scholarly journals Influence Of Total Body Controlled Hyperthermic Perfusion on Levels of Heat Shock Proteins 70 kDa in Patients with Active Infective Endocarditis

2019 ◽  
pp. 14-26
Author(s):  
A. A. Krikunov ◽  
A. B. Koltunova
Keyword(s):  
Infective Endocarditis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
General Tendency ◽  
Hsp 70 ◽  
Total Blood ◽  
Wide Range ◽  
Total Body ◽  
Shock Proteins ◽  
The Relationship

Development of infective endocarditis initiates a complex immunological response of the organism changing over time: the prevalence of pro-and anti-inflammatory mechanisms at the beginning is replaced by immunosuppression. A significant role in antigen presentation, cross-presentation, activation of macrophages and lymphocytes play the heat shock proteins 70 kDa (HSP). The aim of the study was to investigate the relationship between systemic inflammatory response and HSP 70 kDa values in patients operated on under the total body controlled hyper-thermic perfusion (TBCHP). Materials and methods.The study included 18 patients with active infective valve endocarditis operated from 01.01.2016 to 01.01.2017 with the use of TBCHP. Assessment of the relationship between clinical characteristics of patients with infective endocarditis and the level of heat shock protein 70 kDa was performed preoperatively, 2 hours after TBCHP, 8 hours after TBCHP, 20 hours after TBCHP. Results.The presence of high levels of heat shock proteins 70 kDa (5.6 ± 3.3 ng/ml) pre-operatively indicated the depression of cellular and humoral immunity. Reduction in total blood plasma protein level as an indicator of catabolism was also combined with the registration of higher values of HSP70 kDa. After 2 hours after TBCHP a wide range of HSP 70 kDa levels was observed. A blood test performed after 2 hours after TBCHP showed HSP70 kDa – average level of 6.06 ± 3.8 ng/ml. Values range between 0.96 to 9.08 ng/ml. According to these data it was possible to distinguish two subgroups of patients who differ significantly in the average values of HSP70 kDa after TBCHP. There was a general tendency to reduce the values of HSP 70kDa from the initial preoperative level to the end of 20 hour after TBCHP – 5.6 ± 3.3 ng/ml and 1.6 ± 0.68 ng/ml correspondingly (p = 0.116). Conclusion. Taking into account the previously identified preoperative relationships between HSP70 kDa level and clinical parameters of patients we may suggest that reduction of HSP 70 kDa corresponds with elimination of signs of the syndrome of persistent inflammation, immunosuppression and catabolism.

Expression of heat shock proteins in medulloblastoma

2013 ◽  
Vol 12 (5) ◽  
pp. 452-457 ◽  
Author(s):  
George A. Alexiou ◽  
George Vartholomatos ◽  
Kalliopi Stefanaki ◽  
Amalia Patereli ◽  
Lefkothea Dova ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Significant Positive Correlation ◽  
Large Cell ◽  
Hsp70 Expression ◽  
Ki 67 ◽  
Positive Correlation ◽  
Wide Range ◽  
Shock Proteins ◽  
Multiplex Bead

Object Medulloblastoma (MB) is the most common malignant brain tumor in children. Heat shock proteins (HSPs) comprise a superfamily of proteins that serve as molecular chaperones and are overexpressed in a wide range of human cancers. The purpose of the present study was to investigate the expression of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt by multiplex bead array assay of MBs. The results of HSP and Akt expression were correlated with MB subtype; immunohistochemical expression of Ki-67 index, bcl-2, and p53; and patients' prognosis. Methods The authors retrospectively evaluated 25 children with MB who underwent surgery. Immunohistochemical analysis of Ki-67, p53, and bcl-2 expression was performed in all cases. By using multiplex bead array assay, a simultaneous detection of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt was performed. Results Medulloblastoma with extensive nodularity had significantly lower HSP27 (pSer15) expression (p = 0.039) but significantly higher HSP60 expression (p = 0.021) than classic MB. Large-cell MB had significantly higher HSP70 expression (p = 0.028) than classic MB. No significant difference was found between HSP27 (pSer82), HSP40, HSP90-α, Akt, or phospho-Akt expression and MB subtype. Large-cell MBs had significantly higher Ki-67 index compared with classic MBs (p = 0.033). When analyzing all MBs, there was a significant negative correlation between HSP27 (pSer15) and Ki-67 index (r = −0.475, p = 0.016); a significant positive correlation between HSP70 expression and Ki-67 index (r = 0.407, p = 0.043); and a significant positive correlation between HSP70 expression and bcl-2 index (r = 0.491, p = 0.023). Patients with large-cell MB had a worse survival than those with classic MB, but the difference did not reach statistical significance (p = 0.076). Conclusions A substantial expression of several HSPs in MB was observed. Given that HSPs represent an attractive strategy for anticancer therapy, further studies, involving larger series of patients, are obviously necessary to clarify the relationship of HSPs with tumor aggressiveness and prognosis.

scholarly journals Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation

2011 ◽  
Vol 108 (17) ◽  
pp. 6915-6920 ◽  
Author(s):  
M. Miot ◽  
M. Reidy ◽  
S. M. Doyle ◽  
J. R. Hoskins ◽  
D. M. Johnston ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Hsp 70 ◽  
Species Specific ◽  
Shock Proteins

Different expression patterns of heat shock proteins hsp 60 and hsp 70 in zebra mussels (Dreissena polymorpha) exposed to copper and tributyltin

2000 ◽  
Vol 47 (3-4) ◽  
pp. 213-226 ◽  
Author(s):  
Maureen E Clayton ◽  
Roland Steinmann ◽  
Karl Fent
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Dreissena Polymorpha ◽  
Expression Patterns ◽  
Zebra Mussels ◽  
Hsp 70 ◽  
Shock Proteins

Interaction of Plasminogen and Angiostatin with Heat Shock Proteins.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 1622-1622
Author(s):  
Anil K. Dudani ◽  
Jelica Mehic ◽  
Anthony Martyres
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Dependent Manner ◽  
Hsp 70 ◽  
Molar Excess ◽  
Hsp 27 ◽  
Human Plasminogen ◽  
Shock Proteins ◽  
Dose Dependent ◽  
Mcf 7

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.

scholarly journals Heat shock proteins and cancer: intracellular chaperones or extracellular signalling ligands?

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160524 ◽  
Author(s):  
Stuart K. Calderwood
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tumour Cells ◽  
Future Studies ◽  
Proteotoxic Stress ◽  
Wide Range ◽  
Window Of Vulnerability ◽  
Shock Proteins ◽  
Extracellular Signalling ◽  
Key Questions

Heat shock proteins (HSPs) are found at elevated concentrations in tumour cells, and this increase reflects the proteotoxic stress experienced by the cells due to expanding levels of the mutated oncoproteins that drive tumorigenesis. The protection of oncogenic proteins by HSPs offers a window of vulnerability in tumour metabolism that has been exploited using Hsp90-targeting drugs. Such compounds have been shown to cause inhibition and degradation of a wide range of proteins essential for oncogenesis. Recently, Hsp90 has also been shown to be secreted by tumour cells and to interact in autocrine or paracrine manners with the surfaces of adjacent cells, leading to increased growth and metastasis. Future studies will address a number of key questions associated with these findings, including the relative importance of intracellular versus extracellular HSPs in tumorigenesis, as well as overcoming potential problems with normal tissue toxicity associated with Hsp90 drugs. Targeting individual members of HSP families and inactivating extracellular HSPs may be desirable future approaches that offer increased selectivity in targeting HSPs in cancer. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

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

1994 ◽  
Vol 19 (5) ◽  
pp. 335-341 ◽  
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

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

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.

scholarly journals STUDY THE RELATIONSHIP BETWEEN SELENIUM AND HEAT SHOCK PROTEINS UNDER HEAT STRESS FOR LOCAL SINAI CHICKENS STRAIN

2016 ◽  
Vol 36 (1) ◽  
pp. 337-354 ◽  
Author(s):  
Hanan Mohamed ◽  
Y. Rizk ◽  
A. Elslamony ◽  
A. Soliman ◽  
A. Ebrahim
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins ◽  
The Relationship
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