Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve.

Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve. Research Abstract Details 

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Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve. Abstract Text:

Peter Matt,Zongming Fu,Thierry Carrel,David L Huso,Stefan Dirnhofer,Ivan Lefkovits,Hans-Reinhard Zerkowski,Jennifer E Van Eyk,Peter Matt,Zongming Fu,Thierry Carrel,David L Huso,Stefan Dirnhofer,Ivan Lefkovits,Hans-Reinhard Zerkowski,Jennifer E Van Eyk,Peter Matt,Zongming Fu,Thierry Carrel,David L Huso,Stefan Dirnhofer,Ivan Lefkovits,Hans-Reinhard Zerkowski,Jennifer E Van Eyk,

Whether or not there are molecular differences, at the intra- and extracellular level, between aortic dilatation in patients with bicuspid (BAV) and those with a tricuspid aortic valve (TAV) has remained controversial for years. We have performed 2-dimensional gel electrophoresis and mass spectrometry coupled with dephosphorylation and phosphostaining experiments to reveal and define protein alterations and the high abundant structural phosphoproteins in BAV compared to TAV aortic aneurysm samples. 2-D gel patterns showed a high correlation in protein expression between BAV and TAV specimens (n=10). Few proteins showed significant differences, among those a phosphorylated form of heat shock protein (HSP) 27 with significantly lower expression in BAV compared to TAV aortic samples (p=0.02). The phosphoprotein tracing revealed four different phosphoproteins including Rho GDP dissociation inhibitor 1, calponin 3, myosin regulatory light chain 2 and four differentially phosphorylated forms of HSP27. Levels of total HSP27 and dually phosphorylated HSP27 (S78/S82) were investigated in an extended patient cohort (n=15) using ELISA. Total HSP27 was significantly lower in BAV compared to TAV patients (p=0.03), with no correlation in levels of phospho-HSP27 (S78/S82) (p=0.4). Western blots analysis showed a trend towards lower levels of phospho-HSP27 (S78) in BAV patients (p=0.07). Immunohistochemical analysis revealed that differences in HSP27 occur in the cytoplasma of VSMC's and not extracellularly. Alterations in HSP27 may give early evidence for intracellular differences in aortic aneurysm of patients with BAV and TAV. Whether HSP27 and the defined phosphoproteins have a specific role in BAV associated aortic dilatation remains to be elucidated.

Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve. Publishing Authors By Initials

P Matt,Z Fu,T Carrel,DL Huso,S Dirnhofer,I Lefkovits,HR Zerkowski,JE Van Eyk,P Matt,Z Fu,T Carrel,DL Huso,S Dirnhofer,I Lefkovits,HR Zerkowski,JE Van Eyk,P Matt,Z Fu,T Carrel,DL Huso,S Dirnhofer,I Lefkovits,HR Zerkowski,JE Van Eyk,

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Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of molecular and cellular cardiology

VOLUME: 43

Page Numbers: 792-801

Journal Abbreviation: J. Mol. Cell. Cardiol.

ISSN: 0022-2828

DAY: 28

MONTH: 08

YEAR: 2007

Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve. Information

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LANGUAGE: eng

NlmUniqueID: 262322

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Grant and Affiliation Information for Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve.

AFFILIATION: Johns Hopkins Bayview Proteomics Center, Department of Medicine, Johns Hopkins University, 5200 Eastern Avenue, Baltimore, MD 21224, USA. pmatt1@jmhi.edu

Country: England

AGENCY: United States NHLBI

GRANT: HV 28120

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MEDLINETA: J Mol Cell Cardiol

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