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Enhancement of Lysine Acetylation Accelerates Wound Repair

Enhancement of Lysine Acetylation Accelerates Wound Repair

Francesco Spallotta, Chiara Cencioni, Stefania Straino, Gianluca Sbardella, Sabrina Castellano, Maurizio C Capogrossi, Fabio Martelli, Carlo Gaetano

Commun Integr Biol. 2013 Sep 1;6(5):e25466.

PMID: 24265859

Abstract:

In physiopathological conditions, such as diabetes, wound healing is significantly compromised and chronic complications, including ulcers, may occur. In a mouse model of skin repair, we recently reported that wound treatment with Sirtuin activators and class I HDAC inhibitors induced keratinocyte proliferation and enhanced healing via a nitric oxide (NO) dependent mechanism. We observed an increase in total protein acetylation in the wound area, as determined by acetylation of α-tubulin and histone H3 Lysine 9. We reasoned that this process activated cell function as well as regulated gene expression to foster tissue repair. We report here that the direct activation of P300/CBP-associated factor (PCAF) by the histone acetylase activator pentadecylidenemalonate 1b (SPV-106) induced Lysine acetylation in the wound area. This intervention was sufficient to enhance repair process by a NO-independent mechanism. Hence, an impairment of PCAF and/or other GCN5 family acetylases may delay skin repair in physiopathological conditions.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1036939384	SPV-106		1036939-38-4	Price

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