{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T19:21:44Z","timestamp":1790709704762,"version":"4.1.0"},"reference-count":189,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,5,30]],"date-time":"2023-05-30T00:00:00Z","timestamp":1685404800000},"content-version":"am","delay-in-days":180,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001677","name":"Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001677","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007526","name":"Universit\u00e9 Fran\u00e7ois-Rabelais","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007526","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012948","name":"Minist\u00e8re de l'Enseignement sup\u00e9rieur, de la Recherche et de l'Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012948","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009469","name":"Conseil R\u00e9gional du Centre-Val de Loire","doi-asserted-by":"publisher","award":["2019\u201300134916"],"award-info":[{"award-number":["2019\u201300134916"]}],"id":[{"id":"10.13039\/501100009469","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Aspects of Medicine"],"published-print":{"date-parts":[[2022,12]]},"DOI":"10.1016\/j.mam.2022.101086","type":"journal-article","created":{"date-parts":[[2022,3,16]],"date-time":"2022-03-16T17:16:11Z","timestamp":1647450971000},"page":"101086","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":56,"special_numbering":"C","title":["Cathepsin V: Molecular characteristics and significance in health and disease"],"prefix":"10.1016","volume":"88","author":[{"given":"Fabien","family":"Lecaille","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thibault","family":"Chazeirat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahlame","family":"Saidi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8562-4821","authenticated-orcid":false,"given":"Gilles","family":"Lalmanach","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mam.2022.101086_bib1","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/0076-6879(94)44051-4","article-title":"Cystatins","volume":"244","author":"Abrahamson","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.mam.2022.101086_bib2","first-page":"179","author":"Abrahamson","year":"2003","journal-title":"Cystatins. Biochem. Soc."},{"key":"10.1016\/j.mam.2022.101086_bib3","first-page":"1789","article-title":"Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium","volume":"39","author":"Adachi","year":"1998","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib4","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1002\/prca.201300105","article-title":"Cathepsin B: multiple roles in cancer","volume":"8","author":"Aggarwal","year":"2014","journal-title":"Proteonomics Clin. Appl."},{"key":"10.1016\/j.mam.2022.101086_bib5","doi-asserted-by":"crossref","first-page":"9140","DOI":"10.3390\/ijms21239140","article-title":"Procathepsin V is secreted in a TSH regulated manner from human thyroid epithelial cells and is accessible to an activity-based probe","volume":"21","author":"Al-Hashimi","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib6","doi-asserted-by":"crossref","first-page":"118846","DOI":"10.1016\/j.bbamcr.2020.118846","article-title":"Significance of nuclear cathepsin V in normal thyroid epithelial and carcinoma cells","volume":"1867","author":"Al-Hashimi","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"10.1016\/j.mam.2022.101086_bib7","doi-asserted-by":"crossref","first-page":"9682","DOI":"10.1038\/s41598-019-45918-1","article-title":"Elastolytic activity of cysteine cathepsins K, S, and V promotes vascular calcification","volume":"9","author":"Andrault","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mam.2022.101086_bib8","first-page":"4896","article-title":"Inhibition of experimental metastasis by an alpha-glucosidase inhibitor, 1,6-epi-cyclophellitol","volume":"53","author":"Atsumi","year":"1993","journal-title":"Cancer Res."},{"key":"10.1016\/j.mam.2022.101086_bib9","doi-asserted-by":"crossref","first-page":"6664","DOI":"10.1073\/pnas.1131604100","article-title":"Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs","volume":"100","author":"Bania","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.mam.2022.101086_bib10","first-page":"1363","article-title":"The cystatins: a diverse superfamily of cysteine peptidase inhibitors","volume":"45","author":"Barrett","year":"1986","journal-title":"Biomed. Biochim. Acta"},{"key":"10.1016\/j.mam.2022.101086_bib11","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1046\/j.1523-1747.2003.12086.x","article-title":"Analysis of proteins with caseinolytic activity in a human stratum corneum extract revealed a yet unidentified cysteine protease and identified the so-called \u201cStratum corneum thiol protease\u201d as cathepsin L2","volume":"120","author":"Bernard","year":"2003","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mam.2022.101086_bib12","doi-asserted-by":"crossref","first-page":"4622","DOI":"10.1016\/j.bmcl.2009.06.090","article-title":"Design of selective cathepsin inhibitors","volume":"19","author":"Bethel","year":"2009","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.mam.2022.101086_bib13","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1159\/000030123","article-title":"N-Glycans influence the in vitro adhesive and invasive behaviour of three metastatic cell lines","volume":"21","author":"Bironaite","year":"2000","journal-title":"Tumour Biol"},{"key":"10.1016\/j.mam.2022.101086_bib14","doi-asserted-by":"crossref","first-page":"108153","DOI":"10.1016\/j.jmgm.2022.108153","article-title":"In silico and in vitro mapping of specificity patterns of glycosaminoglycans towards cysteine cathepsins B, L, K, S and V","author":"Bojarski","year":"2022","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.mam.2022.101086_bib15","doi-asserted-by":"crossref","first-page":"5222","DOI":"10.1074\/jbc.M003642200","article-title":"Conformational dependence of collagenase (Matrix Metalloproteinase-1) up-regulation by elastin peptides in cultured fibroblasts","volume":"276","author":"Brassart","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib16","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1023\/A:1006550503612","article-title":"Regulation of matrix metalloproteinase-2 (gelatinase A, MMP-2), membrane-type matrix metalloproteinase-1 (MT1-MMP) and tissue inhibitor of metalloproteinases-2 (TIMP-2) expression by elastin-derived peptides in human HT-1080 fibrosarcoma cell line","volume":"16","author":"Brassart","year":"1998","journal-title":"Clin. Exp. Metastasis"},{"key":"10.1016\/j.mam.2022.101086_bib17","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.biochi.2007.07.024","article-title":"Cysteine cathepsins: cellular roadmap to different functions","volume":"90","author":"Brix","year":"2008","journal-title":"Biochimie"},{"key":"10.1016\/j.mam.2022.101086_bib18","series-title":"Proteases: Structure and Function","first-page":"85","article-title":"Compartmentalization of proteolysis","author":"Brix","year":"2013"},{"key":"10.1016\/j.mam.2022.101086_bib190","article-title":"Papain-like cysteine proteases","author":"Br\u00f6mme","year":"2001","journal-title":"Curr. Protoc. Protein Sci."},{"key":"10.1016\/j.mam.2022.101086_bib20","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1517\/13543780902832661","article-title":"Cathepsin K inhibitors for osteoporosis and potential off-target effects","volume":"18","author":"Br\u00f6mme","year":"2009","journal-title":"Expet Opin. Invest. Drugs"},{"key":"10.1016\/j.mam.2022.101086_bib21","doi-asserted-by":"crossref","first-page":"2377","DOI":"10.1021\/bi982175f","article-title":"Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization","volume":"38","author":"Br\u00f6mme","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.mam.2022.101086_bib22","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/S0014-4835(03)00148-9","article-title":"Involvement of corneal nerves in the progression of keratoconus","volume":"77","author":"Brookes","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.mam.2022.101086_bib23","doi-asserted-by":"crossref","first-page":"20104","DOI":"10.1074\/jbc.M001392200","article-title":"Clitocypin, a new type of cysteine proteinase inhibitor from fruit bodies of mushroom Clitocybe nebularis","volume":"275","author":"Brzin","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib24","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1515\/BC.2007.053","article-title":"Inhibition of cathepsin L-like proteases by cathepsin V propeptide","volume":"388","author":"Burden","year":"2007","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib25","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1111\/j.1399-3011.1997.tb01156.x","article-title":"Structure-activity relationships for some elastin-derived peptide chemoattractants","volume":"49","author":"Castiglione Morelli","year":"1997","journal-title":"J. Pept. Res."},{"key":"10.1016\/j.mam.2022.101086_bib26","doi-asserted-by":"crossref","first-page":"117261","DOI":"10.1016\/j.carbpol.2020.117261","article-title":"The abnormal accumulation of heparan sulfate in patients with mucopolysaccharidosis prevents the elastolytic activity of cathepsin V","volume":"253","author":"Chazeirat","year":"2021","journal-title":"Carbohydr. Polym."},{"key":"10.1016\/j.mam.2022.101086_bib27","doi-asserted-by":"crossref","first-page":"2345","DOI":"10.1038\/sj.jid.5700409","article-title":"Cathepsin L2 levels inversely correlate with skin color","volume":"126","author":"Chen","year":"2006","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mam.2022.101086_bib28","doi-asserted-by":"crossref","first-page":"15893","DOI":"10.1074\/jbc.M600694200","article-title":"Cystatin M\/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site","volume":"281","author":"Cheng","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib29","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1111\/j.1365-2133.2009.09156.x","article-title":"The cystatin M\/E-controlled pathway of skin barrier formation: expression of its key components in psoriasis and atopic dermatitis","volume":"161","author":"Cheng","year":"2009","journal-title":"Br. J. Dermatol."},{"key":"10.1016\/j.mam.2022.101086_bib30","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1038\/nature09531","article-title":"A genome-wide RNAi screen reveals determinants of human embryonic stem cell identity","volume":"468","author":"Chia","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.mam.2022.101086_bib31","doi-asserted-by":"crossref","first-page":"12824","DOI":"10.1074\/jbc.M513331200","article-title":"Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities","volume":"281","author":"Choe","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib32","doi-asserted-by":"crossref","first-page":"5321","DOI":"10.1021\/jm020238t","article-title":"Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides","volume":"45","author":"Chowdhury","year":"2002","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib33","doi-asserted-by":"crossref","first-page":"3205","DOI":"10.1158\/1078-0432.CCR-09-3331","article-title":"Molecular imaging of N-linked glycosylation suggests glycan biosynthesis is a novel target for cancer therapy","volume":"16","author":"Contessa","year":"2010","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.mam.2022.101086_bib34","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1016\/j.bcp.2008.07.041","article-title":"Cathepsins: key modulators of cell death and inflammatory responses","volume":"76","author":"Conus","year":"2008","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.mam.2022.101086_bib35","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1515\/bc.2010.049","article-title":"Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor","volume":"391","author":"Coppini","year":"2010","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib36","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.exer.2015.03.012","article-title":"Corneal angiogenesis modulation by cysteine cathepsins: in vitro and in vivo studies","volume":"134","author":"Coppini","year":"2015","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.mam.2022.101086_bib37","doi-asserted-by":"crossref","first-page":"5492","DOI":"10.1002\/j.1460-2075.1996.tb00934.x","article-title":"Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment","volume":"15","author":"Coulombe","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.mam.2022.101086_bib38","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1186\/s12879-019-4463-8","article-title":"Exploring Leishmania infantum cathepsin as a new molecular marker for phylogenetic relationships and visceral leishmaniasis diagnosis","volume":"19","author":"da Silva","year":"2019","journal-title":"BMC Infect. Dis."},{"key":"10.1016\/j.mam.2022.101086_bib39","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1161\/01.ATV.0000168412.50855.9f","article-title":"Elastin-derived peptides induce a T-helper type 1 polarization of human blood lymphocytes","volume":"25","author":"Debret","year":"2005","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.mam.2022.101086_bib40","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1038\/onc.2009.466","article-title":"Deficiency for the cysteine protease cathepsin L promotes tumor progression in mouse epidermis","volume":"29","author":"Dennem\u00e4rker","year":"2010","journal-title":"Oncogene"},{"key":"10.1016\/j.mam.2022.101086_bib41","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1046\/j.1432-1033.2003.03382.x","article-title":"Kininogen-derived peptides for investigating the putative vasoactive properties of human cathepsins K and L","volume":"270","author":"Desmazes","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.mam.2022.101086_bib42","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1515\/bchm.2001.382.5.811","article-title":"Cathepsin L, but not cathepsin B, is a potential kininogenase","volume":"382","author":"Desmazes","year":"2001","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib43","doi-asserted-by":"crossref","first-page":"34871","DOI":"10.1074\/jbc.M113.510008","article-title":"Elastin degradation by cathepsin V requires two exosites","volume":"288","author":"Du","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib44","doi-asserted-by":"crossref","first-page":"6623","DOI":"10.1158\/0008-5472.CAN-08-0463","article-title":"Sensitization to the lysosomal cell death pathway by oncogene-induced down-regulation of lysosome-associated membrane proteins 1 and 2","volume":"68","author":"Fehrenbacher","year":"2008","journal-title":"Cancer Res."},{"key":"10.1016\/j.mam.2022.101086_bib45","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1093\/emboj\/19.6.1187","article-title":"Secreted cathepsin L generates endostatin from collagen XVIII","volume":"19","author":"Felbor","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.mam.2022.101086_bib46","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1001\/jama.2016.19043","article-title":"Global burden of hypertension and systolic blood pressure of at least 110 to 115 mm Hg, 1990-2015","volume":"317","author":"Forouzanfar","year":"2017","journal-title":"JAMA"},{"key":"10.1016\/j.mam.2022.101086_bib47","doi-asserted-by":"crossref","first-page":"15232","DOI":"10.1074\/jbc.M111.310607","article-title":"Human cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters","volume":"287","author":"Funkelstein","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib48","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.exer.2003.09.005","article-title":"Anti-angiogenic role of angiostatin during corneal wound healing","volume":"78","author":"Gabison","year":"2004","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.mam.2022.101086_bib49","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1042\/BJ20040864","article-title":"Cathepsin K: a cysteine protease with unique kinin-degrading properties","volume":"383","author":"Godat","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.mam.2022.101086_bib50","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/0014-5793(92)80339-I","article-title":"Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L","volume":"297","author":"Goretzki","year":"1992","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mam.2022.101086_bib51","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0021-9258(18)64818-5","article-title":"Purification and properties of beef spleen cathepsin B","volume":"226","author":"Greenbaum","year":"1957","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib52","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1513\/pats.200606-130MS","article-title":"State of the art. Role of CD4+ T cells in sarcoidosis","volume":"4","author":"Grunewald","year":"2007","journal-title":"Proc. Am. Thorac. Soc."},{"key":"10.1016\/j.mam.2022.101086_bib53","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1078\/0171-9335-00404","article-title":"The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles","volume":"83","author":"Hagemann","year":"2004","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.mam.2022.101086_bib54","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1038\/sj.jid.5700157","article-title":"Genomic analysis defines a cancer-specific gene expression signature for human squamous cell carcinoma and distinguishes malignant hyperproliferation from benign hyperplasia","volume":"126","author":"Haider","year":"2006","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mam.2022.101086_bib55","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1067\/mva.2002.120382","article-title":"Monocyte chemotactic activity in human abdominal aortic aneurysms: role of elastin degradation peptides and the 67-kD cell surface elastin receptor","volume":"35","author":"Hance","year":"2002","journal-title":"J. Vasc. Surg."},{"key":"10.1016\/j.mam.2022.101086_bib56","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0200374","article-title":"Crystal structures of human procathepsin H","volume":"13","author":"Hao","year":"2018","journal-title":"PLoS One"},{"key":"10.1016\/j.mam.2022.101086_bib57","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1080\/10409238.2020.1768208","article-title":"Elastases and elastokines: elastin degradation and its significance in health and disease","volume":"55","author":"Heinz","year":"2020","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.mam.2022.101086_bib58","doi-asserted-by":"crossref","first-page":"1495","DOI":"10.1093\/eurheartj\/ehi706","article-title":"Possible role for mast cell-derived cathepsin G in the adverse remodelling of stenotic aortic valves","volume":"27","author":"Helske","year":"2006","journal-title":"Eur. Heart J."},{"key":"10.1016\/j.mam.2022.101086_bib59","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.bbrc.2018.04.070","article-title":"Melanosome degradation in epidermal keratinocytes related to lysosomal protease cathepsin V","volume":"500","author":"Homma","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mam.2022.101086_bib60","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.biocel.2017.05.020","article-title":"Exogenous cathepsin V protein protects human cardiomyocytes HCM from angiotensin \u2161-Induced hypertrophy","volume":"89","author":"Huang","year":"2017","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.mam.2022.101086_bib61","doi-asserted-by":"crossref","first-page":"13192","DOI":"10.1074\/jbc.M108460200","article-title":"Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation","volume":"277","author":"Irving","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib62","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1093\/dnares\/6.2.137","article-title":"Genomic organization and chromosomal localization of the human cathepsin L2 gene","volume":"6","author":"Itoh","year":"1999","journal-title":"DNA Res."},{"key":"10.1016\/j.mam.2022.101086_bib63","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.3389\/fimmu.2019.02037","article-title":"Cysteine cathepsins in tumor-associated immune cells","volume":"10","author":"Jako\u0161","year":"2019","journal-title":"Front. Immunol."},{"key":"10.1016\/j.mam.2022.101086_bib64","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/bj3610173","article-title":"Characterization of human cathepsin L promoter and identification of binding sites for NF-Y, Sp1 and Sp3 that are essential for its activity","volume":"361","author":"Jean","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.mam.2022.101086_bib65","doi-asserted-by":"crossref","first-page":"1474","DOI":"10.1038\/sj.onc.1209196","article-title":"Expression of cathepsin L in human tumor cells is under the control of distinct regulatory mechanisms","volume":"25","author":"Jean","year":"2006","journal-title":"Oncogene"},{"issue":"8","key":"10.1016\/j.mam.2022.101086_bib66","first-page":"4035","article-title":"Elevated CTSL2 expression is associated with an adverse prognosis in hepatocellular carcinoma","volume":"11","author":"Jing","year":"2018","journal-title":"Int. J. Clin. Exp. Pathol."},{"key":"10.1016\/j.mam.2022.101086_bib67","doi-asserted-by":"crossref","first-page":"273","DOI":"10.3109\/15419069509081013","article-title":"Growth stimulation of human skin fibroblasts by elastin-derived peptides","volume":"3","author":"Kamoun","year":"1995","journal-title":"Cell Adhes. Commun."},{"key":"10.1016\/j.mam.2022.101086_bib68","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1110\/ps.062401806","article-title":"The crystal structure of a Cys25 \u2192 Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions","volume":"15","author":"Kaulmann","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.mam.2022.101086_bib69","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/s11010-012-1320-0","article-title":"Tumor necrosis factor alpha stimulates cathepsin K and V activity via juxtacrine monocyte-endothelial cell signaling and JNK activation","volume":"367","author":"Keegan","year":"2012","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.mam.2022.101086_bib70","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1167\/iovs.04-0549","article-title":"Increased levels of catalase and cathepsin V\/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder","volume":"46","author":"Kenney","year":"2005","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib71","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1111\/febs.13980","article-title":"Inherited diseases caused by mutations in cathepsin protease genes","volume":"284","author":"Ketterer","year":"2017","journal-title":"FEBS J."},{"key":"10.1016\/j.mam.2022.101086_bib72","series-title":"Novartis Foundation Symposia","first-page":"15","article-title":"Lysosomal cysteine proteinases","author":"Kirschke","year":"1979"},{"key":"10.1016\/j.mam.2022.101086_bib73","doi-asserted-by":"crossref","first-page":"32810","DOI":"10.1074\/jbc.M111.221804","article-title":"Classical and neonatal Marfan Syndrome mutations in fibrillin-1 cause differential protease susceptibilities and protein function","volume":"286","author":"Kirschner","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib74","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.humpath.2016.09.027","article-title":"Expression of cathepsins V and S in thymic epithelial tumors","volume":"60","author":"Kiuchi","year":"2017","journal-title":"Hum. Pathol."},{"key":"10.1016\/j.mam.2022.101086_bib75","doi-asserted-by":"crossref","first-page":"5147","DOI":"10.1016\/S0021-9258(19)67767-7","article-title":"Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA)","volume":"266","author":"Kobayashi","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib76","first-page":"95","article-title":"An exploratory study of host polymorphisms in genes that clinically characterize breast cancer tumors and pretreatment cognitive performance in breast cancer survivors","volume":"9","author":"Koleck","year":"2017","journal-title":"Breast Cancer"},{"key":"10.1016\/j.mam.2022.101086_bib77","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.pharmthera.2018.05.011","article-title":"Therapeutic targeting of cathepsin C: from pathophysiology to treatment","volume":"90","author":"Korkmaz","year":"2018","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.mam.2022.101086_bib78","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.tips.2017.06.003","article-title":"The future of cysteine cathepsins in disease management","volume":"38","author":"Kramer","year":"2017","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib79","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1093\/molbev\/msy096","article-title":"Mega X: molecular evolutionary genetics analysis across computing platforms","volume":"35","author":"Kumar","year":"2018","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.mam.2022.101086_bib80","doi-asserted-by":"crossref","DOI":"10.3390\/cancers13081877","article-title":"Cystatin M\/E (Cystatin 6): a Janus-Faced cysteine protease inhibitor with both tumor-suppressing and tumor-promoting functions","volume":"13","author":"Lalmanach","year":"2021","journal-title":"Cancers"},{"issue":"6","key":"10.1016\/j.mam.2022.101086_bib81","doi-asserted-by":"crossref","first-page":"1944","DOI":"10.3390\/ijms21061944","article-title":"Regulation of the proteolytic activity of cysteine cathepsins by oxidants","volume":"21","author":"Lalmanach","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib82","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1515\/hsz-2014-0210","article-title":"Cysteine cathepsins and cystatins: from ancillary tasks to prominent status in lung diseases","volume":"396","author":"Lalmanach","year":"2015","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib83","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1021\/bi9822271","article-title":"The crystal structure of human procathepsin K","volume":"38","author":"LaLonde","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.mam.2022.101086_bib84","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.biochi.2007.08.011","article-title":"Biochemical properties and regulation of cathepsin K activity","volume":"90","author":"Lecaille","year":"2008","journal-title":"Biochimie"},{"key":"10.1016\/j.mam.2022.101086_bib85","doi-asserted-by":"crossref","first-page":"4459","DOI":"10.1021\/cr0101656","article-title":"Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design","volume":"102","author":"Lecaille","year":"2002","journal-title":"Chem. Rev."},{"key":"10.1016\/j.mam.2022.101086_bib86","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.biochi.2015.08.014","article-title":"Antimicrobial proteins and peptides in human lung diseases: a friend and foe partnership with host proteases","volume":"122","author":"Lecaille","year":"2016","journal-title":"Biochimie"},{"key":"10.1016\/j.mam.2022.101086_bib87","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1111\/bph.13920","article-title":"l-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia","volume":"175","author":"Leng","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.mam.2022.101086_bib88","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/S1078-5884(97)80219-5","article-title":"Serum-elastin-peptides as a predictor of expansion of small abdominal aortic aneurysms","volume":"14","author":"Lindholt","year":"1997","journal-title":"Eur. J. Vasc. Endovasc."},{"key":"10.1016\/j.mam.2022.101086_bib89","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1053\/ejvs.2001.1329","article-title":"Five-year results of elastin and collagen markers as predictive tools in the management of small abdominal aortic aneurysms","volume":"21","author":"Lindholt","year":"2001","journal-title":"Eur. J. Vasc. Endovasc."},{"key":"10.1016\/j.mam.2022.101086_bib90","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1515\/BC.2006.160","article-title":"Degradation of apolipoprotein B-100 by lysosomal cysteine cathepsins","volume":"387","author":"Linke","year":"2006","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib91","series-title":"Biology of the Lysosome, Subcellular Biochemistry","year":"1996"},{"key":"10.1016\/j.mam.2022.101086_bib92","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1002\/jcp.1041400316","article-title":"Elastin repeat peptides as chemoattractants for bovine aortic endothelial cells","volume":"140","author":"Long","year":"1989","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.mam.2022.101086_bib93","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.ijcard.2019.09.070","article-title":"Angiotensin II-Induced vascular remodeling and hypertension involves cathepsin L\/V- MEK\/ERK mediated mechanism","volume":"298","author":"Lu","year":"2020","journal-title":"Int. J. Cardiol."},{"key":"10.1016\/j.mam.2022.101086_bib94","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0041813","article-title":"Plasma cathepsin S and cystatin C levels and risk of abdominal aortic aneurysm: a randomized population\u2013based study","volume":"7","author":"Lv","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.mam.2022.101086_bib95","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.atherosclerosis.2013.05.018","article-title":"Plasma levels of cathepsins L, K, and V and risks of abdominal aortic aneurysms: a randomized population-based study","volume":"230","author":"Lv","year":"2013","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.mam.2022.101086_bib96","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1167\/iovs.06-0884","article-title":"Generation of endostatin by matrix metalloproteinase and cathepsin from human limbocorneal epithelial cells cultivated on amniotic membrane","volume":"48","author":"Ma","year":"2007","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib97","doi-asserted-by":"crossref","first-page":"1258","DOI":"10.1095\/biolreprod.110.086413","article-title":"Transcriptomic signature of trophoblast differentiation in a human embryonic stem cell model","volume":"84","author":"Marchand","year":"2011","journal-title":"Biol. Reprod."},{"key":"10.1016\/j.mam.2022.101086_bib98","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0046086","article-title":"Validation of the cancer BioChip System as a 3D siRNA screening tool for breast cancer targets","volume":"7","author":"Marhefka","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.mam.2022.101086_bib99","doi-asserted-by":"crossref","first-page":"3870","DOI":"10.1038\/s41598-019-40432-w","article-title":"Reactive centre loop dynamics and serpin specificity","volume":"9","author":"Marijanovic","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mam.2022.101086_bib100","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.ejmech.2012.04.002","article-title":"Evaluation of synthetic acridones and 4-quinolinones as potent inhibitors of cathepsins L and V","volume":"54","author":"Marques","year":"2012","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib101","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1159\/000496609","article-title":"Possible association between cathepsin V and the development of placenta accreta spectrum disorders","volume":"84","author":"Matsukawa","year":"2019","journal-title":"Gynecol. Obstet. Invest."},{"key":"10.1016\/j.mam.2022.101086_bib102","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.tcm.2012.12.004","article-title":"Elastin fragmentation and atherosclerosis progression: the elastokine concept","volume":"23","author":"Maurice","year":"2013","journal-title":"Trends Cardiovasc. Med."},{"key":"10.1016\/j.mam.2022.101086_bib103","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1146\/annurev.biophys.28.1.181","article-title":"The lysosomal cysteine proteases","volume":"28","author":"McGrath","year":"1999","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"issue":"69","key":"10.1016\/j.mam.2022.101086_bib104","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.matbio.2018.03.001","article-title":"The impaired proteases and anti-proteases balance in Idiopathic Pulmonary Fibrosis","volume":"68","author":"Menou","year":"2018","journal-title":"Matrix Biol."},{"key":"10.1016\/j.mam.2022.101086_bib105","doi-asserted-by":"crossref","first-page":"14453","DOI":"10.1074\/jbc.M801283200","article-title":"Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation","volume":"283","author":"Miheli\u010d","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib106","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1515\/BC.2007.155","article-title":"Two decades of thyroglobulin type-1 domain research","volume":"388","author":"Miheli\u010d","year":"2007","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib107","doi-asserted-by":"crossref","first-page":"44854","DOI":"10.1074\/jbc.M205630200","article-title":"Signaling pathways transduced through the elastin receptor facilitate proliferation of arterial smooth muscle cells","volume":"277","author":"Mochizuki","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib108","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1038\/nrc1949","article-title":"Cysteine cathepsins: multifunctional enzymes in cancer","volume":"6","author":"Mohamed","year":"2006","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.mam.2022.101086_bib109","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/5584_2014_26","article-title":"Endostatin and cathepsin-V in bronchoalveolar lavage fluid of patients with pulmonary sarcoidosis","volume":"833","author":"Naumnik","year":"2015","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.mam.2022.101086_bib110","doi-asserted-by":"crossref","first-page":"10853","DOI":"10.1074\/jbc.272.16.10853","article-title":"Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins","volume":"272","author":"Ni","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib111","doi-asserted-by":"crossref","first-page":"3601","DOI":"10.1016\/j.febslet.2012.08.001","article-title":"Determination of cathepsin V activity and intracellular trafficking by N-glycosylation","volume":"586","author":"Niwa","year":"2012","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mam.2022.101086_bib112","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1093\/rheumatology\/kes379","article-title":"Decreased cathepsin V expression due to Fli1 deficiency contributes to the development of dermal fibrosis and proliferative vasculopathy in systemic sclerosis","volume":"52","author":"Noda","year":"2013","journal-title":"Rheumatology"},{"key":"10.1016\/j.mam.2022.101086_bib113","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1515\/hsz-2013-0134","article-title":"Cathepsin K: a unique collagenolytic cysteine peptidase","volume":"394","author":"Novinec","year":"2013","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib114","doi-asserted-by":"crossref","first-page":"375","DOI":"10.2340\/0001555574375379","article-title":"In vivo studies concerning a pH gradient in human stratum corneum and upper epidermis","volume":"74","author":"Ohman","year":"1994","journal-title":"Acta Derm. Venereol."},{"key":"10.1016\/j.mam.2022.101086_bib115","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1038\/nrc4027","article-title":"Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response","volume":"15","author":"Olson","year":"2015","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.mam.2022.101086_bib116","doi-asserted-by":"crossref","first-page":"36980","DOI":"10.1074\/jbc.M706991200","article-title":"DNA accelerates the inhibition of human cathepsin V by serpins","volume":"282","author":"Ong","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib117","doi-asserted-by":"crossref","first-page":"3726","DOI":"10.1200\/JCO.2005.04.7985","article-title":"Gene expression and benefit of chemotherapy in women with node-negative, estrogen receptor\u2013positive breast cancer","volume":"24","author":"Paik","year":"2006","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.mam.2022.101086_bib118","doi-asserted-by":"crossref","first-page":"129544","DOI":"10.1016\/j.bbagen.2020.129544","article-title":"Expression of elastolytic cathepsins in human skin and their involvement in age-dependent elastin degradation","volume":"1864","author":"Panwar","year":"2020","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.mam.2022.101086_bib119","doi-asserted-by":"crossref","first-page":"2415","DOI":"10.1002\/jbmr.3227","article-title":"An Ectosteric inhibitor of cathepsin K inhibits bone resorption in ovariectomized mice","volume":"32","author":"Panwar","year":"2017","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.mam.2022.101086_bib120","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/j.biochi.2015.10.010","article-title":"Endothelial cells and cathepsins: biochemical and biomechanical regulation","volume":"122","author":"Platt","year":"2016","journal-title":"Biochimie"},{"key":"10.1016\/j.mam.2022.101086_bib121","doi-asserted-by":"crossref","first-page":"1972","DOI":"10.1002\/ijc.23296","article-title":"Locally generated VGVAPG and VAPG elastin-derived peptides amplify melanoma invasion via the galectin-3 receptor","volume":"122","author":"Pocza","year":"2008","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.mam.2022.101086_bib122","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2018.e00673","article-title":"Human brain gene expression profiles of the cathepsin V and cathepsin L cysteine proteases, with the PC1\/3 and PC2 serine proteases, involved in neuropeptide production","volume":"4","author":"Podvin","year":"2018","journal-title":"Heliyon"},{"key":"10.1016\/j.mam.2022.101086_bib123","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.1038\/nprot.2017.091","article-title":"Synthesis of a HyCoSuL peptide substrate library to dissect protease substrate specificity","volume":"12","author":"Poreba","year":"2017","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.mam.2022.101086_bib124","doi-asserted-by":"crossref","first-page":"749","DOI":"10.2119\/molmed.2015.00197","article-title":"The HIV protease inhibitor saquinavir inhibits HMGBl-driven inflammation by targeting the interaction of cathepsin V with TLR4\/MyD88","volume":"21","author":"Pribis","year":"2015","journal-title":"Mol. Med."},{"key":"10.1016\/j.mam.2022.101086_bib125","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1084\/jem.192.6.789","article-title":"Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages","volume":"192","author":"Punturieri","year":"2000","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.mam.2022.101086_bib126","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1515\/BC.2008.020","article-title":"Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen","volume":"389","author":"Puzer","year":"2008","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib127","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.abb.2004.07.006","article-title":"Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L","volume":"430","author":"Puzer","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.mam.2022.101086_bib128","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1515\/BC.2005.081","article-title":"A possible alternative mechanism of kinin generation in vivo by cathepsin L","volume":"386","author":"Puzer","year":"2005","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib129","doi-asserted-by":"crossref","first-page":"D624","DOI":"10.1093\/nar\/gkx1134","article-title":"The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database","volume":"46","author":"Rawlings","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mam.2022.101086_bib130","doi-asserted-by":"crossref","first-page":"3849","DOI":"10.1073\/pnas.92.9.3849","article-title":"Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages","volume":"92","author":"Reddy","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.mam.2022.101086_bib131","doi-asserted-by":"crossref","first-page":"3421","DOI":"10.1172\/JCI42918","article-title":"Specialized roles for cysteine cathepsins in health and disease","volume":"120","author":"Reiser","year":"2010","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.mam.2022.101086_bib132","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1074\/jbc.M109.043331","article-title":"Versatile loops in mycocypins inhibit three protease families","volume":"285","author":"Renko","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib133","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1096\/fj.99-0970com","article-title":"Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling","volume":"14","author":"Roth","year":"2000","journal-title":"Faseb. J."},{"key":"10.1016\/j.mam.2022.101086_bib134","doi-asserted-by":"crossref","first-page":"4334","DOI":"10.1111\/j.1742-4658.2009.07138.x","article-title":"Macrocypins, a family of cysteine protease inhibitors from the basidiomycete Macrolepiota procera","volume":"276","author":"Saboti\u010d","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.mam.2022.101086_bib135","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.matbio.2013.07.002","article-title":"Differential expression of cathepsins K, S and V between young and aged Caucasian women skin epidermis","volume":"33","author":"Sage","year":"2014","journal-title":"Matrix Biol."},{"key":"10.1016\/j.mam.2022.101086_bib136","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/1465-9921-12-13","article-title":"Lack of cathepsin activities alter or prevent the development of lung granulomas in a mouse model of sarcoidosis","volume":"12","author":"Samokhin","year":"2011","journal-title":"Respir. Res."},{"key":"10.1016\/j.mam.2022.101086_bib137","article-title":"Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas","volume":"8","author":"Santamar\u00eda","year":"1998","journal-title":"Cancer Res."},{"key":"10.1016\/j.mam.2022.101086_bib138","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0006-291X(67)80055-X","article-title":"On the size of the active site in proteases","volume":"27","author":"Schechter","year":"1967","journal-title":"I. Papain. Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mam.2022.101086_bib139","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1007\/s00011-012-0495-x","article-title":"Decreased arthritis severity in cathepsin L-deficient mice is attributed to an impaired T helper cell compartment","volume":"61","author":"Schurigt","year":"2012","journal-title":"Inflamm. Res."},{"key":"10.1016\/j.mam.2022.101086_bib140","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1242\/dev.025627","article-title":"Cathepsin proteases have distinct roles in trophoblast function and vascular remodelling","volume":"135","author":"Screen","year":"2008","journal-title":"Development"},{"key":"10.1016\/j.mam.2022.101086_bib141","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1186\/s13058-020-01376-6","article-title":"Cathepsin V suppresses GATA3 protein expression in luminal A breast cancer","volume":"22","author":"Sereesongsaeng","year":"2020","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.mam.2022.101086_bib142","doi-asserted-by":"crossref","first-page":"1674","DOI":"10.1016\/j.biochi.2010.03.014","article-title":"Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice","volume":"92","author":"Sevenich","year":"2010","journal-title":"Biochimie"},{"key":"10.1016\/j.mam.2022.101086_bib143","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1016\/j.bmc.2010.12.056","article-title":"Acridone alkaloids as potent inhibitors of cathepsin V","volume":"19","author":"Severino","year":"2011","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib144","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.bbrc.2005.06.119","article-title":"Elastin-derived peptides and TGF-beta1 induce osteogenic responses in smooth muscle cells","volume":"334","author":"Simionescu","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mam.2022.101086_bib145","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1038\/ncb1762","article-title":"Identification of genes that regulate epithelial cell migration using an siRNA screening approach","volume":"10","author":"Simpson","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.mam.2022.101086_bib146","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1110\/ps.8.2.283","article-title":"Crystal structure of wild-type human procathepsin K","volume":"8","author":"Sivaraman","year":"1999","journal-title":"Protein Sci."},{"key":"10.1016\/j.mam.2022.101086_bib147","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1006\/jmbi.1999.3410","article-title":"Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine","volume":"295","author":"Sivaraman","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2022.101086_bib148","doi-asserted-by":"crossref","first-page":"398","DOI":"10.3109\/07357907.2012.672608","article-title":"Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes","volume":"30","author":"Skrzypczak","year":"2012","journal-title":"Cancer Invest."},{"key":"10.1016\/j.mam.2022.101086_bib149","doi-asserted-by":"crossref","first-page":"12543","DOI":"10.1021\/bi000951p","article-title":"Crystal structure of human cathepsin V","volume":"39","author":"Somoza","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.mam.2022.101086_bib150","doi-asserted-by":"crossref","first-page":"37045","DOI":"10.1074\/jbc.M703447200","article-title":"Cell type-specific functions of the lysosomal protease cathepsin L in the heart","volume":"282","author":"Spira","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib151","doi-asserted-by":"crossref","first-page":"575","DOI":"10.3892\/ol.2015.3960","article-title":"Expression profile of cathepsins indicates the potential of cathepsins B and D as prognostic factors in breast cancer patients","volume":"11","author":"Sun","year":"2016","journal-title":"Oncol. Lett."},{"key":"10.1016\/j.mam.2022.101086_bib152","doi-asserted-by":"crossref","first-page":"1501200","DOI":"10.1183\/13993003.01200-2015","article-title":"Protean proteases: at the cutting edge of lung diseases","volume":"49","author":"Taggart","year":"2017","journal-title":"Eur. Respir. J."},{"key":"10.1016\/j.mam.2022.101086_bib153","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/s00109-008-0423-2","article-title":"Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT\/GSK3\u03b2 signaling","volume":"87","author":"Tang","year":"2009","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.mam.2022.101086_bib154","doi-asserted-by":"crossref","DOI":"10.1515\/bc.2010.109","article-title":"Nuclear cysteine cathepsin variants in thyroid carcinoma cells","volume":"391","author":"Tedelind","year":"2010","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib155","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1172\/JCI200318028","article-title":"Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis","volume":"112","author":"Tolosa","year":"2003","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.mam.2022.101086_bib156","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1136\/jclinpath-2019-205939","article-title":"Prognostic significance of cathepsin V (CTSV\/CTSL2) in breast ductal carcinoma in situ","volume":"73","author":"Toss","year":"2020","journal-title":"J. Clin. Pathol."},{"key":"10.1016\/j.mam.2022.101086_bib157","doi-asserted-by":"crossref","first-page":"5406","DOI":"10.2741\/3089","article-title":"Cystatins: biochemical and structural properties, and medical relevance","volume":"ume","author":"Turk","year":"2008","journal-title":"Front. Biosci."},{"key":"10.1016\/j.mam.2022.101086_bib158","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/nrd2092","article-title":"Targeting proteases: successes, failures and future prospects","volume":"5","author":"Turk","year":"2006","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.mam.2022.101086_bib159","doi-asserted-by":"crossref","first-page":"2761","DOI":"10.1016\/j.febslet.2007.05.038","article-title":"Protease signalling in cell death: caspases versus cysteine cathepsins","volume":"581","author":"Turk","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mam.2022.101086_bib160","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/S0167-4838(99)00263-0","article-title":"Lysosomal cysteine proteases: more than scavengers","volume":"1477","author":"Turk","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.mam.2022.101086_bib161","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1515\/bchm.1998.379.2.137","article-title":"Revised definition of substrate binding sites of papain-like cysteine proteases","volume":"379","author":"Turk","year":"1998","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib162","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0014-5793(96)00309-2","article-title":"Crystal structures of human procathepsin B at 3.2 and 3.3 \u00c5 resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide","volume":"384","author":"Turk","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mam.2022.101086_bib163","doi-asserted-by":"crossref","first-page":"5","DOI":"10.17344\/acsi.2018.4639","article-title":"Characteristics, structure, and biological role of stefins (Type-1 Cystatins) of human","volume":"66","author":"Turk","year":"2019","journal-title":"Acta Chim. Slov."},{"key":"10.1016\/j.mam.2022.101086_bib164","doi-asserted-by":"crossref","first-page":"997","DOI":"10.3390\/ijms22030997","article-title":"Mechanisms applied by protein inhibitors to inhibit cysteine proteases","volume":"22","author":"Tu\u0161ar","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.mam.2022.101086_bib165","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1042\/bj3390705","article-title":"Extrahepatic synthesis of plasminogen in the human cornea is up-regulated by interleukins-1\u03b1 and -1 8","volume":"339","author":"Twining","year":"1999","journal-title":"Biochem. J."},{"key":"10.1016\/j.mam.2022.101086_bib166","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s00109-005-0032-2","article-title":"The importance of cysteine cathepsin proteases for placental development","volume":"84","author":"Varanou","year":"2006","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.mam.2022.101086_bib167","doi-asserted-by":"crossref","first-page":"387","DOI":"10.2174\/138161207780162962","article-title":"Emerging roles of cysteine cathepsins in disease and their potential as drug targets","volume":"13","author":"Vasiljeva","year":"2007","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.mam.2022.101086_bib168","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1016\/j.biocel.2007.10.030","article-title":"Lung cysteine cathepsins: intruders or unorthodox contributors to the kallikrein-kinin system?","volume":"40","author":"Veillard","year":"2008","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.mam.2022.101086_bib169","doi-asserted-by":"crossref","first-page":"264","DOI":"10.3390\/cells8030264","article-title":"Cysteine cathepsins and their extracellular roles: shaping the microenvironment","volume":"8","author":"Vidak","year":"2019","journal-title":"Cells"},{"key":"10.1016\/j.mam.2022.101086_bib170","series-title":"Natural Products as Cathepsin Inhibitors. Studies in Natural Products Chemistry","first-page":"179","author":"Vidal-Albalat","year":"2016"},{"key":"10.1016\/j.mam.2022.101086_bib171","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.15252\/embj.201796750","article-title":"Protease cleavage site fingerprinting by label-free in-gel degradomics reveals pH-dependent specificity switch of legumain","volume":"36","author":"Vidmar","year":"2017","journal-title":"EMBO J."},{"key":"10.1016\/j.mam.2022.101086_bib172","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1016\/j.humimm.2007.05.009","article-title":"Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis","volume":"68","author":"Viken","year":"2007","journal-title":"Hum. Immunol."},{"key":"10.1016\/j.mam.2022.101086_bib173","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1007\/s12013-020-00940-3","article-title":"Cathepsin V mediates the tazarotene-induced gene 1-induced reduction in invasion in colorectal cancer cells","volume":"78","author":"Wang","year":"2020","journal-title":"Cell Biochem. Biophys."},{"key":"10.1016\/j.mam.2022.101086_bib174","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1007\/s004030050406","article-title":"Stratum corneum thiol protease (SCTP): a novel cysteine protease of late epidermal differentiation","volume":"291","author":"Watkinson","year":"1999","journal-title":"Arch. Dermatol. Res."},{"key":"10.1016\/j.mam.2022.101086_bib175","doi-asserted-by":"crossref","first-page":"7381","DOI":"10.1021\/bi027307q","article-title":"Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis","volume":"42","author":"Welss","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.mam.2022.101086_bib176","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.abb.2011.09.009","article-title":"Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues","volume":"516","author":"Wilder","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.mam.2022.101086_bib177","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1515\/hsz-2015-0114","article-title":"Cathepsin S: therapeutic, diagnostic, and prognostic potential","volume":"396","author":"Wilkinson","year":"2015","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib178","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1186\/rr29","article-title":"Importance of lysosomal cysteine proteases in lung disease","volume":"1","author":"Wolters","year":"2000","journal-title":"Respir. Res."},{"key":"10.1016\/j.mam.2022.101086_bib179","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1038\/onc.2013.72","article-title":"CTSL2 is a pro-apoptotic target of E2F1 and a modulator of histone deacetylase inhibitor and DNA damage-induced apoptosis","volume":"33","author":"Wong","year":"2014","journal-title":"Oncogene"},{"key":"10.1016\/j.mam.2022.101086_bib180","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1042\/bj3320499","article-title":"Quantification of cathepsins B and L in cells","volume":"332","author":"Xing","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.mam.2022.101086_bib181","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.3390\/cells9071679","article-title":"The ins and outs of cathepsins: physiological function and role in disease management","volume":"9","author":"Yadati","year":"2020","journal-title":"Cells"},{"key":"10.1016\/j.mam.2022.101086_bib182","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1089\/104454900314591","article-title":"Transcription of human cathepsin B is mediated by Sp1 and Ets family factors in glioma","volume":"19","author":"Yan","year":"2000","journal-title":"DNA Cell Biol."},{"key":"10.1016\/j.mam.2022.101086_bib183","doi-asserted-by":"crossref","first-page":"14042","DOI":"10.1074\/jbc.M110.105262","article-title":"GATA3 inhibits breast cancer metastasis through the reversal of epithelial-mesenchymal transition","volume":"285","author":"Yan","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib184","doi-asserted-by":"crossref","first-page":"36761","DOI":"10.1074\/jbc.M403986200","article-title":"Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages","volume":"279","author":"Yasuda","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2022.101086_bib185","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1021\/acschemneuro.1c00653","article-title":"Distinct dibasic cleavage specificities of neuropeptide-producing cathepsin L and cathepsin V cysteine proteases compared to PC1\/3 and PC2 serine proteases","volume":"13","author":"Yoon","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.mam.2022.101086_bib186","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1038\/jid.2009.40","article-title":"The biology of cystatin M\/E and its cognate target proteases","volume":"129","author":"Zeeuwen","year":"2009","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mam.2022.101086_bib187","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/sj.jid.5700480","article-title":"Colocalization of cystatin M\/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation","volume":"127","author":"Zeeuwen","year":"2007","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mam.2022.101086_bib188","doi-asserted-by":"crossref","first-page":"2867","DOI":"10.1093\/hmg\/11.23.2867","article-title":"A null mutation in the cystatin M\/E gene of ichq mice causes juvenile lethality and defects in epidermal cornification","volume":"11","author":"Zeeuwen","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.mam.2022.101086_bib189","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.7150\/ijbs.11751","article-title":"Evolutionary history of cathepsin L (L-like) Family genes in vertebrates","volume":"11","author":"Zhou","year":"2015","journal-title":"Int. J. Biol. Sci."}],"container-title":["Molecular Aspects of Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0098299722000280?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0098299722000280?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T18:16:47Z","timestamp":1758824207000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0098299722000280"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12]]},"references-count":189,"alternative-id":["S0098299722000280"],"URL":"https:\/\/doi.org\/10.1016\/j.mam.2022.101086","relation":{},"ISSN":["0098-2997"],"issn-type":[{"value":"0098-2997","type":"print"}],"subject":[],"published":{"date-parts":[[2022,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cathepsin V: Molecular characteristics and significance in health and disease","name":"articletitle","label":"Article Title"},{"value":"Molecular Aspects of Medicine","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mam.2022.101086","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"101086"}}