Abstract:
:Stimulation of insulin secretion is accompanied by changes in the phosphorylation state of several islet polypeptides. Protein (de)phosphorylation is mediated by the action of protein kinases and phosphoprotein phosphatases. In this study we have investigated expression of phospho-serine/threonine phosphatases (PPs) in rat islets of Langerhans and studied the role of these enzymes in the regulation of insulin secretion. PP1, PP2A and PP2B were identified in rat islets and high levels of PP1/2A activities were detected. Inhibition of PP1/2A markedly inhibited glucose-stimulated insulin secretion, whilst glucose increased islet PP1/2A activities in situ. Insulin secretion at basal glucose was unaffected by inhibitors of PP1/2A. Inhibition of PP2B had no effect on either basal or glucose stimulated insulin secretion. These results suggest that PP1/2A are stimulated by glucose in rat islets and the presence of active PP1/2A is required for stimulation of insulin secretion by glucose.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Murphy LI,Jones PMdoi
10.1016/0303-7207(95)03747-0subject
Has Abstractpub_date
1996-03-25 00:00:00pages
195-202issue
2eissn
0303-7207issn
1872-8057pii
0303720795037470journal_volume
117pub_type
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journal_title:Molecular and cellular endocrinology
pub_type: 杂志文章
doi:10.1016/j.mce.2019.01.012
更新日期:2019-03-15 00:00:00