Activation of Histone Deacetylase-6 (HDAC6) Induces Contractile Dysfunction through Derailment of -Tubulin Proteostasis in Experimental and Human Atrial Fibrillation
نویسندگان
چکیده
Dept of Clinical Pharmacology, University Medical Center Groningen, University of Groningen, The Netherlands; Research Center and Dept of Medicine; Montreal Heart Institute and Université de Montréal, Montreal, Canada; Chang-Gung Memorial Hospital and ChangGung University, Taoyuan, Taiwan, Republic of China; Nyken BV, Groningen, The Netherlands; Ankara University Biotechnology Institute, Ankara, Turkey; Ankara University Stem Cell Institute, Ankara, Turkey; Dept of Cardiovascular Surgery, Ankara University School of Medicine, Turkey; Dept of Cell Biology, University Medical Center Groningen, University of Groningen, The Netherlands; Dept of Pharmacology, McGill University, Montreal, Canada
منابع مشابه
Activation of histone deacetylase-6 induces contractile dysfunction through derailment of α-tubulin proteostasis in experimental and human atrial fibrillation.
BACKGROUND Atrial fibrillation (AF) is characterized by structural remodeling, contractile dysfunction, and AF progression. Histone deacetylases (HDACs) influence acetylation of both histones and cytosolic proteins, thereby mediating epigenetic regulation and influencing cell proteostasis. Because the exact function of HDACs in AF is unknown, we investigated their role in experimental and clini...
متن کاملHighly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate.
To find novel histone deacetylase 6 (HDAC6)-selective inhibitors and clarify the structural requirements for HDAC6-selective inhibition, we prepared thiolate analogues designed based on the structure of an HDAC6-selective substrate and evaluated the histone/alpha-tubulin acetylation selectivity by Western blot analysis. Aliphatic compounds 17b-20b selectively caused alpha-tubulin acetylation ov...
متن کاملModulation of histone deacetylase 6 (HDAC6) nuclear import and tubulin deacetylase activity through acetylation.
The reversible acetylation of histones and non-histone proteins by histone acetyltransferases and deacetylases (HDACs) plays a critical role in many cellular processes in eukaryotic cells. HDAC6 is a unique histone deacetylase with two deacetylase domains and a C-terminal zinc finger domain. HDAC6 resides mainly in the cytoplasm and regulates many important biological processes, including cell ...
متن کاملHistone Deacetylase 6 (HDAC6) Is an Independent Deacetylase for -Tubulin
Histone deacetylase 6 (HDAC6) is a cytosolic enzyme that catalyzes deacetylation of several proteins. Acetylated tubulin has been recently identified as a physiological substrate of HDAC6. However in previous reports, all in vitro binding and enzymatic assays were accomplished with only partially purified protein samples. Therefore, it still remained unclear whether HDAC6 alone could interact w...
متن کاملHDAC6 Deacetylase Activity Is Required for Hypoxia-Induced Invadopodia Formation and Cell Invasion
Despite significant progress in the cancer field, tumor cell invasion and metastasis remain a major clinical challenge. Cell invasion across tissue boundaries depends largely on extracellular matrix degradation, which can be initiated by formation of actin-rich cell structures specialized in matrix degradation called invadopodia. Although the hypoxic microenvironment within solid tumors has bee...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2013