NDLI: Structure, Properties, and Probable Physiological Role of Small Heat Shock Protein with Molecular Mass 20 kD (Hsp20, HspB6)

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Structure, Properties, and Probable Physiological Role of Small Heat Shock Protein with Molecular Mass 20 kD (Hsp20, HspB6)

Content Provider	Springer Nature Link
Author	Gusev, N. B. Bukach, O. V. Marston, S. B.
Copyright Year	2005
Abstract	This review is devoted to critical analysis of data concerning the structure and functions of small heat shock proteins with apparent molecular mass 20 kD (Hsp20). We describe the structure of Hsp20, its phosphorylation by different protein kinases, interaction of Hsp20 with other small heat shock proteins, and chaperone activity of Hsp20. The distribution of Hsp20 in different animal tissues and the factors affecting expression of Hsp20 are also described. Data on the possible involvement of Hsp20 in regulation of platelet aggregation and glucose transport are presented and analyzed. Special attention is paid to literature data describing probable regulatory effect of Hsp20 on contraction of smooth muscle. Two hypotheses postulating direct effect of Hsp20 on actomyosin interaction or its effect on cytoskeleton are compared and analyzed. The most recent data on the effect of Hsp20 on apoptosis and contractile activity of cardiomyocytes are also presented.
Starting Page	629
Ending Page	637
Page Count	9
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	70
Issue Number	6
e-ISSN	16083040
Language	English
Publisher	Nauka/Interperiodica
Publisher Date	2005-01-01
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	small heat shock proteins phosphorylation chaperone activity apoptosis contractile activity of smooth and skeletal muscles Biomedicine general Bioorganic Chemistry Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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