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Characterization of the zebrafish small heat shock protein family
Author(s) -
Elicker Kimberly S,
Kurihara Tomoki,
Hutson Lara D
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a226-a
Subject(s) - zebrafish , heat shock protein , downregulation and upregulation , chaperone (clinical) , biology , microbiology and biotechnology , desmin , hspa12a , heat shock , protein family , hsf1 , hsp70 , genetics , medicine , pathology , gene , immunology , immunohistochemistry , vimentin
Heat shock proteins (HSPs), so named for their transcriptional upregulation in response to sudden temperature elevation, are best known for their roles in chaperoning nascent proteins and preventing aggregation. Many HSPs also have functions independent of their chaperone activity. A handful of degenerative diseases, including distal hereditary motor neuropathy, axonal Charcot‐Marie‐Tooth disease, and desmin‐related myopathy, are caused by mutations in specific members of the small heat shock protein (sHSP), or alpha‐crystallin, family. However, it is not clear whether these diseases are caused by abnormal development, disturbed function, protein aggregation, or some combination of the three. We are systematically characterizing the developmental and heat shock‐induced expression of the complete zebrafish sHSP family with the aim of identifying candidates for regulating development and for helping the organism recover from the effects of environmental stressors. We have identified thirteen zebrafish sHSPs nearly all of which are expressed during development. Consistent with observations in a variety of other species, only two are upregulated by heat shock. Our combined results suggest that many sHSPs may be important during normal development and for protection and recovery from environmental stress. NIH R03EY015207 and the Essel Foundation