Phosphorylation and nuclear translocation of serine 722 and serine 910 of focal adhesion kinase in hypertrophic cardiac myocytes of left ventricle of spontaneously hypertensive rats.
- Author:
Ling ZHONG
1
;
Xian-Ping YI
;
Zhan-Yu LI
;
Li FAQIAN
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Cardiomegaly; enzymology; metabolism; Cell Nucleus; enzymology; metabolism; Focal Adhesion Kinase 1; metabolism; Focal Adhesion Protein-Tyrosine Kinases; metabolism; physiology; Heart Failure; Heart Ventricles; pathology; Hypertension; enzymology; Hypertrophy; enzymology; Myocytes, Cardiac; enzymology; pathology; Phosphorylation; Protein Transport; drug effects; physiology; Rats; Rats, Inbred SHR; Rats, Inbred WKY; Serine; metabolism; Signal Transduction; drug effects; physiology
- From: Chinese Journal of Pathology 2008;37(5):328-332
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the role of focal adhesion kinase (FAK) in cardiac hypertrophy induced by hypertension.
METHODSUsing immunofluorescent labeling, confocal microscopy and Western blot, the expression and subcellular location of FAK-pSer722 and FAK-pSer910 were determined in cardiac myocytes of the left ventricles from 2, 6, 12, and 18 month-old spontaneously hypertensive heart failure (SHHF) rats and age-matched Wistar-Kyoto (WKY) control rats, respectively.
RESULTSThere was no obvious difference in FAK-pSer722 and FAK-pSer910 expression between 2 month-old SHHF and WKY rats. In contrast with the control groups, the expression of FAK-pSer722 and FAK-pSer910 significantly increased in cardiac myocytes of the left ventricle, from 6, 12 and 18 month-old SHHF rats. Both FAK-pSer722 and FAK-pSer910 were translocated and acummulated in nuclei of cardiac myocytes from 6, 12, and 18 month-old SHHF rats.
CONCLUSIONPhosphorylation and translocation of serine 722 and serine 910 of phosphorylated FAK play an important role in the de-compensatory cardiac hypertrophy.
