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Lead-Stimulated p38MAPK-Dependent Hsp27 Phosphorylation

Toxicology and Applied Pharmacology, 2002
Lead (Pb2+) is a cytotoxic metal ion whose mechanism of action is not established. However, Pb2+ is known to interact with a wide variety of molecules involved in signal transduction. In this study the effect of Pb2+ on protein phosphorylation in bovine adrenal chromaffin cells and human SH SY5Y cells was examined.
Leal, Rodrigo B. +4 more
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Role of Hsp27 and Related Proteins

1999
Investigations of the cellular response to thermal and other types of stresses have allowed the identification of families of proteins (the heat shock or stress proteins, Hsp) whose expression is enhanced when environmental conditions become deleterious (reviewed in Georgopoulos and Welch 1993; Morimoto et al. 1994).
A.-P. Arrigo, X. Préville
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Expression of HSP27 in Hepatocellular Carcinoma.

Anticancer research, 2017
Heat-shock protein 27 (HSP27), a low molecular weight stress protein, is recognized as a molecular chaperone. The expression of HSP27 has been detected in some human tumors and while HSP27 is phosphorylated as a reresponse to stress, the function of phosphorylated HSP27 (p-HSP27) is not known.
Daimei, Eto +10 more
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Role of phospho-Hsp27 in the binding of Hsp27 with tropomyosin