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Dual role of proapoptotic BAD in insulin secretion and beta cell survival


By JPGRAY - Posted on 24 February 2009

TitleDual role of proapoptotic BAD in insulin secretion and beta cell survival
Publication TypeJournal Article
Year of Publication2008
AuthorsDanial NN, Walensky LD, Zhang CY, Choi CS, Fisher JK, Molina AJ, Datta SR, Pitter KL, Bird GH, Wikstrom JD, Deeney JT, Robertson K, Morash J, Kulkarni A, Neschen S, Kim S, Greenberg ME, Corkey BE, Shirihai OS, Shulman GI, Lowell BB, Korsmeyer SJ
JournalNat Med
Volume14
Issue2
Pagination144-53
Date PublishedFeb
Publication Languageeng
ISBN Number1546-170X (Electronic)
Accession Number18223655
Key WordsGlucokinase/metabolism, Diet, Cell Survival/drug effects, Cell Count, Calcium/metabolism, Blood Glucose, Animals, Amino Acid Sequence, bcl-Associated Death Protein/chemistry/deficiency/*metabolism, Protein Structure, Tertiary, Phosphoserine/metabolism, Peptides/pharmacology, Molecular Sequence Data, Models, Genetic, Mice, Membrane Potential, Mitochondrial/drug effects, Insulin-Secreting Cells/*cytology/drug effects/enzymology/*secretion, Insulin/*secretion, Hydrocarbons/pharmacology, Humans, Glucose/pharmacology
Abstract

The proapoptotic BCL-2 family member BAD resides in a glucokinase-containing complex that regulates glucose-driven mitochondrial respiration. Here, we present genetic evidence of a physiologic role for BAD in glucose-stimulated insulin secretion by beta cells. This novel function of BAD is specifically dependent upon the phosphorylation of its BH3 sequence, previously defined as an essential death domain. We highlight the pharmacologic relevance of phosphorylated BAD BH3 by using cell-permeable, hydrocarbon-stapled BAD BH3 helices that target glucokinase, restore glucose-driven mitochondrial respiration and correct the insulin secretory response in Bad-deficient islets. Our studies uncover an alternative target and function for the BAD BH3 domain and emphasize the therapeutic potential of phosphorylated BAD BH3 mimetics in selectively restoring beta cell function. Furthermore, we show that BAD regulates the physiologic adaptation of beta cell mass during high-fat feeding. Our findings provide genetic proof of the bifunctional activities of BAD in both beta cell survival and insulin secretion.

Notes

5K08HL074049/HL/NHLBI NIH HHS/United States5R01CA50239/CA/NCI NIH HHS/United States5R01DK68781/DK/NIDDK NIH HHS/United StatesK01CA10659/CA/NCI NIH HHS/United StatesJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov'tUnited States

URLhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18223655
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