The PACAP-regulated gene selenoprotein T is abundantly expressed in mouse and human β-cells and its targeted inactivation impairs glucose tolerance

Endocrinology

Volumn 154, Issue 10, 2013, Pages 3796-3806

  Prevost, Gaëtan ^a,b   Arabo, Arnaud ^a   Jian, Long ^a,d   Quelennec, Eddy ^a   Cartier, Dorthe ^a   Hassan, Sahar ^a   Falluel Morel, Anthony ^a   Tanguy, Yannick ^a   Gargani, Sophia ^c   Lihrmann, Isabelle ^a   Kerr Conte, Julie ^c   Lefebvre, Hervé ^a,b   Pattou, François ^c   Anouar, Youssef ^a  

^a UNIVERSITÉ DE ROUEN   (France)

^b ROUEN UNIVERSITY HOSPITAL   (France)

^c UNIV LILLE   (France)

^d CHONGQING MEDICAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; INSULIN; SELENOPROTEIN; SELENOPROTEIN T; UNCLASSIFIED DRUG;

ALLELE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; ENDOPLASMIC RETICULUM; EXON; GENE DISRUPTION; GLUCOSE HOMEOSTASIS; GLUCOSE INTAKE; HUMAN; HUMAN TISSUE; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; IMPAIRED GLUCOSE TOLERANCE; INSULIN LIKE ACTIVITY; INSULIN RELEASE; MALE; MOUSE; NONHUMAN; PANCREAS ISLET BETA CELL; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; UPREGULATION; WILD TYPE;

ANIMALS; BLOOD GLUCOSE; CELL LINE; CROSSES, GENETIC; GENE EXPRESSION REGULATION; GENE SILENCING; GLUCOSE INTOLERANCE; HUMANS; INSULIN; INSULIN-SECRETING CELLS; MICE; MICE, INBRED C57BL; MICE, KNOCKOUT; MICE, TRANSGENIC; PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE; SELENOPROTEINS; SOMATOSTATIN-SECRETING CELLS; TISSUE CULTURE TECHNIQUES;

EID: 84884681004     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2013-1167     Document Type: Article

References (41)

1. Rayman MP. Selenium and human health. Lancet. 2012;379:1256-1268.
2. Kryukov GV, Castellano S, Novoselov SV, et al. Characterization of mammalian selenoproteomes. Science. 2003;300:1439-1443. (Pubitemid 36638165)
3. Hawkes WC, Alkan Z. Regulation of redox signaling by selenoproteins. Biol Trace Elem Res. 2010;134:235-251.
4. Bellinger FP, Raman AV, Reeves MA, Berry MJ. Regulation and function of selenoproteins in human disease. Biochem J. 2009;422:11-22.
5. Dikiy A, Novoselov SV, Fomenko DE, et al. SelT, Sel W, Sel H, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Biochemistry. 2007;46:6871-6882. (Pubitemid 46906416)
6. Tanguy Y, Falluel-Morel A, Arthaud S, et al. The PACAP-regulated gene selenoprotein T is highly induced in nervous, endocrine, and metabolic tissues during ontogenetic and regenerative processes. Endocrinology. 2011;152:4322-4335.
7. 2+ mobilization and neuroendocrine secretion. FASEB J. 2008;22:1756-1768.
8. Mueller AS, Mueller K, Wolf NM, Pallauf J. Selenium and diabetes: an enigma? Free Radic Res. 2009;43:1029-1059.
9. Shchedrina VA, Zhang Y, Labunskyy VM, Hatfield DL, Gladyshev VN. Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins. Antioxid Redox Signal. 2010;12:839-849.
10. Misu H, Takamura T, Takayama H, et al. A liver-derived secretory protein, selenoprotein P, causes insulin resistance. Cell Metab. 2010;12:483-495.
11. McClung JP, Roneker CA, Mu W, et al. Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase. Proc Natl Acad Sci U S A. 2004;101:8852-8857. (Pubitemid 38781575)
12. Loh K, Deng H, Fukushima A, et al. Reactive oxygen species enhance insulin sensitivity. Cell Metab. 2009;10:260-272.
13. Medina MC, Molina J, Gadea Y, et al. The thyroid hormone-inactivating type III deiodinase is expressed in mouse and human β-cells and its targeted inactivation impairs insulin secretion. Endocrinology. 2011;152:3717-3727.
14. Labunskyy VM, Lee BC, Handy DE, Loscalzo J, Hatfield DL, Gladyshev VN. Both maximal expression of selenoproteins and selenoprotein deficiency can promote development of type 2 diabetes-like phenotype in mice. Antioxid Redox Signal. 2011;14:2327-2336.
15. Seale LA, Hashimoto AC, Kurokawa S, et al. Disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice. Mol Cell Biol. 2012;32:4141-4154.
16. Schoenmakers E, Agostini M, Mitchell C, et al. Mutations in the selenocysteine insertion sequence-binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans. J Clin Invest. 2010;120:4220-4235.
17. Olsson M, Olsson B, Jacobson P, et al. Expression of the selenoprotein S (SELS) gene in subcutaneous adipose tissue and SELS genotype are associated with metabolic risk factors. Metab Clin Exp. 2011;60:114-120.
18. Hotta M, Tashiro F, Ikegami H, et al. Pancreatic β Cell-specific expression of thioredoxin, an antioxidative and antiapoptotic protein, prevents autoimmune and streptozotocin-induced diabetes. J Exp Med. 1998;188:1445-1451. (Pubitemid 28489581)
19. Chou FC, Sytwu HK. Overexpression of thioredoxin in islets transduced by a lentiviral vector prolongs graft survival in autoimmune diabetic NOD mice. J Biomed Sci. 2009;16:71.
20. Oslowski CM, Hara T, O'Sullivan-Murphy B, et al. Thioredoxin-interacting protein mediates ER stress-induced β cell death through initiation of the inflammasome. Cell Metab. 2012;16:265-273.
21. Lalloyer F, Vandewalle B, Percevault F, et al. Peroxisome prolifera-tor- activated receptor alpha improves pancreatic adaptation to insulin resistance in obese mice and reduces lipotoxicity in human islets. Diabetes. 2006;55:1605-1613. (Pubitemid 44324112)
22. Miyazaki J, Araki K, Yamato E, et al. Establishment of a pancreatic β-cell line that retains glucose-inducible insulin secretion: special reference to expression of glucose transporter isoforms. Endocrinology. 1990;127:126-132. (Pubitemid 20228111)
23. Grumolato L, Elkahloun AG, Ghzili H, et al. Microarray and suppression subtractive hybridization analyses of gene expression in pheochromocytoma cells reveal pleiotropic effects of pituitary adenylate cyclase-activating polypeptide on cell proliferation, survival, and adhesion. Endocrinology. 2003;144:2368-2379. (Pubitemid 36637089)
24. Dubois M, Kerr-Conte J, Gmyr V, et al. Non-esterified fatty acids are deleterious for human pancreatic islet function at physiological glucose concentration. Diabetologia. 2004;47:463-469. (Pubitemid 38491242)
25. Inagaki N, Yoshida H, Mizuta M, et al. Cloning and functional characterization of a third pituitary adenylate cyclase-activating polypeptide receptor subtype expressed in insulin-secreting cells. Proc Natl Acad Sci U S A. 1994;91:2679-2683.
26. Hansson HA, Holmgren A, Rozell B, Täljedal IB. Immunohistochemical localization of thioredoxin and thioredoxin reductase in mouse exocrine and endocrine pancreas. Cell Tissue Res. 1986;245:189-195. (Pubitemid 16033441)
27. Steinbrenner H, Hotze AL, Speckmann B, et al. Localization and regulation of pancreatic selenoprotein P. J Mol Endocrinol. 2013;50:31-42.
28. Sengupta A, Carlson BA, Labunskyy VM, Gladyshev VN, Hatfield DL. Selenoprotein T deficiency alters cell adhesion and elevates selenoprotein W expression in murine fibroblast cells. Biochem Cell Biol. 2009;87:953-961.
29. Lee S, Kim SM, Lee RT. Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance. Antioxid Redox Signal. 2013;18:1165-1207.
30. Lei XG, Vatamaniuk MZ. Two tales of antioxidant enzymes on β-cells and diabetes. Antioxid Redox Signal. 2011;14:489-503.
31. Wang X, Vatamaniuk MZ, Roneker CA, et al. Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. Antioxid Redox Signal. 2011;14:391-401.
32. Harmon JS, Bogdani M, Parazzoli SD, et al. β-Cell-Specific overexpression of glutathione peroxidase preserves intranuclear MafA and reverses diabetes in db/db mice. Endocrinology. 2009;150:4855-4862.
33. Mysore TB, Shinkel TA, Collins J, et al. Overexpression of glutathione peroxidase with two isoforms of superoxide dismutase protects mouse islets from oxidative injury and improves islet graft function. Diabetes. 2005;54:2109-2116. (Pubitemid 40911274)
34. Poitout V, Robertson RP. Glucolipotoxicity: fuel excess and betacell dysfunction. Endocr Rev. 2008;29:351-366. (Pubitemid 351679704)
35. Tang C, Han P, Oprescu AI, et al. Evidence for a role of superoxide generation in glucose-induced β-cell dysfunction in vivo. Diabetes. 2007;56:2722-2731. (Pubitemid 350044915)
36. Yamamoto K, Hashimoto H, Tomimoto S, et al. Overexpression of PACAP in transgenic mouse pancreatic beta-cells enhances insulin secretion and ameliorates streptozotocin-induced diabetes. Diabetes. 2003;52:1155-1162. (Pubitemid 36523350)
37. Sakurai Y, Shintani N, Hayata A, Hashimoto H, Baba A. Trophic effects of PACAP on pancreatic islets: a mini-review. J Mol Neurosci. 2011;43:3-7.
38. Ghzili H, Grumolato L, Thouënnon E, et al. Role of PACAP in the physiology and pathology of the sympathoadrenal system. Front Neuroendocrinol. 2008;29:128-141.
39. Nakata M, Shintani N, Hashimoto H, Baba A, Yada T. Intra-islet PACAP protects pancreatic β-cells against glucotoxicity and lipotoxicity. J Mol Neurosci. 2010;42:404-410.
40. 2- toxicity in islet β-cells and its prevention by PACAP. Peptides. 2002;23:135-142.
41. Yada T, Sakurada M, Ishihara H, et al. Pituitary adenylate cyclase-activating polypeptide (PACAP) is an islet substance serving as an intra-islet amplifier of glucose-induced insulin secretion in rats. J Physiol (Lond.) 1997;505(Pt 2):319-328. (Pubitemid 28043379)