Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0022116 (ischemia)
 91,303 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Heat shock proteins (HSPs) are a highly conserved group of proteins which are produced when cells are confronted with a variety of stressful insults such as heat shock, hypoxia/ischemia, metabolic disruption, and exposure to cytotoxic reagents. Under unstressed conditions, HSPs act as molecular chaperones which play pivotal roles in the course of maturation of various cellular proteins. Under stressed conditions, they play a protective role against irreversible cell damage and promote recovery of the cells experiencing stress. In the central nervous system, proteins of the HSP 90, HSP 70, HSP 60, and small HSP families are expressed constitutively and/or induced by stressful events, differentially in distinct cell types. Aberrant expression of HSPs might be implicated in the pathogenesis of neurological disorders such as multiple sclerosis and Alzheimer's disease.
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PMID:[Heat shock proteins and neurological disorders]. 799 81

We investigated the protective effect of heat stress and metabolic preconditioning in cultured adult rat cardiac myocytes and correlated this effect with induction of heat shock proteins (HSP). Myocytes were preconditioned with sublethal heat shock or metabolic preconditioning for 30 min. Twenty hours later, preconditioned myocytes were subjected to lethal heat shock (46 degrees C for 2 h) or ischemia by incubation in ischemic buffer for 2 h. Cellular injury index was reduced from 69 +/- 4.0% in lethally heat-shocked cells to 27.0 +/- 1.6% with heat shock preconditioning (mean +/- SE; P < 0.01) and 19.0 +/- 3.0% with metabolic preconditioning (P < 0.01). Cellular injury index was 81.0 +/- 1.0% in ischemic myocytes and was reduced to 25.9 +/- 2.7 and 21.4 +/- 2.6% in heat shock- and metabolic-preconditioned myocytes, respectively (P < 0.01). A significant cross-tolerance of myocytes against lethal injury was observed with the two preconditioning methods. Western blot analysis revealed 3.3- and 2.5-fold increases in HSP 90 and 500- and 15-fold increases in HSP 70 with heat shock and metabolic preconditioning, respectively. HSP 27 expression remained unaltered relative to control cells. We conclude that heat shock and metabolic preconditioning induce delayed tolerance against lethal injuries in adult cardiac myocytes with elevated levels of HSP 70 and HSP 90.
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PMID:Delayed preconditioning of cultured adult rat cardiac myocytes: role of 70- and 90-kDa heat stress proteins. 927 4

This study determined the role of body temperature during chronic exercise on myocardial stress proteins and antioxidant enzymes as well as functional recovery after an ischemic insult. Male Sprague-Dawley rats were exercised for 3, 6, or 9 wk in a 23 degrees C room (3WK, 6WK, and 9WK, respectively) or in a 4-8 degrees C environment with wetted fur (3WKC, 6WKC, and 9WKC, respectively). The colder room prevented elevations in core temperature. During weeks 3-9 the animals ran 5 days/wk up a 6% grade at 20 m/min for 60 min. Myocardial heat shock protein 70 (HSP 70) increased 12.3-fold (P < 0.05) in 9WK versus sedentary (SED) rats but was unchanged in the cold-room runners. Compared with SED rats, alphaB-crystallin was 90% higher in 9WKC animals, HSP 90 was 50% higher in 3WKC and 6WKC animals, and catalase was 23% higher in 3WK animals (P < 0.05 for all). Cytosolic superoxide dismutase increased and mitochondrial SOD decreased (P < 0.05) in 3WK and 6WK rats compared with 3WKC and 6WKC rats. Antioxidant enzymes returned to SED values in all runners by 9 wk. No differences were observed among any of the groups for glucose-regulated protein 75, heme oxygenase-1, or glutathione peroxidase. Mechanical recovery of isolated working hearts after 22.5 min of global ischemia was enhanced in 9WK (P < 0.05) but not in 9WKC rats. We conclude that exercise training results in dynamic changes in cardioprotective proteins over time which are influenced by core temperature. In addition, cardioprotection resulting from chronic exercise appears to be due to increased HSP 70.
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PMID:Effects of body temperature during exercise training on myocardial adaptations. 1129 31

Heat shock proteins (HSPs) constitute an endogenous cellular defense mechanism against environmental stresses. In the past few years, studies have shown that overexpression of HSPs can protect cardiac myocytes against ischemia-reperfusion injury. In an attempt to increase the HSPs in cardiac tissue, we used the compound radicicol that activates HSP expression by binding to the HSP 90 kDa (HSP90). HSP90 is the main component of the cytosolic molecular chaperone complex, which has been implicated in the regulation of the heat shock factor 1 (HSF1). HSF1 is responsible for the transcriptional activation of the heat shock genes. In the present study, we show that radicicol induces HSP expression in neonatal rat cardiomyocytes, and this increase in HSPs confers cardioprotection to these cardiomyocytes. We also show that radicicol induction of the HSP and cardioprotection is dependent on the inhibition of HSP90 in cardiomyocytes. These results indicate that modulation of the active HSP90 protein level plays an important role in cardioprotection. Therefore, compounds, such as radicicol and its possible derivatives that inhibit the function of HSP90 in the cell may represent potentially useful cardioprotective agents.
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PMID:Radicicol activates heat shock protein expression and cardioprotection in neonatal rat cardiomyocytes. 1511 20

The main adaptable response to increased temperature is heat shock response resulting in induction of proteins called heat shock proteins (HSP). They are present in all cells under proper growth conditions and they create 5-10% of the whole protein contents. HSP were divided into five basic groups according to their approximate molecular mass, expressed in kDa and called respectively: HSP 100, HSP 90, HSP 70, HSP 60 and small HSP. Heat shock proteins can act like antigens in many infectious diseases. Immunological response against proteins from HSP 60, HSP 70 and HSP 90 families was observed in diseases caused by bacterial and protozoan pathogens. It is known that ischemia and reperfusion activate HSP genes transcription in heart cells of various experimental animals. Human and Chlamydia pneumoniae HSP 60 were found in patients with stable coronary disease. Hence many researchers connect the increase of ischaemia with the passed infection caused by Chlamydia pneumoniae, which can influence the origin or development of atheromatous plaque in the vascular wall. HSPs play an important role in hyperthermic therapy commonly used together with irradiation. Moreover, works on the possibility of HSP application to delay of disease process in neurodegenerative diseases, such as Parkinson or Alzheimer diseases are conducted. The paper presents characteristics of heat shock proteins, role in the state of health and disease and possibilities of their usage in monitoring and/or treatment of diseases, e.g. cancers.
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PMID:[Heat shock proteins and their characteristics]. 1624 38

Nephrotoxicity is the main side effect of antibiotics such as gentamicin. Preconditioning has been reported to protect against injuries as ischemia/reperfusion. The objective of the present study was to determine the effect of preconditioning with gentamicin on LLC-PK1 cells. Preconditioning was induced in LLC-PK1 cells by 24-h exposure to 2.0 mM gentamicin (G/IU). After 4 or 15 days of preconditioning, cells were again exposed to gentamicin (2.0 mM) and compared to untreated control or G/IU cells. Necrosis and apoptosis were assessed by acridine orange and HOESCHT 33346. Nitric oxide (NO) and endothelin-1 were assessed by the Griess method and available kit. Heat shock proteins were analyzed by Western blotting. After 15 days of preconditioning, LLC-PK1 cells exhibited a significant decrease in necrosis (23.5 +/- 4.3 to 6.5 +/- 0.3%) and apoptosis (23.5 +/- 4.3 to 6.5 +/- 2.1%) and an increase in cell proliferation compared to G/IU. NO (0.177 +/- 0.05 to 0.368 +/- 0.073 microg/mg protein) and endothelin-1 (1.88 +/- 0.47 to 2.75 +/- 0.53 pg/mL) production significantly increased after 15 days of preconditioning compared to G/IU. No difference in inducible HSP 70, constitutive HSC 70 or HSP 90 synthesis in tubular cells was observed after preconditioning with gentamicin. The present data suggest that preconditioning with gentamicin has protective effects on proximal tubular cells, that involved NO synthesis but not reduction of endothelin-1 or production of HSP 70, HSC 70, or HSP 90. We conclude that preconditioning could be a useful tool to prevent the nephrotoxicity induced by gentamicin.
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PMID:Gentamicin-induced preconditioning of proximal tubular LLC-PK1 cells stimulates nitric oxide production but not the synthesis of heat shock protein. 1946 82

Heat shock proteins (HSPs) have changed very little with evolution, suggesting that they play important role(s) in cellular survival. Specifically, HSPs protect cells from induced cell death. Their expression is triggered by heat or other stress, such as ischemia. HSPs provide protection against protein denaturation, although they slightly differ with respect to group affiliation. Release of HSPs from necrotic and ischemic cardiomyocytes into the intercellular space and plasma may correlate with the intensity of the pro-inflammatory response observed during and immediately after myocardial infarction. We hypothesized that the plasma concentration of particularly inducible forms of HSPs from different groups (HSP 90, HSP 70, HSP 60 and/or HSP 20) can be used as early specific markers for diagnosing myocardial infarction in patients with acute coronary syndrome. Our hypothesis is supported by the following data: (I) HSP expression occurs very early after acute coronary events; (II) HSP concentrations increase rapidly in the peripheral blood; (III) HSP concentrations correlate with markers of myocardial necrosis and pro-inflammatory biochemical parameters. The magnitude of the increase in plasma HSP concentrations over initial concentrations during the period of highest sensitivity and specificity of the assay could be important for early detection of myocardial infarction and distinguishing it from unstable angina. We suggest that these parameters, along with close observation of patients with chest pain, will assist providers who must differentiate between acute myocardial damage and other organ diseases.
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PMID:Can we assess an acute myocardial infarction in patients with acute coronary syndrome according to diagnostic accuracy of heat shock proteins? 2295 95