70 kDa heat shock proteins from mollusc and human cells have common structural and functional domains

Margulis, Boris A.; Antropova, Olga; Харазова, А. Д.

doi:10.1016/0305-0491(89)90138-7

Cited by 20 publications

(12 citation statements)

References 7 publications

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“…HSP70 is the largest and most highly conserved of the stress protein families (Sanders 1993). At least 121 proteins have been characterized within this family and cross-hybridization occurs across mammals, fish and molluscs; indeed, humans and molluscs share the same antigenic and ATP binding domains (Margulis, Antropova & Kharazova 1989).…”

Section: Heat Shock Proteinsmentioning

confidence: 99%

Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review

Roberts

Agius

Saliba

et al. 2010

Journal of Fish Diseases

465

246

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Heat shock proteins (HSPs), also known as stress proteins and extrinsic chaperones, are a suite of highly conserved proteins of varying molecular weight (c. 16-100 kDa) produced in all cellular organisms when they are exposed to stress. They develop following up-regulation of specific genes, whose transcription is mediated by the interaction of heat shock factors with heat shock elements in gene promoter regions. HSPs function as helper molecules or chaperones for all protein and lipid metabolic activities of the cell, and it is now recognized that the up-regulation in response to stress is universal to all cells and not restricted to heat stress. Thus, other stressors such as anoxia, ischaemia, toxins, protein degradation, hypoxia, acidosis and microbial damage will also lead to their up-regulation. They play a fundamental role in the regulation of normal protein synthesis within the cell. HSP families, such as HSP90 and HSP70, are critical to the folding and assembly of other cellular proteins and are also involved in regulation of kinetic partitioning between folding, translocation and aggregation within the cell. HSPs also have a wider role in relation to the function of the immune system, apoptosis and various facets of the inflammatory process. In aquatic animals, they have been shown to play an important role in health, in relation to the host response to environmental pollutants, to food toxins and in particular in the development of inflammation and the specific and non-specific immune responses to bacterial and viral infections in both finfish and shrimp. With the recent development of non-traumatic methods for enhancing HSP levels in fish and shrimp populations via heat, via provision of exogenous HSPs or by oral or water administration of HSP stimulants, they have also, in addition to the health effects, been demonstrated to be valuable in contributing to reducing trauma and physical stress in relation to husbandry events such as transportation and vaccination.

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Section: Heat Shock Proteinsmentioning

confidence: 99%

Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review

Roberts

Agius

Saliba

et al. 2010

Journal of Fish Diseases

465

246

View full text Add to dashboard Cite

show abstract

“…The levels of heat shock proteins with an approximate weight of 70 kDa were measured in the hepatopancreas of the test organisms. These proteins belong to the Hsp70 stress protein family and are highly conserved across a wide range of taxa (Margulis et al, 1989). They serve to fold unfolded proteins and to re-fold partially damaged proteins.…”

Section: Introductionmentioning

confidence: 99%

Impact of the Antidiabetic Drug Metformin and Its Transformation Product Guanylurea on the Health of the Big Ramshorn Snail (Planorbarius corneus)

Jacob

Köhler

Tisler

et al. 2019

Front. Environ. Sci.

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Pharmaceuticals can enter surface waters via sewage treatment plants. In the environment, the substances and their transformation products, formed by the degradation of the parent compounds, can affect aquatic wildlife, including freshwater invertebrates. However, research on pharmaceutical-induced effects in wild freshwater organisms other than fish is still scarce. In our study, we investigated the impact of the highly consumed antidiabetic drug metformin and its main transformation product, guanylurea, on the health of a freshwater gastropod-the big ramshorn snail (Planorbarius corneus) by analysing its biochemical and cellular stress responses and apical parameters. The snails were exposed to different concentrations of the drug (0, 0.01, 0.1, 1, and 10 mg/L) and its transformation product (0, 0.1, 10, and 100 mg/L). The examined parameters were mortality, weight, tissue integrity of the hepatopancreas, and the levels of stress proteins and lipid peroxides. Mortality and the levels of stress proteins and lipid peroxides were not influenced by the two substances. In response to the highest concentrations of both chemicals, the weight of the snails was slightly but not significantly reduced. The histopathological investigation of the hepatopancreas revealed a significant effect of guanylurea at a concentration of 100 mg/L with an increased number of symptoms of cellular responses in the tissue (e.g., dilated lumen, disturbed compartmentation of the digestive cells, nucleus deformation, hyperplasia, and hypertrophy of crypt cells). For the parent compound, a similar trend was also observed for the highest concentration. Overall, the observed effects did not occur at environmentally relevant concentrations, but at concentrations which were 10,000 times higher than these. Thus, the results did not give rise to a major concern that metformin and guanylurea could pose a risk to the big ramshorn snail in the environment.

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“…According to results from an ELISA assay, four of the nine immunized animals developed a positive reaction after an immunization procedure of 5-6 months. The specificity of affinity-purified antibodies was first evaluated by immunoblotting with the preparation of HeLa cells known to contain four components of the hsp70 family [8]. Each antibody was shown to recognize a specific profile of hsp70 isoforms after denaturation by sodium dodecyl sulfate (Fig.…”

Section: Resultsmentioning

confidence: 99%

The characterization and use of different antibodies against the hsp70 major heat shock protein family for the development of an immunoassay

et al. 1991

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The hsp70 family of major stress proteins is composed of several different members exhibiting similar structural and functional properties. In order to obtain an antiserum with wide epitope reactivity, rabbits were immunized with a mixture of native and denatured hsp70 purified from bovine muscle by ATP-affinity chromatography. Screening for antibody specificity was performed by a "sandwich" enzyme linked immunosorbent assay (ELISA). Immunoprecipitation and immunoblotting analyses demonstrated that the polyclonal antiserum obtained by us and a monoclonal antibody raised against a different preparation of antigen recognized the same determinant on the native hsp70 molecule (inducible form). With a different specificity the polyclonal antiserum recognized only the denatured monomers of the other members of the hsp70 family. These results are discussed in relation to the immunological features of the hsp70 molecule and to the development of an immunoassay for the detection of hsp70 in cell and tissue extracts.

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70 kDa heat shock proteins from mollusc and human cells have common structural and functional domains

Cited by 20 publications

References 7 publications

Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review

Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review

Impact of the Antidiabetic Drug Metformin and Its Transformation Product Guanylurea on the Health of the Big Ramshorn Snail (Planorbarius corneus)

The characterization and use of different antibodies against the hsp70 major heat shock protein family for the development of an immunoassay

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