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

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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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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Membrane-bound Heat Shock Protein HSP70 as a Target for Theranostics of Tumors

Российский иммунологический журнал ◽

10.31857/s102872210002681-4 ◽

2018 ◽

pp. 802-804

Author(s):

M. Shevtsov ◽

B. Margulis ◽

I. Guzhova ◽

B. Nikolaev ◽

A. Ischenko ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Membrane Bound ◽

Heat Shock Protein Hsp70

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Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein HSP70 family.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.87.14.5293 ◽

1990 ◽

Vol 87 (14) ◽

pp. 5293-5297 ◽

Cited By ~ 43

Author(s):

K. Alvares ◽

A. Carrillo ◽

P. M. Yuan ◽

H. Kawano ◽

R. I. Morimoto ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Binding Protein ◽

Peroxisome Proliferator ◽

Hsp70 Family ◽

Heat Shock Protein Hsp70

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Heat Shock Protein HSP70 in Oxidative Stress in Apnea Patients

Bulletin of Experimental Biology and Medicine ◽

10.1007/s10517-020-04957-9 ◽

2020 ◽

Vol 169 (5) ◽

pp. 695-697

Author(s):

I. M. Madaeva ◽

N. A. Kurashova ◽

N. V. Semenova ◽

E. B. Ukhinov ◽

S. I. Kolesnikov ◽

...

Keyword(s):

Oxidative Stress ◽

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Protein Hsp70

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

Biochemistry and Cell Biology ◽

10.1139/o89-112 ◽

1989 ◽

Vol 67 (11-12) ◽

pp. 749-750 ◽

Cited By ~ 13

Author(s):

Boyd Hardesty ◽

Gisela Kramer

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Protein A

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

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.00305.2002 ◽

2003 ◽

Vol 285 (4) ◽

pp. L957-L963 ◽

Cited By ~ 22

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.

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Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein.

Molecular and Cellular Biology ◽

10.1128/mcb.9.6.2615 ◽

1989 ◽

Vol 9 (6) ◽

pp. 2615-2626 ◽

Cited By ~ 172

Author(s):

E Hickey ◽

S E Brandon ◽

G Smale ◽

D Lloyd ◽

L A Weber

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Normal Growth ◽

Gene Families ◽

Growth Conditions ◽

Complete Sequence ◽

Start Codon ◽

Hybridization Probe ◽

Reading Frame ◽

Alpha Gene

Vertebrate cells synthesize two forms of the 82- to 90-kilodalton heat shock protein that are encoded by distinct gene families. In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. Only the larger form, hsp89 alpha, is induced by the adenovirus E1A gene product (M. C. Simon, K. Kitchener, H. T. Kao, E. Hickey, L. Weber, R. Voellmy, N. Heintz, and J. R. Nevins, Mol. Cell. Biol. 7:2884-2890, 1987). We have isolated a human hsp89 alpha gene that shows complete sequence identity with heat- and E1A-inducible cDNA used as a hybridization probe. The 5'-flanking region contained overlapping and inverted consensus heat shock control elements that can confer heat-inducible expression on a beta-globin reporter gene. The gene contained 10 intervening sequences. The first intron was located adjacent to the translation start codon, an arrangement also found in the Drosophila hsp82 gene. The spliced mRNA sequence contained a single open reading frame encoding an 84,564-dalton polypeptide showing high homology with the hsp82 to hsp90 proteins of other organisms. The deduced hsp89 alpha protein sequence differed from the human hsp89 beta sequence reported elsewhere (N. F. Rebbe, J. Ware, R. M. Bertina, P. Modrich, and D. W. Stafford (Gene 53:235-245, 1987) in at least 99 out of the 732 amino acids. Transcription of the hsp89 alpha gene was induced by serum during normal cell growth, but expression did not appear to be restricted to a particular stage of the cell cycle. hsp89 alpha mRNA was considerably more stable than the mRNA encoding hsp70, which can account for the higher constitutive rate of hsp89 synthesis in unstressed cells.

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