Defective association of dystrophin with sarcolemmal glycoproteins in the cardiomyopathic hamster heart

FEBS Letters

Ozawa, Eijro¹  Yoshida, Mikiharu¹  Iwata, Yuko²  Shigekawa, Munekazu²  Mizuno, Yuji¹  Nakamura, Hiroshi² 

[1] Division of Cell Biology, National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187, Japan;Department of Molecular Physiology, National Cardiovascular Center Research Institute, Osaka 565, Japan

关键词: Cardiomyopathy;    Cardiomyopathic hamster;    Dystrophin;    Dystrophin-associated glycoprotein;    Muscular dystrophy;    DMD;    Duchenne muscular dystrophy;    TCA;    trichloroacetic acid;    WGA;    wheat germ agglutinin;    LBP;    laminin binding protein;    NAG;    N-acetyl-d-glucosaniine;   

DOI  :  10.1016/0014-5793(93)80227-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In ventricular muscle from 30- to 60-day-old Bio 14.6 cardiomyopathic hamsters, dystrophin-associated glycoproteins of 43, 50 and 150 kDa are markedly reduced in abundance. In particular, the 50-kDa glycoprotein is totally deficient in the sareolemma of myopathic ventricular myocytes as revealed by immunofluorescence microscopy. The dystrophin-glycoprotein complex formation is defective in the cardiomyopathic hamster heart, because dystrophin and the glycoproteins behave independently when digitonin-solubilized ventricular homogenates are fractionated on wheat germ agglutinin beads or anti-dystrophin immunoaffinity beads.

【 授权许可】

Unknown