{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T12:05:16Z","timestamp":1790683516167,"version":"4.1.0"},"reference-count":45,"publisher":"Japan Endocrine Society","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Endocr J"],"published-print":{"date-parts":[[2017]]},"DOI":"10.1507\/endocrj.ej16-0319","type":"journal-article","created":{"date-parts":[[2016,12,12]],"date-time":"2016-12-12T22:09:23Z","timestamp":1481580563000},"page":"255-268","source":"Crossref","is-referenced-by-count":15,"title":["Glucose deprivation attenuates sortilin levels in skeletal muscle cells"],"prefix":"10.1507","volume":"64","author":[{"given":"Miyako","family":"Ariga","sequence":"first","affiliation":[{"name":"Department of Animal Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yosuke","family":"Yoneyama","sequence":"additional","affiliation":[{"name":"Department of Animal Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshiaki","family":"Fukushima","sequence":"additional","affiliation":[{"name":"Department of Animal Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuri","family":"Ishiuchi","sequence":"additional","affiliation":[{"name":"Department of Life Sciences, Graduate School of Life Sciences, Toyo University, Gunma, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takayuki","family":"Ishii","sequence":"additional","affiliation":[{"name":"Department of Life Sciences, Graduate School of Life Sciences, Toyo University, Gunma, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hitoshi","family":"Sato","sequence":"additional","affiliation":[{"name":"Department of Life Sciences, Graduate School of Life Sciences, Toyo University, Gunma, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fumihiko","family":"Hakuno","sequence":"additional","affiliation":[{"name":"Department of Animal Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taku","family":"Nedachi","sequence":"additional","affiliation":[{"name":"Department of Life Sciences, Graduate School of Life Sciences, Toyo University, Gunma, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shin-Ichiro","family":"Takahashi","sequence":"additional","affiliation":[{"name":"Department of Animal Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"386","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1. Lefrancois S, Canuel M, Zeng J, Morales CR (2005) Inactivation of sortilin (a novel lysosomal sorting receptor) by dominant negative competition and RNA interfer-ence. <i>Biol Proced Online<\/i> 7: 17-25.","DOI":"10.1251\/bpo101"},{"key":"2","doi-asserted-by":"crossref","unstructured":"2. Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, <i>et al<\/i>. (2001) The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein. <i>EMBO J<\/i> 20: 2180-2190.","DOI":"10.1093\/emboj\/20.9.2180"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3. Shi J, Kandror KV (2007) The luminal Vps10p domain of sortilin plays the predominant role in targeting to insulin-responsive Glut4-containing vesicles. <i>J Biol Chem<\/i> 282: 9008-9016.","DOI":"10.1074\/jbc.M608971200"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4. Huang G, Buckler-Pena D, Nauta T, Singh M, Asmar A, <i>et al<\/i>. (2013) Insulin responsiveness of glucose transporter 4 in 3T3-L1 cells depends on the presence of sortilin. <i>Mol Biol Cell<\/i> 19: 3115-3122.","DOI":"10.1091\/mbc.E12-10-0765"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5. Shi J, Huang G, Kandror KV (2008) Self-assembly of Glut4 Storage Vesicles during Differentiation of 3T3-L1 Adipocytes. <i>J Biol Chem<\/i> 283: 30311-30321.","DOI":"10.1074\/jbc.M805182200"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6. Shi J, Kandror KV (2005) Sortilin is essential and sufficient for the formation of Glut4 storage vesicles in 3T3-L1 adipocytes. <i>Dev Cell<\/i> 9: 99-108.","DOI":"10.1016\/j.devcel.2005.04.004"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7. Ariga M, Nedachi T, Katagiri H, Kanzaki M (2008) Functional role of sortilin in myogenesis and development of insulin-responsive glucose transport system in C2C12 myocytes. <i>J Biol Chem<\/i> 283: 10208-10220.","DOI":"10.1074\/jbc.M710604200"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8. Nykjaer A, Lee R, Teng KK, Jansen P, Madsen P, <i>et al<\/i>. (2004) Sortilin is essential for proNGF-induced neuronal cell death. <i>Nature<\/i> 427: 843-848.","DOI":"10.1038\/nature02319"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9. Bronfman FC, Fainzilber M (2004) Multi-tasking by the p75 neurotrophin receptor: sortilin things out? <i>EMBO Rep<\/i> 5: 867-871.","DOI":"10.1038\/sj.embor.7400219"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10. Pandey A, Chawla S, Guchhait P (2015) Type-2 diabetes: Current under-standing and future perspectives. <i>IUBMB Life<\/i> 67: 506-513.","DOI":"10.1002\/iub.1396"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11. Kurowski TG, Lin Y, Luo Z, Tsichlis PN, Buse MG, <i>et al<\/i>. (1999) Hyperglycemia inhibits insulin activation of Akt\/protein kinase B but not phosphati-dylinositol 3-kinase in rat skeletal muscle. <i>Diabetes<\/i> 48: 658-663.","DOI":"10.2337\/diabetes.48.3.658"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12. Nedachi T, Kanzaki M (2006) Regulation of glucose transporters by insulin and extracellular glucose in C2C12 myotubes. <i>Am J Physiol Endocrinol Metab<\/i> 291: E817-828.","DOI":"10.1152\/ajpendo.00194.2006"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13. Krook A, Kawano Y, Song XM, Efendic S, Roth RA, <i>et al<\/i>. (1997) Improved glucose tolerance restores insulin-stimulated Akt kinase activity and glucose transport in skeletal muscle from diabetic Goto-Kakizaki rats. <i>Diabetes<\/i> 46: 2110-2114.","DOI":"10.2337\/diab.46.12.2110"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14. Oku A, Nawano M, Ueta K, Fujita T, Umebayashi I, <i>et al<\/i>. (2001) Inhibitory effect of hyperglycemia on insulin-induced Akt\/protein kinase B activation in skeletal muscle. <i>Am J Physiol Endocrinol Metab<\/i> 280: E816-824.","DOI":"10.1152\/ajpendo.2001.280.5.E816"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15. McCall AL (2012) Insulin therapy and hypoglycemia. <i>Endocrinol Metab Clin North Am<\/i> 41: 57-87.","DOI":"10.1016\/j.ecl.2012.03.001"},{"key":"16","unstructured":"16. Brun JF, Dumortier M, Fedou C, Mercier J (2001) Exercise hypoglycemia in nondiabetic subjects. <i>Diabetes Metab<\/i> 27: 92-106."},{"key":"17","doi-asserted-by":"crossref","unstructured":"17. von der Crone S, Deppe C, Barthel A, Sasson S, Joost HG, <i>et al<\/i>. (2000) Glucose deprivation induces Akt-dependent synthesis and incorporation of GLUT1, but not of GLUT4, into the plasma membrane of 3T3-L1 adipocytes. <i>Eur J Cell Biol<\/i> 79: 943-949.","DOI":"10.1078\/0171-9335-00118"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18. Nedachi T, Kadotani A, Ariga M, Katagiri H, Kanzaki M (2008) Ambient glucose levels qualify the potency of insulin myogenic actions by regulating SIRT1 and FoxO3a in C2C12 myocytes. <i>Am J Physiol Endocrinol Metab<\/i> 294: E668-678.","DOI":"10.1152\/ajpendo.00640.2007"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19. Shibata H, Suzuki Y, Omata W, Tanaka S, Kojima I (1995) Dissection of GLUT4 recycling pathway into exocytosis and endocytosis in rat adipocytes. Evidence that GTP-binding proteins are involved in both processes. <i>J Biol Chem<\/i> 270: 11489-11495.","DOI":"10.1074\/jbc.270.19.11489"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20. McKeel DW, Jarett L (1970) Preparation and characterization of a plasma membrane fraction from isolated fat cells. <i>J Cell Biol<\/i> 44: 417-432.","DOI":"10.1083\/jcb.44.2.417"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21. Mitsumoto Y, Klip A (1992) Development regulation of the subcellular dis-tribution and glycosylation of GLUT1 and GLUT4 glucose transporters during myo-genesis of L6 muscle cells. <i>J Biol Chem<\/i> 267: 4957-4962.","DOI":"10.1016\/S0021-9258(18)42923-7"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22. Kahn BB, Alquier T, Carling D, Hardie DG (2005) AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. <i>Cell Metab<\/i> 1: 15-25.","DOI":"10.1016\/j.cmet.2004.12.003"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23. Hardie DG (2011) Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism. <i>Proc Nutr Soc<\/i> 70: 92-99.","DOI":"10.1017\/S0029665110003915"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24. Hardie DG, Scott JW, Pan DA, Hudson ER (2003) Management of cellular energy by the AMP-activated protein kinase system. <i>FEBS Lett<\/i> 546: 113-120.","DOI":"10.1016\/S0014-5793(03)00560-X"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25. Wapnir RA, Lifshitz F (1977) Fasting-induced hypoglycemia in experi-mentally malnourished rats. <i>J Nutr<\/i> 107: 383-390.","DOI":"10.1093\/jn\/107.3.383"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26. Braulke T, Bonifacino JS (2009) Sorting of lysosomal proteins. <i>Biochim Biophys Acta<\/i> 1793: 605-614.","DOI":"10.1016\/j.bbamcr.2008.10.016"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27. Tsuchiya Y, Hatakeyama H, Emoto N, Wagatsuma F, Matsushita S,<i> et al<\/i>. (2010)Palmitate-induced down-regulation of sortilin and impaired GLUT4 traf-ficking in C2C12 myotubes. <i>J Biol Chem <\/i>285: 34371-34381.","DOI":"10.1074\/jbc.M110.128520"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28. Starling GP1, Yip YY, Sanger A, Morton PE, Eden ER, <i>et al<\/i>. (2016) Folliculin directs the formation of a Rab34-RILP complex to control the nutri-ent-dependent dynamic distribution of lysosomes. <i>EMBO Rep<\/i> 17: 823-841.","DOI":"10.15252\/embr.201541382"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29. Thoreen CC, Chantranupong L, Keys HR, Wang T, Gray NS, <i>et al<\/i>. (2012) A unifying model for mTORC1-mediated regulation of mRNA translation. <i>Nature<\/i> 485: 109-113.","DOI":"10.1038\/nature11083"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30. Moschetta M, Reale A, Marasco C, Vacca A, Carrat&ugrave; MR (2014) Therapeutic targeting of the mTOR-signalling pathway in cancer: benefits and limitations. <i>Br J Pharmacol<\/i> 171: 3801-3813.","DOI":"10.1111\/bph.12749"},{"key":"31","doi-asserted-by":"crossref","unstructured":"31. Pause A, Belsham GJ, Gingras AC, Donz&eacute; O, Lin TA, <i>et al<\/i>. (1994) Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5&rsquo;-cap function. <i>Nature<\/i> 371: 762-767.","DOI":"10.1038\/371762a0"},{"key":"32","doi-asserted-by":"crossref","unstructured":"32. Dann SG, Thomas G (2006) The amino acid sensitive TOR pathway from yeast to mammals. <i>FEBS Lett<\/i> 580: 2821-2829.","DOI":"10.1016\/j.febslet.2006.04.068"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33. Palm W, Park Y, Wright K, Pavlova NN, Tuveson DA, <i>et al<\/i>. (2015) The Utilization of Extracellular Proteins as Nutrients Is Suppressed by mTORC1. <i>Cell <\/i>162: 259-270.","DOI":"10.1016\/j.cell.2015.06.017"},{"key":"34","doi-asserted-by":"crossref","unstructured":"34. Gaudreault N, Santur&eacute; M, Pitre M, Nadeau A, Marette A, <i>et al<\/i>. (2001) Effects of insulin on regional blood flow and glucose uptake in Wistar and Sprague-Dawley rats. <i>Metabolism<\/i> 50: 65-73.","DOI":"10.1053\/meta.2001.18569"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35. Takekura H, Yoshioka T (1987) Determination of metabolic profiles on single muscle fibres of different types. <i>J Muscle Res Cell Motil<\/i> 8: 342-348.","DOI":"10.1007\/BF01568890"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36. Sandri M, Barberi L, Bijlsma AY, Blaauw B, Dyar KA, <i>et al<\/i>. (2013) Signalling pathways regulating muscle mass in ageing skeletal muscle: the role of the IGF1-Akt-mTOR-FoxO pathway. <i>Biogerontology<\/i> 14: 303-323.","DOI":"10.1007\/s10522-013-9432-9"},{"key":"37","doi-asserted-by":"crossref","unstructured":"37. Fry CS, Drummond MJ, Glynn EL, Dickinson JM, Gundermann DM, <i>et al<\/i>. (2011) Aging impairs contraction-induced human skeletal muscle mTORC1 signaling and protein synthesis. <i>Skelet Muscle<\/i> 1: 11.","DOI":"10.1186\/2044-5040-1-11"},{"key":"38","doi-asserted-by":"crossref","unstructured":"38. Welle S (2002) Cellular and molecular basis of age-related sarcopenia. <i>Can J Appl Physiol <\/i>27: 19-41.","DOI":"10.1139\/h02-002"},{"key":"39","doi-asserted-by":"crossref","unstructured":"39. Meissner JD, Umeda PK, Chang KC, Gros G, Scheibe RJ (2007) Activation of the beta myosin heavy chain promoter by MEF-2D, MyoD, p300, and the calcineu-rin\/NFATc1 pathway. <i>J Cell Physiol<\/i> 211: 138-148.","DOI":"10.1002\/jcp.20916"},{"key":"40","doi-asserted-by":"crossref","unstructured":"40. Ai H, Ihlemann J, Hellsten Y, Lauritzen HP, Hardie DG, <i>et al<\/i>. (2002) Effect of fiber type and nutritional state on AICAR- and contraction-stimulated glucose transport in rat muscle. <i>Am J Physiol Endocrinol Metab<\/i> 282: E1291-1300.","DOI":"10.1152\/ajpendo.00167.2001"},{"key":"41","doi-asserted-by":"crossref","unstructured":"41. Cant&oacute; C, Jiang LQ, Deshmukh AS, Mataki C, Coste A, <i>et al<\/i>. (2010) Interdependence of AMPK and SIRT1 for Metabolic Adaptation to Fasting and Exercise in Skeletal Muscle. <i>Cell Metab<\/i> 11: 213-219.","DOI":"10.1016\/j.cmet.2010.02.006"},{"key":"42","doi-asserted-by":"crossref","unstructured":"42. Frier BC, Jacobs RL, Wright DC (2011) Interactions between the con-sumption of a high-fat diet and fasting in the regulation of fatty acid oxidation enzyme gene expression: an evaluation of potential mechanisms. <i>Am J Physiol<\/i> <i>Regul Integr Comp Physiol <\/i>300: R212-221.","DOI":"10.1152\/ajpregu.00367.2010"},{"key":"43","doi-asserted-by":"crossref","unstructured":"43. Liu X, Yuan H, Niu Y, Niu W, Fu L (2012) The role of AMPK\/mTOR\/S6K1 signaling axis in mediating the physiological process of exercise-induced insulin sensi-tization in skeletal muscle of C57BL\/6 mice. <i>Biochim Biophys Acta<\/i> 1822: 1716-1726.","DOI":"10.1016\/j.bbadis.2012.07.008"},{"key":"44","doi-asserted-by":"crossref","unstructured":"44. Ai H, Ihlemann J, Hellsten Y, Lauritzen HP, Hardie DG, <i>et al<\/i>. (2002) Effect of fiber type and nutritional state on AICAR- and contraction-stimulated glucose transport in rat muscle. <i>Am J Physiol Endocrinol Metab<\/i> 282: E1291-1300.","DOI":"10.1152\/ajpendo.00167.2001"},{"key":"45","doi-asserted-by":"crossref","unstructured":"45. Holecek M, Sispera L (2016) Effects of Arginine Supplementation on Amino Acid Profiles in Blood and Tissues in Fed and Overnight-Fasted Rats. <i>Nutrients<\/i> 8: 206-216.","DOI":"10.3390\/nu8040206"}],"container-title":["Endocrine Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/endocrj\/64\/3\/64_EJ16-0319\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,7,16]],"date-time":"2022-07-16T23:31:41Z","timestamp":1658014301000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/endocrj\/64\/3\/64_EJ16-0319\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017]]},"references-count":45,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2017]]}},"URL":"https:\/\/doi.org\/10.1507\/endocrj.ej16-0319","relation":{},"ISSN":["0918-8959","1348-4540"],"issn-type":[{"value":"0918-8959","type":"print"},{"value":"1348-4540","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017]]}}}