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J Biol Chem, Vol. 275, Issue 2, 1095-1104, January 14, 2000
From the Previously, we identified a new
mammalian sHSP, MKBP, as a myotonic dystrophy protein kinase-binding
protein, and suggested its important role in muscle maintenance
(Suzuki, A., Sugiyama, Y., Hayashi, Y., Nyu-i, N., Yoshida, M., Nonaka,
I., Ishiura, S., Arahata, K., and Ohno, S. (1998) J. Cell
Biol. 140, 1113-1124). In this paper, we develop the former work
by performing extensive characterization of five of the six sHSPs so
far identified, that is, HSP27,
Muscle Develops a Specific Form of Small Heat Shock Protein
Complex Composed of MKBP/HSPB2 and HSPB3 during Myogenic
Differentiation*
,§,,,,
, and**
Department of Molecular Biology, Yokohama
City University School of Medicine, Kanazawa-ku, Yokohama 236-0004, Japan, the ¶ Department of Biochemistry, The Chinese University of
Hong Kong, Shatin, N.T., Hong Kong, and the Department of
Pathology and Tumor Biology, Graduate School of Medicine, Kyoto
University, Sakyo-ku, Kyoto 606-8501, Japan
B-crystallin, p20, MKBP/HSPB2, and
HSPB3, omitting lens-specific A-crystallin. Tissue distribution
analysis revealed that although each sHSP shows differential
constitutive expression in restricted tissues, tissues that express all
five sHSPs are only muscle-related tissues. Especially, the expressions
of HSPB3, identified for the first time as a 17-kDa protein in this
paper, and MKBP/HSPB2 are distinctly specific to muscles. Moreover,
these sHSPs form an oligomeric complex with an apparent molecular mass of 150 kDa that is completely independent of the oligomers formed by
HSP27, B-crystallin, and p20. The expressions of MKBP/HSPB2 and
HSPB3 are induced during muscle differentiation under the control of
MyoD, suggesting that the sHSP oligomer comprising MKBP/HSPB2 and HSPB3
represents an additional system closely related to muscle function. The
functional divergence among sHSPs in different oligomers is also
demonstrated in several ways: 1) an interaction with myotonic dystrophy
protein kinase, which has been suggested to be important for the
maintenance of myofibril integrity, was observed only for MKBP/HSPB2;
2) a myotube-specific association with actin bundles was observed for
HSP27 and B-crystallin, but not for MKBP/HSPB2; and 3) sHSPs whose
mRNAs are induced by heat shock are B-crystallin and HSP27.
Taken together, the results suggest that muscle cells develop two kinds
of stress response systems composed of diverged sHSP members, and that
these systems work independently in muscle maintenance and differentiation.
*
This work was supported by Grant 8A-1 from the National
Center of Neurology and Psychiatry of the Ministry of Health and
Welfare and Grant 09770103 from the Ministry of Education, Science,
Culture, and Sports, Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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