The common 90-kd protein component of non-transformed '8S' steroid receptors is a heat-shock protein.

来自 NCBI

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作者：

MG Catelli，N Binart，I Jung-Testas，JM Renoir，EE Baulieu，JR Feramisco，WJ Welch

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摘要：

Non-transformed steroid receptors have an approximately 8S sedimentation coefficient that corresponds to an oligomeric structure of 250-300 kd which includes a non-hormone binding 90-kd protein. A monoclonal antibody BF4 raised against the purified, molybdate-stabilized, 8S progesterone receptor (8S-PR) from chick oviduct, recognizes 8S forms of all steroid hormone receptors. BF4 was found specific for a 90-kd protein present in great abundance in all chicken tissues, including that present in 8S-forms of steroid receptors. Here, using immunological and biochemical techniques, we demonstrate that this ubiquitous BF4-positive 90-kd protein is in fact the chicken 90 kd heat-shock protein (hsp 90): it increased in heat-shocked chick embryo fibroblasts, and displayed identical migration in two-dimensional gel electrophoresis and the same V8 peptide map as the already described hsp 90. We discuss the possibility that the interaction between hsp 90 and steroid hormone-binding subunits may play a role in keeping the receptor in an inactive form.

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关键词：

Linkage helicity magnetohydrodynamics solar magnetism

DOI：

10.1089/dna.1985.4.469

被引量：

765

年份：

1985