Expression of the 31-kD Stress Protein in Rat Myoblasts and Hepatocytes

Shuman, Jon D.; Przybyla, Alan

doi:10.1089/dna.1.1988.7.475

Cited by 6 publications

(2 citation statements)

References 38 publications

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“…It is clear that induction of the stress protein response by a specific metal/metalloid may follow a unique pattern and is dependent upon the experimental model used. The induction of a specific stress protein is usually dependent on the stressor or agent, the tissue and cell type, the species or organism, and even the treatment protocol, dose, and mode of exposure [26][27][28]. This is important to consider when one is establishing stress protein induction patterns as a biomarker of exposure and/or effect for risk assessment analysis of combined-toxicant exposures.…”

Section: Introductionmentioning

confidence: 99%

A comparison of 60, 70, and 90 kDa stress protein expression in normal rat NRK‐52 and human HK‐2 kidney cell lines following in vitro exposure to arsenite and cadmium alone or in combination

Madden

Akkerman

Fowler

2002

J Biochem & Molecular Tox

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Arsenite and cadmium are two potent nephrotoxicants and common Superfund site elements. These elements are included among the stress protein inducers, but information regarding relationships between toxicity produced by combinations of these agents to the stress protein response is lacking. In this study, the immortalized cell lines normal rat kidney NRK-52E and human kidney HK-2 were exposed in vitro to arsenite (As(3+)), cadmium (Cd(2+)), or to equimolar As(3+) plus Cd(2+) mixture combinations for 3 and 5 h over a concentration range of 0.1-100 microM. After a 12-h recovery period, cultured cells were then evaluated for expression of the 60, 70, and 90 kDa major stress protein families. Results indicated that expression of stress proteins varied depending on the species of kidney cells exposed, the exposure concentrations, and the length of exposure to each element on an individual basis and for combined mixtures. For the HK-2 kidney cell line, increased levels of the 70 kDa stress protein was observed for single and combined element exposures whereas there was no change or a decrease of stress proteins 60 and 90 kDa. Increased 70 kDa expression was observed for 10-microM doses of single elements and for a lower dose of 1 microM of the As plus Cd mixture at 3- and 5-h exposures. NRK-52 kidney cells exposed to equivalent doses of As(3+) and Cd(2+) alone or in combination showed increased levels of all stress proteins 60, 70, and 90 kDa. This increase was seen for 10 microM of the As plus Cd mixture at 3 h whereas for single element exposures, increased stress protein levels were generally observed for the 100-microM doses. At 5 h- exposure, 60 and 90 kDa levels increased for 10 microM of Cd(2+) and 60 kDa levels increased for 1 microM of As(3+). However, exposures to 10 microM of the As plus Cd mixture decreased 60 kDa protein expression to control levels at 5 h. For both kidney cell lines, there was a decrease in the stress protein expression levels for all three stress protein families for 100-microM doses of the mixture combination for 3- and 5-h exposures. These data indicate a dose- and combination-related correlation between depression of the stress protein response and the onset of overt cellular toxicity and/or cell death. The threshold for these changes was cell line specific.

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Section: Introductionmentioning

confidence: 99%

A comparison of 60, 70, and 90 kDa stress protein expression in normal rat NRK‐52 and human HK‐2 kidney cell lines following in vitro exposure to arsenite and cadmium alone or in combination

Madden

Akkerman

Fowler

2002

J Biochem & Molecular Tox

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“…The mechanism of HO induction is not completely understood. Although hyperthermia normally does not induce HO in mammalian cells, the rat HO gene contains a functional heat shock element, and exposure of rat glioma cells, myoblasts or hepatocytes to elevated temperatures causes a rapid increase in HO synthesis, indicating that this enzyme is a heat shock protein in rat [39,40]. In human cells, induction of HO expression associated with hsp70 synthesis has been reported in hepatoma cell lines after heat shock treatment [41], and in macrophages after erythrophagocytosis [42].…”

Section: Discussionmentioning

confidence: 99%

Induction by prostaglandin A1 of haem oxygenase in myoblastic cells: an effect independent of expression of the 70 kDa heat shock protein

Rossi¹,

Santoro

1995

Biochemical Journal

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Prostaglandins of the A type (PGA) induce the synthesis of 70 kDa heat shock proteins (hsp70) in a large variety of mammalian cells. Induction of hsp70 has been associated with a cytoprotective effect of PGA1 after virus infection or thermal injury. In the present report we provide evidence that, in murine myoblasts, PGA1 is not able to induce hsp70 expression, whereas it increases the synthesis of the constitutive protein, hsc70, and dramatically induces the synthesis of a 32 kDa protein (p32). The p32 protein has been identified as haem oxygenase. PGA1 acts at the transcriptional level by inducing haem oxygenase mRNA synthesis, and the signal for induction appears to be associated with decreased intracellular GSH levels. Haem oxygenase, a low-molecular-mass stress protein induced in mammalian cells by oxidant stress, is known to be part of a general inducible antioxidant defence pathway. The fact that prostaglandin synthesis is stimulated in muscle during contraction and in the heart in response to ischaemia raises the possibility that induction of haem oxygenase by PGA in myoblasts could be part of a protective mechanisms in operation during stress and hypoxia.

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Heat-shock protein 90 and ubiquitin: Developmental regulation during myogenesis

Bornman¹,

Polla²,

Gericke³

1996

Muscle Nerve

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Heat‐shock/stress proteins are constitutive and stress‐inducible proteins, regulated by a number of factors including developmental processes. The 90‐kD heat‐shock protein (hsp90) and ubiquitin are up‐regulated in regenerating fibers and diseased fibers of Duchenne muscular dystrophy. The aim of the present study was to investigate whether the heat‐shock response in regenerating fibers is developmentally regulated or disease‐associated. Immunohistochemistry and immunoblot analysis were employed to compare the expression of hsp90 and ubiquitin in normal immature muscle from infants and regenerating fibers in polymyositis and dermatomyositis with the basal expression in normal, mature muscle from adults. A significant up‐regulation of hsp90 and ubiquitin in regenerating fibers and developing infantile fibers suggests that hsp90 and ubiquitin, during myogenesis, are largely regulated by the activation of developmental mechanisms rather than being primarily disease‐related. Modulation of the stress response may promote myogenesis and provide a new therapeutic approach in myopathies. © 1996 John Wiley & Sons, Inc.

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Expression of the 31-kD Stress Protein in Rat Myoblasts and Hepatocytes

Cited by 6 publications

References 38 publications

A comparison of 60, 70, and 90 kDa stress protein expression in normal rat NRK‐52 and human HK‐2 kidney cell lines following in vitro exposure to arsenite and cadmium alone or in combination

A comparison of 60, 70, and 90 kDa stress protein expression in normal rat NRK‐52 and human HK‐2 kidney cell lines following in vitro exposure to arsenite and cadmium alone or in combination

Induction by prostaglandin A1 of haem oxygenase in myoblastic cells: an effect independent of expression of the 70 kDa heat shock protein

Heat-shock protein 90 and ubiquitin: Developmental regulation during myogenesis

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