Association of the chaperone alphaB-crystallin with titin in heart muscle.

Journal article

alphaB-crystallin, a major component of the vertebrate lens, is a chaperone belonging to the family of small heat shock proteins. These proteins form oligomers that bind to partially unfolded substrates and prevent denaturation. alphaB-crystallin in cardiac muscle binds to myofibrils under conditions of ischemia, and previous work has shown that the protein binds to titin in the I-band of cardiac fibers (Golenhofen, N., Arbeiter, A., Koob, R., and Drenckhahn, D. (2002) J. Mol. Cell. Cardiol. ...

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Authors: Bullard, B; Ferguson, C; Minajeva, A; Leake, M; Gautel, M

• Journal: Journal of biological chemistry
• Volume: 279
• Issue: 9
• Pages: 7917-7924
• Publication date: 2004-02-01
• DOI: 10.1074/jbc.m307473200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Microscopy, Fluorescence; Microscopy, Immunoelectron; Circular Dichroism; Myocardium; Rabbits; Electrophoresis, Polyacrylamide Gel; Humans; Recombinant Proteins; Sarcomeres; Protein Kinases; Binding Sites; Animals; Drug Stability; alpha-Crystallin B Chain; Protein Folding; Myofibrils; Immunoglobulins; Muscle Proteins; Peptide Fragments