PMID- 10625651 OWN - NLM STAT- MEDLINE DCOM- 20000218 LR - 20210209 IS - 0021-9258 (Print) IS - 0021-9258 (Linking) VI - 275 IP - 2 DP - 2000 Jan 14 TI - Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. PG - 1095-104 AB - 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, alphaB-crystallin, p20, MKBP/HSPB2, and HSPB3, omitting lens-specific alphaA-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, alphaB-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 alphaB-crystallin, but not for MKBP/HSPB2; and 3) sHSPs whose mRNAs are induced by heat shock are alphaB-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. FAU - Sugiyama, Y AU - Sugiyama Y AD - Department of Molecular Biology, Yokohama City University School of Medicine, Kanazawa-ku, Yokohama 236-0004, Japan. FAU - Suzuki, A AU - Suzuki A FAU - Kishikawa, M AU - Kishikawa M FAU - Akutsu, R AU - Akutsu R FAU - Hirose, T AU - Hirose T FAU - Waye, M M AU - Waye MM FAU - Tsui, S K AU - Tsui SK FAU - Yoshida, S AU - Yoshida S FAU - Ohno, S AU - Ohno S LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (Carrier Proteins) RN - 0 (Crystallins) RN - 0 (HSP27 Heat-Shock Proteins) RN - 0 (HSPB2 protein, human) RN - 0 (HSPB3 protein, human) RN - 0 (Heat-Shock Proteins) RN - 0 (Hspb2 protein, mouse) RN - 0 (Hspb2 protein, rat) RN - 0 (RNA, Messenger) RN - 0 (Recombinant Proteins) SB - IM MH - Adult MH - Animals MH - Carrier Proteins/*genetics/*metabolism MH - Cell Differentiation MH - Cell Line MH - Crystallins/genetics MH - Female MH - Gene Expression Regulation MH - Gene Library MH - HSP27 Heat-Shock Proteins MH - Heat-Shock Proteins/*genetics/*metabolism MH - Humans MH - Male MH - Mammals MH - Mice MH - Muscle, Skeletal/cytology/*metabolism MH - Organ Specificity MH - RNA, Messenger/genetics MH - Rats MH - Recombinant Proteins/metabolism MH - Reverse Transcriptase Polymerase Chain Reaction MH - Sequence Alignment MH - Sequence Homology, Amino Acid MH - Transcription, Genetic MH - Transfection EDAT- 2000/01/08 09:00 MHDA- 2000/02/26 09:00 CRDT- 2000/01/08 09:00 PHST- 2000/01/08 09:00 [pubmed] PHST- 2000/02/26 09:00 [medline] PHST- 2000/01/08 09:00 [entrez] AID - 10.1074/jbc.275.2.1095 [doi] AID - S0021-9258(18)31223-7 [pii] PST - ppublish SO - J Biol Chem. 2000 Jan 14;275(2):1095-104. doi: 10.1074/jbc.275.2.1095.