The 90 000 dalton heat shock protein, a lot of smoke but no function as yet

1989 ◽  
Vol 67 (11-12) ◽  
pp. 749-750 ◽  
Author(s):  
Boyd Hardesty ◽  
Gisela Kramer
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein A

Increased expression of collagen-binding heat shock protein 47 in murine bleomycin-induced pneumopathy

2003 ◽  
Vol 285 (4) ◽  
pp. L957-L963 ◽  
Author(s):  
Hiroshi Ishii ◽  
Hiroshi Mukae ◽  
Tomoyuki Kakugawa ◽  
Tetsuji Iwashita ◽  
Hideyuki Kaida ◽  
...  
Keyword(s):  
Heat Shock ◽  
Pulmonary Fibrosis ◽  
Heat Shock Protein ◽  
Smooth Muscle Actin ◽  
Protein A ◽  
Immunohistochemical Analysis ◽  
Rt Pcr ◽  
Heat Shock Protein 47 ◽  
Positive Type ◽  
Fibrotic Process

The 47-kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen. Expression of HSP47 has been reported to increase in parallel with expression of collagens during the progression of various fibrosis models. The aim of the present study was to investigate the association between HSP47 expression and collagen accumulation in bleomycin (BLM)-induced murine fibrosis. We investigated the expression of HSP47 protein and mRNA using immunohistochemical analysis and semi-quantitative RT-PCR in murine BLM-induced pulmonary fibrosis. Immunohistochemical analysis showed that higher expression of HSP47 protein was present in BLM-induced pulmonary fibrosis compared with controls. HSP47 was localized predominantly in α-smooth muscle actin-positive myofibroblasts, F4/80 negative, surfactant protein-A-positive type II pneumocytes, and F4/80-positive macrophages. RT-PCR also demonstrated an increase of HSP47 mRNA expression in BLM-treated lungs. Moreover, the relative amounts of HSP47 mRNA correlated significantly with the lung hydroxyproline content as an indicator of pulmonary fibrosis in BLM-treated lungs ( r = 0.406, P <0.05). Our results suggest that these cells may play a role in the fibrotic process of BLM-treated lungs through upregulation of HSP47.

IS HEAT SHOCK PROTEIN A POTENTIAL PROTECTIVE MECHANISM AGAINST ISCHEMIA-REPERFUSION INJURY?

1999 ◽  
Vol 103 (1) ◽  
pp. 336-337 ◽  
Author(s):  
Sean Lille ◽  
Ching-Yuan Su ◽  
Michael Neumeister ◽  
Robert C. Russell ◽  
Chen-Ching Lai
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Protein A ◽  
Protective Mechanism

scholarly journals A Histidine-rich and Cysteine-rich Metal-binding Domain at the C Terminus of Heat Shock Protein A fromHelicobacter pylori

2008 ◽  
Vol 283 (22) ◽  
pp. 15142-15151 ◽  
Author(s):  
Shujian Cun ◽  
Hongyan Li ◽  
Ruiguang Ge ◽  
Marie C. M. Lin ◽  
Hongzhe Sun
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Metal Binding ◽  
Protein A ◽  
Binding Domain ◽  
C Terminus ◽  
Metal Binding Domain

scholarly journals Chemical modifications of a recombinant bovine stress-inducible 70 kDa heat-shock protein (Hsp70) mimics Hsp70 isoforms from tissues

1995 ◽  
Vol 305 (1) ◽  
pp. 197-203 ◽  
Author(s):  
J A Gutierrez ◽  
V Guerriero
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Expression System ◽  
Protein A ◽  
Two Dimensional Gel Electrophoresis ◽  
Calculated Molecular Mass ◽  
Reading Frame ◽  
Heat Shock Protein Hsp70 ◽  
Bovine Skeletal Muscle

A cDNA clone for the stress-inducible 70 kDa heat-shock protein (Hsp70) has been isolated from a bovine skeletal-muscle cDNA library. This mRNA encodes a protein with a calculated molecular mass of 70250 Da. The cDNA has one continuous open reading frame capable of encoding a 641-amino-acid protein. Expression of this cDNA in a bacterial expression system produced a protein with a mobility identical with that of the inducible Hsp70 protein from bovine skeletal muscle as determined by SDS/PAGE. Two-dimensional gel electrophoresis demonstrated this protein to have focusing properties identical with that of a minor isoform from bovine skeletal muscle. Upon carbamylation of this bacterially expressed protein, a train of charged proteins with charge differences of -1 were produced. These carbamylated proteins were shown to have similar focusing mobilities to the Hsp70 isoforms isolated from bovine skeletal muscle. These results demonstrate the identification of a skeletal-muscle inducible Hsp70 gene and suggest that the presence of multiple Hsp70 isoforms may be the product of post-translational modifications to the Hsp70 proteins.

Association of the dioxin receptor with the Mr 90,000 heat shock protein: A structural kinship with the glucocorticoid receptor

1988 ◽  
Vol 155 (2) ◽  
pp. 801-807 ◽  
Author(s):  
Marc Denis ◽  
Scott Cuthill ◽  
Ann-Charlotte Wikström ◽  
Lorenz Poellinger ◽  
Jan-Åke Gustafsson
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Glucocorticoid Receptor ◽  
Protein A ◽  
Dioxin Receptor
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