Issue

Vol. 64 No. 1: Issue 1

The undersigned hereby assign all rights, included but not limited to copyright, for this manuscript to CMB Association upon its submission for consideration to publication on Cellular and Molecular Biology. The rights assigned include, but are not limited to, the sole and exclusive rights to license, sell, subsequently assign, derive, distribute, display and reproduce this manuscript, in whole or in part, in any format, electronic or otherwise, including those in existence at the time this agreement was signed. The authors hereby warrant that they have not granted or assigned, and shall not grant or assign, the aforementioned rights to any other person, firm, organization, or other entity. All rights are automatically restored to authors if this manuscript is not accepted for publication.

The effects of caveolin1 on β cell proliferation

https://doi.org/10.14715/cmb/2018.64.1.8
Haicheng Li
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Hangya Peng
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Haixia Xu
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Fen Xu
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Shuo Lin
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Keyi Lin
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Wen Zeng
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
Longyi Zeng
Department of Endocrinology, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China

Corresponding Author(s) : Longyi Zeng

zengly@mail.sysu.edu.cn

Cellular and Molecular Biology, Vol. 64 No. 1: Issue 1

Abstract

Our study aims to access the influence of caveolin1 (CAV1) on β cell expression profiles. We knocked down the expression of CAV1 in both NIT-1 cells and islets isolated from C57BL/6J mice using an RNA interference technique, which was realized by the transfer of an shRNA vector targeting CAV1 mRNA into NIT-1 cells or islets through latent virus infection. First, we identified the change in gene expression profiles in islets, in which the CAV1 expression level was down-regulated, as ascertained by mouse gene expression microarray, and the results showed that pathways related to β cell proliferation and pancreatic secretion functions were significantly influenced. The results of MTT demonstrated that the knockdown of CAV1 expression in NIT-1 cells promoted proliferation. The protein array results showed that pro-apoptotic cytokines were down-regulated in the NIT-1 cell line with CAV1 knockdown. These findings suggest that CAV1 might be involved in apoptosis and proliferation regulation in β cells, and therefore could be a potential target for the development of novel therapies for diabetes mellitus.

Keywords

Caveolin1 Microarray Pancreatic islets Proliferation Apoptosis High throughput screening.
Li, H., Peng, H., Xu, H., Xu, F., Lin, S., Lin, K., Zeng, W., & Zeng, L. (2018). The effects of caveolin1 on β cell proliferation. Cellular and Molecular Biology, 64(1), 40–46. https://doi.org/10.14715/cmb/2018.64.1.8
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. References
  2. Ogurtsova K, da Rocha Fernandes JD, Huang Y et al. IDF Diabetes Atlas: Global estimates for the prevalence of diabetes for 2015 and 2040. Diabetes Res Clin Pract. Jun 2017; 128: 40-50.
  3. Boutayeb A, Boutayeb S. The burden of non communicable diseases in developing countries. Int J Equity Health. Jan 14 2005; 4(1): 2.
  4. DeFronzo RA. Pharmacologic therapy for type 2 diabetes mellitus. Ann Intern Med. Jul 04 2000; 133(1): 73-74.
  5. Butler AE, Janson J, Bonner-Weir S, Ritzel R, Rizza RA, Butler PC. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes. Diabetes. Jan 2003; 52(1): 102-110.
  6. Rhodes CJ. Type 2 diabetes-a matter of beta-cell life and death? Science. Jan 21 2005; 307(5708): 380-384.
  7. Effect of intensive blood-glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34). UK Prospective Diabetes Study (UKPDS) Group. Lancet. Sep 12 1998; 352(9131): 854-865.
  8. Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33). UK Prospective Diabetes Study (UKPDS) Group. Lancet. Sep 12 1998; 352(9131): 837-853.
  9. Glenney JR, Jr., Zokas L. Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J Cell Biol. Jun 1989; 108(6): 2401-2408.
  10. Glenney JR, Jr. Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus. J Biol Chem. Dec 05 1989; 264(34): 20163-20166.
  11. Nystrom FH, Chen H, Cong LN, Li Y, Quon MJ. Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells. Mol Endocrinol. Dec 1999; 13(12): 2013-2024.
  12. Cohen AW, Razani B, Wang XB et al. Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue. Am J Physiol Cell Physiol. Jul 2003; 285(1): C222-235.
  13. Yamamoto M, Toya Y, Schwencke C, Lisanti MP, Myers MG, Jr., Ishikawa Y. Caveolin is an activator of insulin receptor signaling. J Biol Chem. Oct 09 1998; 273(41): 26962-26968.
  14. Cohen AW, Combs TP, Scherer PE, Lisanti MP. Role of caveolin and caveolae in insulin signaling and diabetes. Am J Physiol Endocrinol Metab. Dec 2003; 285(6): E1151-1160.
  15. Razani B, Engelman JA, Wang XB et al. Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities. J Biol Chem. Oct 12 2001; 276(41): 38121-38138.
  16. Galbiati F, Volonte D, Engelman JA et al. Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO J. Nov 16 1998; 17(22): 6633-6648.
  17. Drab M, Verkade P, Elger M et al. Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice. Science. Sep 28 2001; 293(5539): 2449-2452.
  18. Fodor SPA. Massively Parallel Genomics. Science. 1997; 277(5324): 393-403.
  19. Dudda-Subramanya R, Lucchese G, Kanduc D, Sinha AA. Clinical applications of DNA microarray analysis. J Exp Ther Oncol. Nov-Dec 2003; 3(6): 297-304.
  20. Hamaguchi K, Gaskins HR, Leiter EH. NIT-1, a pancreatic beta-cell line established from a transgenic NOD/Lt mouse. Diabetes. Jul 1991; 40(7): 842-849.
  21. Poy MN, Eliasson L, Krutzfeldt J et al. A pancreatic islet-specific microRNA regulates insulin secretion. Nature. Nov 11 2004; 432(7014): 226-230.
  22. Halperin F, Lopez X, Manning R, Kahn CR, Kulkarni RN, Goldfine AB. Insulin augmentation of glucose-stimulated insulin secretion is impaired in insulin-resistant humans. Diabetes. Feb 2012; 61(2): 301-309.
  23. Parton RG, Simons K. The multiple faces of caveolae. Nat Rev Mol Cell Biol. Mar 2007; 8(3): 185-194.
  24. Engelman JA, Zhang XL, Galbiati F, Lisanti MP. Chromosomal localization, genomic organization, and developmental expression of the murine caveolin gene family (Cav-1, -2, and -3). Cav-1 and Cav-2 genes map to a known tumor suppressor locus (6-A2/7q31). FEBS Lett. Jun 16 1998; 429(3): 330-336.
  25. Shajahan AN, Wang A, Decker M, Minshall RD, Liu MC, Clarke R. Caveolin-1 tyrosine phosphorylation enhances paclitaxel-mediated cytotoxicity. J Biol Chem. Feb 23 2007; 282(8): 5934-5943.
  26. Jasmin JF, Frank PG, Lisanti MP. Caveolins and Caveolae. Advances in Experimental Medicine & Biology. 2005.
  27. Fagerholm S, Ortegren U, Karlsson M, Ruishalme I, Stralfors P. Rapid insulin-dependent endocytosis of the insulin receptor by caveolae in primary adipocytes. PLoS One. Jun 19 2009; 4(6): e5985.
  28. Yang Y, Tong Y, Gong M et al. Activation of PPARbeta/delta protects pancreatic beta cells from palmitate-induced apoptosis by upregulating the expression of GLP-1 receptor. Cell Signal. Feb 2014; 26(2): 268-278.
Read More
Author biographies is not available.
Crossref
Scopus
Google Scholar
Europe PMC
Download this PDF file
PDF SUPPLEMENTARY FILES
Statistic
Read Counter : 889 Download : 364

Most read articles by the same author(s)