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Proteomic analysis of the INS‐1E secretome identify novel vitamin D‐regulated proteins
Author(s) -
Pepaj Milaim,
Bredahl May K.,
Gjerlaugsen Nina,
Thorsby Per M.
Publication year - 2016
Publication title -
diabetes/metabolism research and reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.307
H-Index - 110
eISSN - 1520-7560
pISSN - 1520-7552
DOI - 10.1002/dmrr.2777
Subject(s) - stable isotope labeling by amino acids in cell culture , gelsolin , exocytosis , cell growth , secretory protein , vitamin , proteomics , biology , vitamin d and neurology , quantitative proteomics , biochemistry , cell culture , chemistry , microbiology and biotechnology , secretion , endocrinology , actin , gene , genetics
Abstract Background Experimental evidence indicates that vitamin D may have a beneficial role in pancreatic β‐cell function. Methods In the present study, stable isotope labelling by amino acids in cell culture (SILAC) in combination with liquid chromatography–tandem mass spectrometry was used to quantitatively assess the impact of the active vitamin D metabolite, 1,25‐(OH) 2 D 3 , on global protein expression in INS‐1E cell secretome. Results Twenty‐one proteins were found up‐regulated (≥1.5 fold changes) and three down‐regulated (≤0.67) after treatment of INS‐1E cells with 1,25‐(OH) 2 D 3 . Up‐regulation of proteins implicated in β‐cell growth and proliferation, such as IGF2, IGFBP7 and gelsolin, suggest that 1,25‐(OH) 2 D 3 has a positive effect on β‐cell growth and proliferation. Moreover, modulations of several proteins implicated in prohormone processing and insulin exocytosis (IGF2, IGFBP7, Scg5, ProSAAS, Fabp5, Ptprn2 and gelsolin) appear to support the hypothesis that 1,25‐(OH) 2 D 3 plays positive modulatory role in insulin processing and secretion. Conclusions Together, we reveal a number of novel vitamin D‐regulated proteins that may contribute to a better understanding of the reported beneficial effects of vitamin D on pancreatic β‐cells. Copyright © 2016 John Wiley & Sons, Ltd.

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