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Tributyltin is a potent inducer of the heat shock response in human diploid fibroblasts
Author(s) -
Zhang Hua,
Liu Alice Y.C.
Publication year - 1992
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041530304
Subject(s) - tributyltin , hsp70 , inducer , heat shock protein , heat shock , electrophoretic mobility shift assay , heat shock factor , gene expression , microbiology and biotechnology , shock (circulatory) , heme oxygenase , transcription (linguistics) , messenger rna , chemistry , biology , heme , biochemistry , gene , enzyme , medicine , philosophy , organic chemistry , linguistics
Submicromolar concentrations of tributyltin (TBT), a commercially used organotin compound, were found to induce the expression of several stress proteins, most notably HSP89 and HSP70, in IMR‐90 human diploid fibroblats in a time‐ and dose‐dependent manner. This induction can be demonstrated by quantitation of 1) synthesis of the heat shock proteins (HSPs), 2) relative abundance of mRNA of hsp70, and 3) transient expression of a human hsp70 promoter driven reporter gene. TBT also increased the abundance of mRNA of heme oxygenase, whereas heat shock was without effect. Analysis of protein binding to a consensus heat shock element (HSE)by electrophoretic mobility shift assay suggests that the induction of the heat shock response by TBT was attributable to activation of the heat shock transcription factor (HSTF). © 1992 Wiley‐Liss, Inc.