期刊
ENDOCRINE
卷 31, 期 3, 页码 248-253出版社
SPRINGER
DOI: 10.1007/s12020-007-0046-3
关键词
pancreatic beta-cells; INS-1 832/13 cells; protein phosphatase 2A; glucose-stimulated insulin secretion
资金
- NIDDK NIH HHS [R01-DK74920, R01-DK56005] Funding Source: Medline
Among various phosphatases, the protein phosphatase 2A (PP2A) is relatively well studied in the islet. Previously, we have demonstrated that the catalytic subunit of PP2A (PP2Ac) undergoes okadaic acid (OKA)-sensitive, reversible carboxylmethylation (CML), which appears to be requisite for glucose-stimulated insulin secretion (GSIS). Using the siRNA approach, we examined, herein, the contributory roles of PP2Ac in GSIS from insulin-secreting pancreatic beta-(INS-1 832/13) cells. Immunologically, PP2Ac was detectable in all the subcellular fractions studied in rank order of: cytosol > microsomes > secretory granules = nucleus > mitochondria. Transfection of PP2Ac-specific, but not scrambled-siRNA, markedly attenuated PP2A activity and GSIS in these cells. Together, our findings provide a direct evidence for a positive modulatory role for PP2Ac in signaling steps leading to GSIS.
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