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Down-regulation of a Mr 90,000 Heat Shock Cognate Protein During Granulocytic Differentiation in HL-60 Human Leukemia Cells

Down-regulation of a Mr 90,000 Heat Shock Cognate Protein During Granulocytic Differentiation in HL-60 Human Leukemia Cells

Y Yufu, J Nishimura, H Takahira, H Ideguchi, H Nawata

Cancer Res. 1989 May 1;49(9):2405-8.

PMID: 2706628

Abstract:

Modulation of the synthesis of heat shock proteins in HL-60 human promyelocytic leukemia cells during differentiation was studied by metabolic labeling with [35S]methionine and Northern blot analysis. HL-60 cells were found to synthesize constitutively a high level of a Mr 90,000 protein (heat shock cognate protein, hsc90), which was very closely related to Mr 90,000 heat shock protein, hsp90, as far as molecular weight, isoelectric point, peptide maps, immunoreactivity, and encoded mRNA were concerned. Differentiation induction by dimethyl sulfoxide markedly decreased the level of the hsc90 expression, but preserved the ability to preferentially express hsp90 in response to heat stress. These results suggest distinct regulatory mechanisms of the synthesis between hsc90 and hsp90 although they are indistinguishable by conventional protein or mRNA analysis, and indicate that hsc90 has some role in cell growth and differentiation.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241044	Heat Shock Protein 60 human			Price

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