresses the growth of human osteosarcoma cells in vitro: Repressive effect of extracellular regucalcin","volume":"38","author":"Yamaguchi","year":"2020","journal-title":"Cancer Investig."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"121328","DOI":"10.1016\/j.lfs.2022.121328","article-title":"The overexpressed regucalcin represses the growth via regulating diverse pathways linked to EGF signaling in human ovarian cancer SK-OV-3 cells: Involvement of extracellular regucalcin","volume":"314","author":"Yamaguchi","year":"2023","journal-title":"Life Sci."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.1002\/ijc.25516","article-title":"Estimates of worldwide burden of cancer in 2008: GLOBOCA 2008","volume":"127","author":"Ferlay","year":"2012","journal-title":"Int. J. Cancer"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1056\/NEJMra1001683","article-title":"Hepatocellular carcinoma","volume":"365","year":"2011","journal-title":"N. Engl. J. Med."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Mo, Z., Zheng, S., Ly, Z., Zhuang, Y., Lan, X., Wang, F., Lu, X., Zhao, Y., and Zhou, S. (2016). Senescence marker protein 30 (SMP30) serves as a potential prognostic indicator in hepatocellular carcinoma. Sci. Rep., 6.","DOI":"10.1038\/srep39376"},{"key":"ref_103","first-page":"576","article-title":"Review of the current targeted therapies for non-small-cell lung cancer","volume":"5","author":"Nguyen","year":"2014","journal-title":"Wold J. Clin. Oncol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.4236\/jct.2015.615133","article-title":"The role of CHMP4C on proliferation in the human lung cancer A549 cells","volume":"6","author":"Li","year":"2015","journal-title":"J. Cancer Ther."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"22473","DOI":"10.1074\/jbc.M500963200","article-title":"EGF and hypoxia-induced expression of CXCR4 on non-small cell lung cancer cells are regulated by the PI3-kinase\/PTEN\/Akt\/mTOR signaling pathway and activation of HIF-1\u03b1","volume":"280","author":"Phillips","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1007\/s00109-014-1165-y","article-title":"Oncogenic drivers, targeted therapies, and acquired resistance in non-small-cell lung cancer","volume":"92","author":"Gower","year":"2014","journal-title":"J. Mol. Med."},{"key":"ref_107","first-page":"1407","article-title":"Cell division by the chromosomal passenger complex","volume":"318","author":"Hengeveld","year":"2009","journal-title":"Exp. Cell Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1038\/nrd2907","article-title":"Cell cycle kinases as therapeutic targets for cancer","volume":"8","author":"Lapenna","year":"2009","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"2201","DOI":"10.1111\/j.1742-4658.2009.06949.x","article-title":"The regulation of the endosomal compartment by p53 the tumor suppressor gene","volume":"276","author":"Yu","year":"2009","journal-title":"FEBS J."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1186\/s13148-019-0770-6","article-title":"Live and let die: Epigenetic modifications of Survivin and Regucalcin in non-small cell lung cancer tissues contribute to malignancy","volume":"11","author":"Nitschkowski","year":"2019","journal-title":"Clin. Epigenetics"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"4558","DOI":"10.21037\/tlcr-21-982","article-title":"Senescence marker protein 30 inhibits tumor growth by reducing HDAC4 expression in non-small cell lung cancer","volume":"10","author":"Shao","year":"2021","journal-title":"Transl. Lung Cancer Res."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"100205","DOI":"10.1016\/j.jbo.2018.10.004","article-title":"Metastatic bone disease: Pathogenesis and therapeutic options up-date on bone metastasis management","volume":"15","author":"Coleman","year":"2019","journal-title":"J. Bone Oncol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1186\/s40880-019-0425-1","article-title":"Interactions between cancer cells and bone microenvironment promote bone metastasis in prostate cancer","volume":"39","author":"Zhang","year":"2019","journal-title":"Cancer Commun."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1038\/s41388-018-0540-5","article-title":"Communication of prostate cancer cells with bone cells via extracellular vesicle RND; a potential mechanism of metastasis","volume":"38","author":"Probert","year":"2019","journal-title":"Oncogene"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s00223-017-0353-5","article-title":"Bone-targeted therapies in cancer-induced bone diseases","volume":"102","author":"Sousa","year":"2018","journal-title":"Calcif. Tissue Int."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1002\/pros.24348","article-title":"Overexpression of regucalcin blocks the migration, invasion, and bone metastatic activity of human prostate cancer cells: Crosstalk between cancer cells and bone cells","volume":"82","author":"Yamaguchi","year":"2022","journal-title":"Prostate"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1038\/s41388-020-01565-9","article-title":"Regucalcin promotes dormancy of prostate cancer","volume":"40","author":"Sharma","year":"2021","journal-title":"Oncogene"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1677\/erc.0.0060333","article-title":"Factors regulating the growth of metastasis cancer in bone","volume":"6","author":"Boyce","year":"1999","journal-title":"Endocr. Relat. Cancer"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nrc867","article-title":"Metastasis to bone: Causes, consequences and therapeutic opportunities","volume":"2","author":"Mundy","year":"2002","journal-title":"Nat. Rev. Cancer"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1056\/NEJMra030831","article-title":"Mechanism of bone metastasis","volume":"350","author":"Roodman","year":"2004","journal-title":"N. Engl. J. Med."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"3","DOI":"10.4161\/cbt.7.1.5163","article-title":"Biology of breast cancer bone metastasis","volume":"7","author":"Akhtari","year":"2008","journal-title":"Cancer Biol. Ther."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1053\/ctrv.2000.0210","article-title":"Metastatic bone disease: Clinical features, pathophysiology and treatment strategies","volume":"27","author":"Coleman","year":"2001","journal-title":"Cancer Treat. Rev."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1186\/bcr2781","article-title":"Breast cancer metastasis to the bone: Mechanisms of bone loss","volume":"12","author":"Chen","year":"2010","journal-title":"Breast Cancer Res."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature09495","article-title":"RANK ligand mediates progestin-induced mammary epithelial proliferation and carcinogenesis","volume":"468","author":"Jacob","year":"2010","journal-title":"Nature"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/nm1519","article-title":"NF-\u03baB in breast cancer cells promotes osteolytic bone metastasis by inducing osteoclastogenesis via GM-CSF","volume":"13","author":"Park","year":"2007","journal-title":"Nat. Med."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1038\/nrc3055","article-title":"Cancer to bone: A fatal attraction","volume":"11","author":"Weilbaecher","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1056\/NEJMra0901557","article-title":"Pancreatic cancer","volume":"362","author":"Hidalgo","year":"2010","journal-title":"N. Engl. J. Med."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1093\/carcin\/bgu097","article-title":"The complex landscape of pancreatic cancer metabolism","volume":"35","author":"Sousa","year":"2014","journal-title":"Carcinogenesis"},{"key":"ref_129","first-page":"13","article-title":"Recent advances in pancreatic cancer: Biology, treatment, and prevention","volume":"1856","author":"Singh","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.suc.2017.01.011","article-title":"A typical colorectal neoplasm","volume":"97","author":"Porter","year":"2017","journal-title":"Surg. Clin. N. Am."},{"key":"ref_131","unstructured":"American Cancer Society (2016). Cancer Facts & Figures 2016, American Cancer Society."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"7","DOI":"10.3322\/caac.21332","article-title":"Cancer statics, 2016","volume":"66","author":"Siegel","year":"2016","journal-title":"CA Cancer J. Clin."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1016\/S0140-6736(13)61649-9","article-title":"Colorectal cancer","volume":"383","author":"Brenner","year":"2014","journal-title":"Lancet"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1080\/14789450.2016.1233062","article-title":"Integrative analysis of the colorectal cancer proteome: Potential clinical impact","volume":"13","author":"Alnabulsi","year":"2016","journal-title":"Expert Rev. Proteom."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1038\/bjc.2017.135","article-title":"The differential expression of omega-3 and omega-6 fatty acid metabolizing enzymes in colorectal cancer and its prognostic significance","volume":"116","author":"Alnabulsi","year":"2017","journal-title":"Br. J. Cancer"},{"key":"ref_136","first-page":"4759","article-title":"Colorectal carcinogenesis: Role of oxidative stress and antioxidants","volume":"37","author":"Carini","year":"2017","journal-title":"Anticancer Res."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"16365","DOI":"10.3390\/ijms140816365","article-title":"Molecular pathways involved in colorectal cancer: Implications for disease behaviour and prevention","volume":"14","author":"Colussi","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"53959","DOI":"10.18632\/oncotarget.9796","article-title":"Important molecular genetic markers of colorectal cancer","volume":"7","author":"Kudryavtseva","year":"2016","journal-title":"Oncotarget"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1038\/bjc.2017.37","article-title":"Specific mutations in KRAS codon 12 is associated with worse overall survival in patients with advanced and recurrent colorectal cancer","volume":"116","author":"Jones","year":"2017","journal-title":"Br. J. Cancer"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/nrc969","article-title":"Targeting RAS signalling pathways in cancer therapy","volume":"3","author":"Downward","year":"2003","journal-title":"Nat. Rev. Cancer"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"6539","DOI":"10.1073\/pnas.1507228112","article-title":"MYC oncogene overexpression drives renal cell carcinoma in a mouse model through glutamine metabolism","volume":"112","author":"Shroff","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"69","DOI":"10.3322\/caac.20107","article-title":"Global cancer statistics","volume":"61","author":"Jemal","year":"2011","journal-title":"CA Cancer J. Clin."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"843","DOI":"10.3892\/ijmm.2016.2454","article-title":"Amygdalin blocks the in vitro adhesion and invasion\u2028of renal cell carcinoma cells by an integrin-dependent mechanism","volume":"37","author":"Juengel","year":"2016","journal-title":"Int. J. Mol. Med."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"4458","DOI":"10.1002\/jcp.26347","article-title":"The biological roles and clinical implications of microRNAs in clear cell renal cell carcinoma","volume":"233","author":"He","year":"2018","journal-title":"J. Cell. Physiol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"5938536","DOI":"10.1155\/2016\/5938536","article-title":"Paraneoplastic cough and renal cell carcinoma","volume":"2016","author":"Sullivan","year":"2016","journal-title":"Can. Respir. J."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1007\/s11864-003-0039-2","article-title":"Metastatic renal cell carcinoma","volume":"4","author":"Flanigan","year":"2003","journal-title":"Curr. Treat. Opin. Oncol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1016\/S0140-6736(15)00046-X","article-title":"Renal cancer","volume":"387","author":"Capitanio","year":"2016","journal-title":"Lancet"},{"key":"ref_148","first-page":"158","article-title":"Kidney cancer: Current progress in treatment","volume":"2","author":"Thakur","year":"2011","journal-title":"World J. Oncol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"9","DOI":"10.3322\/caac.21208","article-title":"Cancer statistics, 2014","volume":"64","author":"Siegel","year":"2014","journal-title":"CA Cancer J. Clin."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"30008","DOI":"10.18632\/oncotarget.15611","article-title":"OSR1 is a novel epigenetic silenced tumor suppressor regulating invasion and proliferation in renal cell carcinoma","volume":"8","author":"Zhang","year":"2017","journal-title":"Oncotarget"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1016\/S1470-2045(09)70240-2","article-title":"Resistance to targeted therapy in renal-cell carcinoma","volume":"10","author":"Rini","year":"2009","journal-title":"Lancet Oncol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1158\/1078-0432.CCR-09-2273","article-title":"New strategies in kidney cancer: Therapeutic advances through understanding the molecular basis of response and resistance","volume":"16","author":"Rini","year":"2010","journal-title":"Clin. Cancer Res."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"50023","DOI":"10.18632\/oncotarget.18483","article-title":"Cryptotanshinone inhibits proliferation yet induces apoptosis by suppressing STAT3 signals in renal cell carcinoma","volume":"8","author":"Chen","year":"2017","journal-title":"Oncotarget"},{"key":"ref_154","first-page":"1250131","article-title":"Cervical cancer: Prevention and treatment","volume":"14","author":"Denny","year":"2012","journal-title":"Dis. Med."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"394","DOI":"10.3322\/caac.21492","article-title":"Global cancer statics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries","volume":"68","author":"Bray","year":"2018","journal-title":"CA Cancer J. Clin."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1006\/gyno.2000.5826","article-title":"The rising incidence of adenocarcinoma relative to squamous cell carcinoma of the uterine cervix in the United States-a 24-year population-based study","volume":"78","author":"Smith","year":"2000","journal-title":"Gynecol. Oncol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.ygyno.2012.01.012","article-title":"Prognostic significance of adenocarcinoma histology in women with cervical cancer","volume":"125","author":"Garlic","year":"2012","journal-title":"Gynecol. Oncol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.ygyno.2005.10.004","article-title":"Ovarian metastasis in carcinoma of the uterine cervix","volume":"101","author":"Shimada","year":"2006","journal-title":"Gynecol. Oncol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.ijrobp.2010.02.009","article-title":"Long-term outcome and prognosis factors for adenocarcinoma\/adenosquamous carcinoma of the cervix after definitive radiotherapy","volume":"80","author":"Huang","year":"2011","journal-title":"Int. J. Radiat. Oncol. Biol. Phys."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.ygyno.2011.09.001","article-title":"Treatment outcome of concurrent weekly carboplatin with radiation therapy in locally advanced cervical cancer patients","volume":"123","author":"Katanyoo","year":"2011","journal-title":"Glynecol. Oncol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"205","DOI":"10.2174\/1568009611313020009","article-title":"Current and potential treatment for cervical cancer","volume":"13","author":"Yee","year":"2013","journal-title":"Curr. Cancer Drug Targets"},{"key":"ref_162","first-page":"609","article-title":"Exogenous regucalcin negatively regulates the progression of cervical adenocarcinoma","volume":"18","author":"Li","year":"2019","journal-title":"Oncol. Lett."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"402","DOI":"10.21037\/tcr.2019.02.01","article-title":"A mechanism of regucalcin knock-down in the promotion of proliferation and movement of human cervical cancer HeLa cells","volume":"8","author":"Li","year":"2019","journal-title":"Transl. Cancer Res."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"543","DOI":"10.2217\/fon.09.15","article-title":"Novel therapeutics for the treatment of metastatic melanoma","volume":"5","author":"Mansfield","year":"2009","journal-title":"Future Oncol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"6199","DOI":"10.1200\/JCO.2009.23.4799","article-title":"AJCC melanoma staging and classification","volume":"27","author":"Balch","year":"2009","journal-title":"J. Clin. Oncol."},{"key":"ref_166","doi-asserted-by":"crossref","unstructured":"Redpath, M., van Kempen, L., Robert, C., and Spatz, A. (2014). Molecular Testing in Cutaneous Melanoma Molecular Testing in Cancer, Springer.","DOI":"10.1007\/978-1-4899-8050-2_22"},{"key":"ref_167","first-page":"252","article-title":"Affinity proteomics exploration of melanoma identifies proteins in serum with assocuations","volume":"30","author":"Bystrom","year":"2017","journal-title":"Curr. Opin. Oncol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"e27227","DOI":"10.1002\/pbc.27227","article-title":"Immunotherapy for osteosarcoma: Where do we go from here?","volume":"65","author":"Wedekind","year":"2018","journal-title":"Pediatr. Blood Cancer"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1097\/CCO.0000000000000456","article-title":"Current question in bone sarcomas","volume":"30","author":"Strauss","year":"2018","journal-title":"Curr. Opin. Oncol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.jncc.2024.09.001","article-title":"Osteoimmunology in bone malignancies: A symphony with evil","volume":"4","author":"Song","year":"2024","journal-title":"J. Natl. Cancer Center"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1002\/ijc.24320","article-title":"International osteosarcoma incidence patterns in children and adolescents, middle ages and elderly persons","volume":"125","author":"Mirabello","year":"2009","journal-title":"Int. J. Cancer"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"E508","DOI":"10.1002\/ijc.26426","article-title":"Incidence and survival of malignant bone sarcomas in England 1979\u20132007","volume":"131","author":"Whelan","year":"2012","journal-title":"Int. J. Cancer"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"1706","DOI":"10.1200\/JCO.2004.08.043","article-title":"Laboratory and clinical evidence of synergistic cytotoxicity of sequential treatment with gemcitabine followed by docetaxel in the treatment of sarcoma","volume":"22","author":"Leu","year":"2004","journal-title":"J. Clin. Oncol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.ctrv.2013.11.006","article-title":"Osteosarcoma treatment-where do we stand? A state of the art review","volume":"40","author":"Luetke","year":"2014","journal-title":"Cancer Treat. Rev."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"3312","DOI":"10.1128\/MCB.05318-11","article-title":"The RPB2 flap loop of human RNA polymerase II is dispensable for transcription initiation and elongation","volume":"31","author":"Palangat","year":"2011","journal-title":"Mol. Cell. Biol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"10825","DOI":"10.3748\/wjg.v20.i31.10825","article-title":"Novel therapeutic targets for pancreatic cancer","volume":"20","author":"Tang","year":"2014","journal-title":"World J. Gastroenterol."},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Altamura, C., Greco, M.R., Carrratu, M.R., Cardone, R.A., and Desaphy, J.-F. (2021). Emerging roles for ion channels in ovarian cancer: Pathomechanisms and pharmacological treatment. Cancers, 13.","DOI":"10.3390\/cancers13040668"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"280","DOI":"10.3322\/caac.21559","article-title":"Epithelial ovarian cancer: Evolution of management in the era of precision medicine","volume":"69","author":"Lheureux","year":"2019","journal-title":"CA Cancer J. Clin."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/j.fertnstert.2015.08.006","article-title":"Endometriosis and ovarian cancer: Potential benefits and harmas of screening and risk-reducing surgery","volume":"104","author":"Guo","year":"2015","journal-title":"Fertil. Steril."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.bpobgyn.2016.08.006","article-title":"Epidemiology of epithelial ovarian cancer","volume":"41","author":"Webb","year":"2017","journal-title":"Best Pract. Res. Clin. Obs. Gynaeccol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"243","DOI":"10.3892\/etm.2021.9674","article-title":"Ovarian endometriosis, a precursor of ovarian cancer: Histological aspects, gene expression and microRNA alterations (Review)","volume":"21","author":"Braicu","year":"2021","journal-title":"Exp. Therpeutic Med."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Alshamrani, A.A. (2020). Roles of microRNAs in ovarian cancer tumorigenesis: Two decades later, what have we learned?. Front. Oncol., 10.","DOI":"10.3389\/fonc.2020.01084"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ajpath.2020.09.006","article-title":"The origin of ovarian cancer species and precancerous landscape","volume":"191","author":"Shih","year":"2021","journal-title":"Am. J. Pathol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.soncn.2019.02.001","article-title":"Ovarian cancer: An integrated review","volume":"35","author":"Stewart","year":"2019","journal-title":"Semin. Oncol. Nurs."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1038\/ncomms3126","article-title":"Evaluating cell lines as tumor models by comparison of genomic profiles","volume":"4","author":"Domcke","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Michalak, M., Lach, M.S., Antoszczak, M., Huczynski, A., and Suchorska, W.M. (2020). Overcoming resistant to platinum-based drugs in ovarian cancer by adryamycin and its derivatives\u2014An in vitro study. Molecules, 25.","DOI":"10.3390\/molecules25030537"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/BF00925738","article-title":"Tissue concentration of calcium-binding protein regucalcin in rats by enzyme-linked immunoadsorbent assay","volume":"122","author":"Yamaguchi","year":"1993","journal-title":"Mol. Cell. Biochem."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1023\/A:1006859121897","article-title":"Potential sensitivity of hepatic specific protein regucalcin as a marker of chronic liver injury","volume":"167","author":"Yamaguchi","year":"1997","journal-title":"Mol. Cell. Biochem."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"2457","DOI":"10.1002\/pmic.200800692","article-title":"The secreted salivary proteome of the pea aphid Acyrthosiphon pisum charecterised by mass spectrometry","volume":"9","author":"Carolan","year":"2009","journal-title":"Proteomics"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Stafford-Banks, C.A., Rotenberg, D., Johnson, B.R., Whitfield, A.E., and Ullman, D.E. (2014). Analysis of the salivary gland transcriptome of Frankliniella occidentails. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0094447"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"3532","DOI":"10.1248\/cpb.36.3532","article-title":"Calcium-binding protein regucalcin is an activator (Ca2+-Mg2+)-adenosine triphosphatase in the plasma membranes of rat liver","volume":"36","author":"Yamaguchi","year":"1988","journal-title":"Chem. Pharm. Bull."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"2383","DOI":"10.7314\/APJCP.2013.14.4.2383","article-title":"Soluble expression of recombinant human SMP30 for detecting serum SMP30 antibody levels in hepatocellular carcinoma patients","volume":"14","author":"Zhang","year":"2013","journal-title":"Asian Pac. J. Cancer Prev."},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Wei, X., Yu, H., Zhao, P., Xie, L., Li, L., and Zhang, J. (2019). Serum regucalcin is a useful indicator of liver injury severity in patients with hepatitis B virus-related liver diseases. Braz. J. Med. Biol. Res., 52.","DOI":"10.1590\/1414-431x20198845"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"25510","DOI":"10.1074\/jbc.273.39.25510","article-title":"HBx protein of hepatitis B virus activates Jak1-STAT signaling","volume":"273","author":"Lee","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_195","first-page":"373","article-title":"The transcriptional function of the hepatitis B virus X protein and its role in hepatocarcinogenesis (Review)","volume":"15","author":"Andrisani","year":"1999","journal-title":"Int. J. Oncol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"10350","DOI":"10.1073\/pnas.91.22.10350","article-title":"Hepatitis B virus HBx protein activates Ras-GTP complex formation and establishes a Ras, Raf, MAP kinase signaling cascade","volume":"91","author":"Benn","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1002\/hep.20245","article-title":"Hepatitis B virus X protein is essential for the activation of Wnt\/beta-catenin signaling in hepatoma cells","volume":"39","author":"Cha","year":"2004","journal-title":"Hepatology"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1002\/cbin.11670","article-title":"Targeting molecular signal transduction pathway in hepatocellular carcinoma and its implications for cancer therapy","volume":"45","author":"Mir","year":"2021","journal-title":"Cell Biol. Int."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.clinbiochem.2010.10.008","article-title":"Serum immunoreactivity of SMP30 and its tissues expression in hepatocellular carcinoma","volume":"44","author":"Zhou","year":"2011","journal-title":"Clin. Biochem."},{"key":"ref_200","first-page":"2924","article-title":"Exogenous regucalcin suppresses the growth of human liver cancer HepG2 cells in vitro","volume":"39","author":"Yamaguchi","year":"2018","journal-title":"Oncol. Rep."},{"key":"ref_201","first-page":"894","article-title":"Pancreatic cancer stem cells","volume":"5","author":"Zhu","year":"2015","journal-title":"Am. J. Cancer Res."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/j.ctrv.2014.07.003","article-title":"Progress in the knowledge and treatment of advanced pancreatic cancer: From bench side to bedside","volume":"40","author":"Oettle","year":"2014","journal-title":"Cancer Treat. Rev."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1038\/cgt.2013.83","article-title":"The challenge of pancreatic cancer therapy and novel treatment strategy using engineered mesenchymal stem cells","volume":"21","author":"Moniri","year":"2014","journal-title":"Cancer Gene Ther."},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"McCarroll, J.A., Naim, S., Sharbeen, G., Russia, N., Lee, J., Kavallaris, M., Goldstein, D., and Phillips, P.A. (2014). Role of pancreatic stellate cells in chemoresistance in pancreatic cancer. Front. Physiol., 5.","DOI":"10.3389\/fphys.2014.00141"},{"key":"ref_205","doi-asserted-by":"crossref","unstructured":"Collins, M.A., and di Magliano, M.P. (2014). K-ras as a key oncogene and therapeutic target in pancreatic cancer. Front. Physiol., 4.","DOI":"10.3389\/fphys.2013.00407"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/0092-8674(88)90571-5","article-title":"Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes","volume":"53","author":"Almoguuera","year":"1988","journal-title":"Cell"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1038\/nrc3106","article-title":"RAS oncogenes: Weaving a tumorigenic web","volume":"11","author":"Grabocka","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.3892\/ijmm.2015.2164","article-title":"Suppressive effects of exogenous regucalcin on cell proliferation in human pancreatic cancer MiaPaCa-2 cells in vitro","volume":"35","author":"Yamaguchi","year":"2015","journal-title":"Int. J. Mol. Med."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"7801","DOI":"10.3892\/mmr.2015.4352","article-title":"Exogenous regucalcin suppresses cell proliferation human breast cancer MDA-MB-231-bone metastatic cells in vitro","volume":"12","author":"Yamaguchi","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"4049","DOI":"10.1245\/s10434-014-4010-1","article-title":"A promise to our patients with metastasis bone disease","volume":"21","author":"Randall","year":"2014","journal-title":"Ann. Surg. Oncol."},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Ardura, J.A., Alvarez-Carrion, L., Cutierrrez-Rojas, I., and Alonso, V. (2020). Role of calcium signaling in prostate cancer progression: Effects on cancer hallmarks and bone metastatic mechanisms. Cancers, 12.","DOI":"10.3390\/cancers12051071"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1210\/js.2018-00425","article-title":"Mechanisms of osteoblastic bone metastasis in prostate cancer: Role of prostatic acid phosphatase","volume":"3","author":"Izadmehr","year":"2019","journal-title":"J. Endocr. Soc."},{"key":"ref_213","doi-asserted-by":"crossref","unstructured":"Malinowaski, B., Wicinski, M., Musiala, N., Osowska, H., and Previous, S.M. (2019). Current, and future pharmacotherapy and diagnosis of prostate cancer-A comprehensive review. Diagnostics, 9.","DOI":"10.3390\/diagnostics9040161"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.ajur.2019.02.002","article-title":"Systemic treatment for metastatic prostate cancer","volume":"6","author":"Gravis","year":"2019","journal-title":"Asian J. Urol."},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Zustovich, F., and Barsantiu, R. (2018). Targeted \u03b1 therapies for the treatment of bone metastases. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19010074"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"4861570","DOI":"10.1155\/2017\/4861570","article-title":"Immunotherapy as a promising treatment for prostate cancer: A systemic review","volume":"2017","author":"Janiczek","year":"2017","journal-title":"J. Immunol. Res."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1159\/000524303","article-title":"Extracellular regucalcin suppresses the growth, migration, invasion and adhesion of metastatic human prostate cancer cells","volume":"100","author":"Yamaguchi","year":"2022","journal-title":"Oncology"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/S0733-8619(18)31009-0","article-title":"Growth factors and oncogenes in human malignant glioma","volume":"3","author":"Westermark","year":"1985","journal-title":"Neurol. Clin."},{"key":"ref_219","first-page":"43","article-title":"Genetic alterations associated with glioma progression","volume":"78","author":"Kleihues","year":"1994","journal-title":"Verh. Dtsch. Ges. Pathol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1007\/978-3-030-48457-6_7","article-title":"The role of BEHAB\/Brevican in the tumor microenvironment: Mediating glioma cell invasion and motility","volume":"1272","author":"Giamanco","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/15321819.2017.1411816","article-title":"Current and emerging EGFR therapies for glioblastoma","volume":"39","author":"Artene","year":"2018","journal-title":"J. Immunoass. Immunochem."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1002\/jnr.23687","article-title":"Implications of mitogen-activated protein kinase signaling in glioma","volume":"94","author":"Pandey","year":"2016","journal-title":"J. Neurosci. Res."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.ejphar.2009.10.010","article-title":"EGF receptor inhibitors in the treatment of glioblastoma multiform: Old clinical allies and newly emerging theeraprutic concepts","volume":"625","author":"Gadi","year":"2009","journal-title":"Eur. J. Pharmacol."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1586\/erv.11.177","article-title":"Targeting EGF receptor variant III: Tumor-specific peptide vaccination for malignant gliomas","volume":"11","author":"Vecchio","year":"2012","journal-title":"Expert Rev. Vaccines"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1002\/glia.440150312","article-title":"Molecular pathways in the formation of gliomas","volume":"15","author":"Louis","year":"1995","journal-title":"Glia"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1016\/0006-2952(68)90092-0","article-title":"Effect of partial hepatectomy on the responsiveness of microsomal enzymes and cytochrome P-450 to phenobarbital or 3-methylcholanthrene","volume":"17","author":"Gran","year":"1968","journal-title":"Biochem. Pharmacol."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/BF00935586","article-title":"Expression of hepatic calcium-binding protein regucalcin mRNA is decreased by phenobarbital administration in rats","volume":"141","author":"Isogai","year":"1994","journal-title":"Mol. Cell. Biochem."},{"key":"ref_228","first-page":"203","article-title":"Diagnostic value of serum SMP30 and anti-SMP30 antibody in hepatocellular carcinoma","volume":"49","author":"Zheng","year":"2018","journal-title":"Lab. Med."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/BF00926884","article-title":"Expression of calcium-binding protein regucalcin in the kidney cortex of rats: The stimulation by calcium administration","volume":"146","author":"Yamaguchi","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.3892\/ijmm.2015.2343","article-title":"The potential role of regucalcin in kidney cell regulation: Involvement in renal failure (Review)","volume":"36","author":"Yamaguchi","year":"2015","journal-title":"Int. Mol. Med."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1023\/A:1006821928397","article-title":"Alterations in Ca2+-ATPase activity and calcium- binding protein regucalcin mRNA expression in the kidney cortex of rats with saline ingestion","volume":"170","author":"Shinya","year":"1997","journal-title":"Mol. Cell. Biochem."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1023\/A:1006898910955","article-title":"Stimulatory effect of calcium administration on regucalcin mRNA expression is attenuated in the kidney cortex of rats with saline ingestion","volume":"178","author":"Shinya","year":"1998","journal-title":"Mol. Cell. Biochem."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/0006-2952(86)90527-7","article-title":"Mechanism of S-(1,2 dichlorovinyl) glutathione induced nephrotoxicity","volume":"35","author":"Elfarra","year":"1986","journal-title":"Biochem. Pharmacol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/0006-2952(89)90233-5","article-title":"Oxidative and mitochondrial toxic effects of cephalosporine antibiotics in the kidney. A comparative study of cephaloridine and cephaloglycin","volume":"38","author":"Tune","year":"1989","journal-title":"Biochem. Pharmacol."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1016\/0006-2952(90)90121-Z","article-title":"Role of endogenous sulfur-containing nucleotides in an in vitro model of cis-diamminechloro platinum (II)-induced nephrotoxicity","volume":"39","author":"Montine","year":"1990","journal-title":"Biochem. Pharmacol."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0041-008X(86)90303-0","article-title":"Biochemical mechanism of cephaloridine nephrotoxicity: Time and concentration dependence of peroxidative injury","volume":"83","author":"Goldstein","year":"1986","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/BF01076896","article-title":"Suppressed expression of calcium-binding protein regucalcin mRNA in the renal cortex of rats with chemically induced kidney damage","volume":"151","author":"Kurota","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.taap.2008.02.018","article-title":"Gene expression changes induced by ochratoxin A in renal and hepatic tissues of male F344 rat after oral repeated administration","volume":"230","author":"Arbillaga","year":"2008","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"3431","DOI":"10.1007\/s00216-010-4463-4","article-title":"Proteomics investigation on aristolochic acid nephropathy: A case study on rat kidney tissues","volume":"399","author":"Wu","year":"2011","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.trsl.2015.05.007","article-title":"Kidney tissue proteomics reveals regucalcin downregulation in response to diabetic nephropathy with reflection in urinary exosomes","volume":"166","author":"Zubiri","year":"2015","journal-title":"Transl. Res."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"28","DOI":"10.3892\/ijo.2024.5616","article-title":"Exosome as a crucial communicator between tumor microenvironment and gastric cancer (Review)","volume":"64","author":"Wang","year":"2024","journal-title":"Int. J. Oncol."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1023\/A:1006928402184","article-title":"Expression of calcium-binding protein regucalcin and microsomal Ca2+-ATPase regulation in rat brain: Attenuation with increasing age","volume":"200","author":"Yamaguchi","year":"1999","journal-title":"Mol. Cell. Biochem."},{"key":"ref_243","first-page":"825","article-title":"Role of regucalcin in brain calcium signalling: Involving aging","volume":"4","author":"Yamaguchi","year":"2012","journal-title":"Int. Biol."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1111\/j.1750-3639.2011.00540.x","article-title":"The proteome of the locus ceruleus in Parkinson\u2019s disease: Relevance to pathogenesis","volume":"22","author":"Berendes","year":"2012","journal-title":"Brain Pathol."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.ijdevneu.2012.01.011","article-title":"Proteomic analysis of plasma from a Tau transgenic mouse","volume":"30","author":"Kim","year":"2012","journal-title":"Int. J. Dev. Neurosci."}],"container-title":["Cancers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6694\/17\/2\/240\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T10:27:51Z","timestamp":1759919271000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6694\/17\/2\/240"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,13]]},"references-count":245,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2025,1]]}},"alternative-id":["cancers17020240"],"URL":"https:\/\/doi.org\/10.3390\/cancers17020240","relation":{},"ISSN":["2072-6694"],"issn-type":[{"value":"2072-6694","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,13]]}}}