Structure, function, property, and role in neurologic diseases and other diseases of the sHsp22.
Small heat shock proteins are members of the heat shock proteins family. They share important identical features: 1) they form the conserved structure 'alpha-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 'alpha-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.
Hu
Zhiping
Z
Department of Neurology of the Second Xiangya Hospital, Central South University, Changsha Hunan, Republic of China.
Chen
Lan
L
Zhang
Jie
J
Li
Ting
T
Tang
Jianguang
J
Xu
Niangui
N
Wang
Xiang
X
D000818:Animals; D002545:Brain Ischemia / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones; D015394:Molecular Structure; D009154:Mutation; D017202:Myocardial Ischemia / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism*; D009422:Nervous System Diseases / Q000209:etiology / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D015427:Reperfusion Injury / Q000378:metabolism*; D013329:Structure-Activity Relationship
C413214:HSPB8 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D017346:Protein Serine-Threonine Kinases