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First published online October 30, 2006

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Pumping out insulin

The slightly acidic nature of secretory granules is necessary for the efficient processing and subsequent exocytosis of their contents. Vacuolar-type H⁺-ATPase (V-ATPase) is thought to acidify many intracellular compartments. Now, on p. 4531, Ge-Hong Sun-Wada and co-authors report that the a3 isoform of this multisubunit enzyme helps to regulate insulin secretion. Mammalian cells express four isoforms of the a subunit of V-ATPase. The authors show that V-ATPase containing the a3 isoform is highly expressed in pancreatic islets and localizes to the membranes of the insulin-containing granules in the ß-cells that secrete the hormone. Mice lacking the a3 isoform, they report, have less insulin in their blood than wild-type mice but a near-normal amount of insulin in their islets and a normal insulin-to-proinsulin ratio in their secretory granules. Other experiments reveal that islets isolated from the a3-null mice exhibit impaired insulin secretion in response to glucose. The gene encoding human a3 maps to a chromosome region linked to insulin-dependent diabetes mellitus; so the authors speculate that mutations in it may be involved in diabetes.

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Related articles in JCS:

The a3 isoform of V-ATPase regulates insulin secretion from pancreatic ß-cells

Ge-Hong Sun-Wada, Takao Toyomura, Yoshiko Murata, Akitsugu Yamamoto, Masamitsu Futai, and Yoh Wada
JCS 2006 119: 4531-4540. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?