Identification and molecular characterization of a high‐affinity cardiomyocyte transforming growth factor‐β2 receptor

FEBS Letters

Hreniuk, David¹  Ross, Julie¹  Janero, David R.¹ 

[1]Research Department, Cardiovascular-Atherosclerosis Research, CIBA-GEIGY Corp., Pharmaceuticals Division, Summit, NJ 07901, USA

关键词: Transforming growth factor-β;    Cardiomyocyte;    Heart muscle;    Cytokine;    Receptor;    Affinity labeling;    aFGF;    acidic fibroblast growth factor;    BME;    Eagle's basal medium;    BSA;    bovine serum albumin;    DSS;    disuccinimidyl suberate;    EDTA;    ethylene diaminetetraacetic acid;    HEPES;    N-2-hy-droxyethylpiperazine-N'-2-ethanesulfonic acid;    PDGF;    platelet derived growth factor;    PMSF;    phenylmethanesulfonyl fluoride;    TGF-β;    transforming growth factor-β;    Tris;    tris(hydroxymethyl)aminomethane;   

DOI  :  10.1016/0014-5793(93)80592-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rat neonatal heart muscle cells (cardiomyocytes) were found to express a high-affinity surface receptor for transforming growth factor-β2 (TGF-β2). Specific binding was rapid, saturable, ligand-selective, and reversible. Equilibrium binding analyses revealed that the cardiomyocyte had one class of specific binding sites with a K _d ⩽ 26 pM TGF-β2, a B _max of ~9 fmol/10⁶cells, and ~5,000 binding sites/cardiomyocyte. Binding was selective for TGF-β2 in comparison to other TGF-β isoforms and to unrelated growth factors. Affinity-binding experiments revealed three types of cardiomyocyte TGF-β2 binding proteins, the most prominent of which corresponded to the high-molecular mass proteoglycan. These data raise the possibility that the anti-ischemic cardioprotective effects ofTGF-β may reflect receptor-mediated signal transduction at the cardiomyocyte level.

【 授权许可】

Unknown