Dissertation/Thesis Abstract

Inositol pyrophosphate regulation of SIRT1
by Juluri, Krishna Rangadhamarao, Ph.D., The Johns Hopkins University, 2008, 72; 3309821
Abstract (Summary)

Inositol pyrophosphates have been shown to pyrophosphorylate proteins in eukaryotes in a non-enzymatic manner. We describe here that the inositol pyrophosphate diphosphoinositol pentakisphosphate (5-PP-IP7 ) can pyrophosphorylate the protein deacetylase SIRT1. In addition SIRT1 binds to the IP6 kinase enzymes that synthesize IP7 as well as inositol polyphosphate multikinase. We also demonstrate that alteration of pyrophosphate levels in mammalian cells culture can regulate SIRT1 activity towards its targets. We also generated mice in which the IP6K1 gene has been deleted. We show that these mice exhibit growth retardation, reduced insulin secretion and insulin hypersensitivity, and defects in spermiogenesis.

Indexing (document details)
Advisor: Snyder, Solomon H.
School: The Johns Hopkins University
School Location: United States -- Maryland
Source: DAI-B 69/04, Dissertation Abstracts International
Subjects: Neurosciences, Cellular biology
Keywords: Inositol pyrophosphate, Insulin secretion, Pyrophosphorylation, SIRT1
Publication Number: 3309821
ISBN: 978-0-549-57825-3
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