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

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.

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

Plastic & Reconstructive Surgery ◽

10.1097/00006534-199901000-00078 ◽

1999 ◽

Vol 103 (1) ◽

pp. 336-337 ◽

Cited By ~ 2

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

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Specific antibodies against the stress-inducible 72-kDa protein, a member of the heat-shock protein hsp70, in healthy human subjects

International Journal of Biochemistry ◽

10.1016/0020-711x(91)90132-7 ◽

1991 ◽

Vol 23 (10) ◽

pp. 975-978 ◽

Cited By ~ 20

Author(s):

Hideki Wakui ◽

Hideaki Itoh ◽

Yohtalou Tashima ◽

Ryoji Kobayashi ◽

Yasushi Nakamoto ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Human Subjects ◽

Protein A ◽

Healthy Human ◽

Specific Antibodies ◽

Healthy Human Subjects ◽

Heat Shock Protein Hsp70

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

Journal of Biological Chemistry ◽

10.1074/jbc.m800591200 ◽

2008 ◽

Vol 283 (22) ◽

pp. 15142-15151 ◽

Cited By ~ 78

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

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Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.89.8.3394 ◽

1992 ◽

Vol 89 (8) ◽

pp. 3394-3398 ◽

Cited By ~ 89

Author(s):

D. J. Hartman ◽

N. J. Hoogenraad ◽

R. Condron ◽

P. B. Hoj

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Protein A ◽

Chaperonin 10 ◽

Ornithine Transcarbamoylase

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

Biochemical Journal ◽

10.1042/bj3050197 ◽

1995 ◽

Vol 305 (1) ◽

pp. 197-203 ◽

Cited By ~ 30

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.

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