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Structure, function, property, and role in neurologic diseases and other diseases of the sHsp22
Author(s) -
Hu Zhiping,
Chen Lan,
Zhang Jie,
Li Ting,
Tang Jianguang,
Xu Niangui,
Wang Xiang
Publication year - 2007
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.21231
Subject(s) - heat shock protein , chaperone (clinical) , monomer , microbiology and biotechnology , hsp70 , structural motif , chemistry , protein structure , superfamily , protein folding , family member , biology , biochemistry , genetics , receptor , medicine , gene , organic chemistry , family medicine , pathology , polymer
Small heat shock proteins are members of the heat shock proteins family. They share important identical features: 1) they form the conserved structure ‘α‐crystallin domain’ with about 80–100 residues in the C‐terminal part of the proteins; 2) they have monomeric molecular masses ranging in 12–43 kDa; 3) they associate into large oligomers consisting in many cases of subunits; 4) they increase expression under stress conditions; 5) they exhibit a highly dynamic structure; and 6) they play a chaperone‐like role. Hsp22 (also known as HspB8, H11, and E2IG1) retains the structural motif of the ‘α‐crystallin’ family of Hsps and is a member of the superfamily of sHsps. Hsp22 displays chaperone activity, autokinase activity, and trigger or block apoptosis activity. It differs from canonical family members existing as a monomer. A decrease in the HspB8 activity may contribute to the development of some neurologic diseases and others. © 2007 Wiley‐Liss, Inc.