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Researchers at Mayo Clinic Detail Findings in Breast Cancer


By a News Reporter-Staff News Editor at Women's Health Weekly -- Investigators publish new report on Breast Cancer. According to news reporting originating from Rochester, Minnesota, by NewsRx correspondents, research stated, "The NAD(+)-dependent deacetylase SIRT1 is a key regulator of several aspects of metabolism and aging. SIRT1 activation is beneficial for several human diseases, including metabolic syndrome, diabetes, obesity, liver steatosis, and Alzheimer disease."

Our news editors obtained a quote from the research from Mayo Clinic, "We have recently shown that the protein deleted in breast cancer 1 (DBC1) is a key regulator of SIRT1 activity in vivo. Furthermore, SIRT1 and DBC1 form a dynamic complex that is regulated by the energetic state of the organism. Understanding how the interaction between SIRT1 and DBC1 is regulated is therefore essential to design strategies aimed to activate SIRT1. Here, we investigated which pathways can lead to the dissociation of SIRT1 and DBC1 and consequently to SIRT1 activation. We observed that PKA activation leads to a fast and transient activation of SIRT1 that is DBC1-dependent. In fact, an increase in cAMP/PKA activity resulted in the dissociation of SIRT1 and DBC1 in an AMP-activated protein kinase (AMPK)-dependent manner. Pharmacological AMPK activation led to SIRT1 activation by a DBC1-dependent mechanism. Indeed, we found that AMPK activators promote SIRT1-DBC1 dissociation in cells, resulting in an increase in SIRT1 activity. In addition, we observed that the SIRT1 activation promoted by PKA and AMPK occurs without changes in the intracellular levels of NAD(+). We propose that PKA and AMPK can acutely activate SIRT1 by inducing dissociation of SIRT1 from its endogenous inhibitor DBC1."

According to the news editors, the research concluded: "Our experiments provide new insight on the in vivo mechanism of SIRT1 regulation and a new avenue for the development of pharmacological SIRT1 activators targeted at the dissociation of the SIRT1-DBC1 complex."

For more information on this research see: Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase. Journal of Biological Chemistry, 2012;287(28):23489-501. (American Society for Biochemistry and Molecular Biology -; Journal of Biological Chemistry -

The news editors report that additional information may be obtained by contacting V. Nin, Dept. of Anesthesiology and Kogod Aging Center, Mayo Clinic, Rochester, Minnesota 55905, United States (see also Breast Cancer).

Keywords for this news article include: Oncology, Rochester, Minnesota, Deacetylase, United States, Breast Cancer, Women's Health, Enzymes and Coenzymes, North and Central America, AMP Activated Protein Kinases, Protein Serine Threonine Kinases, Phosphotransferases (Alcohol Group Acceptor), Intracellular Signaling Peptides and Proteins.

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2013, NewsRx LLC

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