SFEBES2009 Poster Presentations Diabetes, Metabolism and Cardiovascular (49 abstracts)
Visfatin regulates insulin secretion and insulin receptor phosphorylation in a clonal beta-cell line
J Brown 1 , D Onyango 2 , A Conner 1 , M Ramanjaneya 1 , S Dunmore 2 & H Randeva 1
1University of Warwick, Coventry, UK; 2University of Wolverhampton, West Midlands, UK.
Visfatin is a controversial molecule secreted from adipose tissue and known to be positively correlated with body mass. Previous reports have suggested that visfatin interacts with the insulin receptor signalling pathway. Due to its high expression in visceral fat tissue and its initial reported insulin sensitising effects it has been suggested to be involved in the pathogenesis of type 2 diabetes, although this link has yet to be well established. Since insulin receptors are expressed in pancreatic beta-cells we sought to evaluate the effects of visfatin on insulin secretion and on insulin receptor signalling in clonal pancreatic beta-cells. To do this, Beta-TC6 mouse pancreatic beta-cells were cultured in RPMI-1640 before being treated with a range of recombinant visfatin concentrations (0, 200 & 500 ng/ml for IR phosphorylation; 0–200 ng/ml for insulin secretion). Insulin signalling was measured by phospho-specific insulin receptor sandwich ELISA and phospho-specific Western blotting. Insulin secretion was measured using ultrasensitive insulin ELISA. Incubation with visfatin caused significant insulin receptor phosphorylation (P<0.001) at both 200 and 500 ng/ml. Time dependent studies showed that this increase was seen between 5 and 15 min post stimulation. Visfatin also significantly increased insulin secretion by 50% at low, but not high glucose (P<0.05). These data suggest that visfatin has a potentially important role in the regulation of beta-cell function in obesity-related diabetes and could provide novel therapeutic targets for type 2 diabetes.
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Endocrine Abstracts
ISSN 1470-3947 (print) | ISSN 1479-6848 (online)
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