Active biomonitoring of a subtropical river using glutathione-S-transferase (GST) and heat shock proteins (HSP 70) in Oreochromis niloticus as surrogate biomarkers of metal contamination

Abstract Previous studies from this laboratory have demonstrated that plasminogen and angiostatin bind to endothelial cell (EC) surface-associated actin via their kringles in a specific manner. Heat shock proteins (hsps) like hsp 27 are constitutively expressed by vascular ECs and regulate actin polymerization, cell growth and migration. Since many hsps have also been found to be highly abundant on cell surfaces and there is evidence that bacterial surface hsps may interact with human plasminogen, the purpose of this study was to determine whether human plasminogen and angiostatin would interact with human hsps. ELISAs were developed in our laboratory to assess these interactions. It was observed that plasminogen bound to hsps 27, 60 and 70. In all cases, binding was inhibited (85–90%) by excess (50 mM) lysine indicating kringle involvement. Angiostatin predominantly bound to hsp 27 and to hsp 70 in a concentration- and kringle-dependent manner. As observed previously for actin, there was dose-dependent inhibition of angiostatin’s interaction with hsp 27 by plasminogen. In addition, thirty-fold molar excess actin inhibited (up to 50%), the interaction of plasminogen with all hsps. However, thirty-fold molar excess actin could only inhibit the interaction of angiostatin with hsp 27 by 15–20%. FACS analyses indicated the presence of hsps 27, 60 and 70 on the surface of MCF-7 breast cancer cells but not on human umbilical vein ECs. Polyclonal antibodies to hsp 27 significantly inhibited the interaction of plasminogen and angiostatin with MCF-7 surface-associated hsp27 in a dose-dependent manner. Collectively, these data indicate that while plasminogen interacts specifically with hsp 27, 60 and 70, angiostatin interacts predominantly with hsp 27 and to some extent with hsp 70; plasminogen only partially displaces angiostatins binding to hsp 27; actin only partially displaces plasminogen/angiostatin binding to hsps and surface-associated hsp 27 can mediate the binding of both plasminogen and angiostatin to MCF-7 cells.

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Seasonal variation in heat shock proteins (hsp 70) in stream fish under natural conditions

Journal of Thermal Biology ◽

10.1016/0306-4565(94)90070-1 ◽

1994 ◽

Vol 19 (5) ◽

pp. 335-341 ◽

Cited By ~ 84

Author(s):

Susan C. Fader ◽

Zhongmo Yu ◽

James R. Spotila

Keyword(s):

Seasonal Variation ◽

Heat Shock ◽

Heat Shock Proteins ◽

Stream Fish ◽

Hsp 70 ◽

Natural Conditions ◽

Shock Proteins

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Matrin 3 co-immunoprecipitates with the heat shock proteins glucose-regulated protein 78 (GRP78), GRP75 and glutathione S-transferase π isoform 2 (GSTπ2) in thymoma cells

Biochimie ◽

10.1016/j.biochi.2014.01.015 ◽

2014 ◽

Vol 101 ◽

pp. 208-214 ◽

Cited By ~ 3

Author(s):

Ahmed M. Osman ◽

Henk van Loveren

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Glutathione S Transferase ◽

Matrin 3 ◽

Shock Proteins ◽

Glucose Regulated Protein

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The effect of synthesized chitosan grafted poly (N-L-lactide) on human genetic material

Innovaciencia Facultad de Ciencias Exactas Físicas y Naturales ◽

10.15649/2346075x.462 ◽

2018 ◽

Vol 6 (1) ◽

pp. 1-10

Author(s):

Hadi S. Al-Lami ◽

Afrodet A. Saleh ◽

Mahir A. Jalal ◽

Sara H. Mutasher

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Graft Copolymer ◽

Ring Opening ◽

Ring Opening Polymerization ◽

Natural Polymers ◽

Hsp 70 ◽

Human Dna ◽

Human Genes ◽

Shock Proteins

Introduction: Chitosan is one of the natural polymers can generally consider as a biocompatible and biodegradable polycationic polymer, which has minimum immunogenicity and low cytotoxicity. Therefore, chitosan and its derivatives may represent potentially safe cationic carriers for use in gene delivery.Materials and Methods: Chitosan with 90.1 DD% obtained by deacetylation of chitin extracted from local shrimp shells. Graft copolymerization of L-lactide onto chitosan was carried out at room temperature by ring opening polymerization under a nitrogen atmosphere to prepare chitosan-g-poly (N-lactide) graft copolymer. It was obtained in good yield and characterized by FTIR. The samples purity and concentration were detected using both Nanodrop UV-spectroscopy and agarose gel electrophoresis techniques. The human heat shock proteins gene, hsp-70, was used as a model of human genes to study the effect of chitosan-g-poly(N-lactide) graft copolymer. Results and Discussion: The results revealed that chitosan-g-poly (N-lactide) graft copolymers had safety effect on the DNA, and binding with it. the human heat shock proteins gene, hsp-70, was used as a model of human genes to study the effect of chitosan-g-poly(N-lactide) graft copolymer, it shows a good binding ability the human gene, implies that it might be used in biomedical applications in the future. Conclusions: Grafting of L-lactide onto chitosn by ring opening polymerization was confirmed by FTIR. The repaired polymer has safety effects on human DNA and genes. The chitosan-g-poly (N-lactide) graft copolymer has shown high efficiency to electrostatic interaction with human DNA and gene, implying that it is suitable to be used as DNA and gene delivery.

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The dynamic state of heat shock proteins in chicken embryo fibroblasts.

The Journal of Cell Biology ◽

10.1083/jcb.103.4.1495 ◽

1986 ◽

Vol 103 (4) ◽

pp. 1495-1507 ◽

Cited By ~ 140

Author(s):

N C Collier ◽

M J Schlesinger

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Intermediate Filament ◽

Chicken Embryo ◽

Dynamic State ◽

Hsp 70 ◽

Embryo Fibroblasts ◽

Shock Proteins ◽

Filament Network ◽

Chicken Embryo Fibroblasts

Subcellular fractionation and immunofluorescence microscopy have been used to study the intracellular distributions of the major heat shock proteins, hsp 89, hsp 70, and hsp 24, in chicken embryo fibroblasts stressed by heat shock, allowed to recover and then restressed. Hsp 89 was localized primarily to the cytoplasm except during the restress when a portion of this protein concentrated in the nuclear region. Under all conditions, hsp 89 was readily extracted from cells by detergent. During stress and restress, significant amounts of hsp 70 moved to the nucleus and became resistant to detergent extraction. Some of this hsp 70 was released from the insoluble form in an ATP-dependent reaction. Hsp 24 was confined to the cytoplasm and, during restress, aggregated to detergent-insoluble perinuclear phase-dense granules. These granules dissociated during recovery and hsp 24 could be solubilized by detergent. The nuclear hsps reappeared in the cytoplasm in cells allowed to recover at normal temperatures. Sodium arsenite also induces hsps and their distributions were similar to that observed after a heat shock, except for hsp 89, which remained cytoplasmic. We also examined by immunofluorescence the cytoskeletal systems of chicken embryo fibroblasts subjected to heat shock and found no gross morphological changes in cytoplasmic microfilaments or microtubules. However, the intermediate filament network was very sensitive and collapsed around the nucleus very shortly after a heat shock. The normal intermediate filament morphology reformed when cells were allowed to recover from the stress. Inclusion of actinomycin D during the heat shock--a condition that prevents synthesis of the hsps--did not affect the intermediate filament collapse, but recovery of the normal morphology did not occur. We suggest that an hsp(s) may aid in the formation of the intermediate filament network after stress.

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Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells

Philosophical Transactions of the Royal Society B Biological Sciences ◽

10.1098/rstb.1993.0031 ◽

1993 ◽

Vol 339 (1289) ◽

pp. 327-333 ◽

Cited By ~ 119

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Molecular Chaperones ◽

Stress Proteins ◽

Elevated Temperatures ◽

Metabolic Stress ◽

Hsp 70 ◽

Degree Of Protection ◽

Stressed Cells ◽

Shock Proteins

In response to either elevated temperatures or several other metabolic insults, cells from all organisms respond by increasing the expression of so-called heat shock proteins (hsp or stress proteins). In general, the stress response appears to represent a universal cellular defence mechanism. The increased expression and accumulation of the stress proteins provides the cell with an added degree of protection. Studies over the past few years have revealed a role for some of the stress proteins as being intimately involved in protein maturation. Members of the hsp 70 family, distributed throughout various intracellular compartments, interact transiently with other proteins undergoing synthesis, translocation, or higher ordered assembly. Although not yet proven, it has been suggested that members of the hsp 70 family function to slow down or retard the premature folding of proteins in the course of synthesis and translocation. Yet another family of stress proteins, the hsp 60 or GroEL proteins (chaperonins), appear to function as catalysts of protein folding. Here I discuss the role of those stress proteins functioning as molecular chaperones, both within the normal cell and in the cell subjected to metabolic stress.

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