Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0020538 (hypertension)
 170,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The current studies were performed to determine whether vascular smooth muscle cells produce stress-induced proteins when subjected to experimental hypertension. Two-dimensional gel electrophoresis was used to analyze labeled proteins in cultured cells in response to either heat shock or arsenite treatment. The major heat shock proteins (HSPs) induced had molecular masses of 70, 90, and 110 kDa. Arsenite treatment produced a similar response with the additional induction of a 30-kDa protein. In vitro translations of total RNA from heat-shocked cells, and RNA blot hybridization using HSP 70 cDNA suggested that HSP 70 induction was transcriptionally regulated. Treatment of cells with norepinephrine or angiotensin II induced cellular hypertrophy without eliciting HSPs. In vitro translation of aortic RNA from rats rendered hypertensive by administration of deoxycorticosterone and a high salt intake also did not reveal HSP induction. The absence of HSP induction using an in vivo model of hypertension suggests that those proteins may not be required to mediate the vascular response to experimental hypertension.
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PMID:Stress-induced proteins in aortic smooth muscle cells and aorta of hypertensive rats. 169 9

We previously demonstrated that restraint and pharmacological agents that activate sympathetic nervous system activity induce expression of the 70-kD heat shock protein (HSP70) in major blood vessels. The magnitude and rapidity in which HSP70 is induced in the aorta suggest that it may play a salient role in the mechanical properties of vascular smooth muscle. Other investigators have reported that HSP70 inducibility is increased in genetically hypertensive animals. In this report, we have investigated the effects of acute and chronic (8-week) exposure to restraint and restraint in the presence of a randomized intermittent air jet on the development of hypertension and the induction of HSP70 in the aorta and adrenal glands of normotensive adult male Sprague-Dawley rats. Acute restraint or air jet resulted in a fivefold to sixfold increase in aortic HSP70 mRNA expression. Chronic exposure to restraint reduced the HSP70 response to acute restraint. In contrast, no adaptation of the HSP70 response to acute air jet was observed in aortas of chronically air jet-treated rats. In adrenal glands, HSP70 expression was reduced after chronic restraint and air jet, indicating that in this tissue, adaptation occurs to both stressors. There was no difference in HSP70 expression in unstressed rats that had been chronically exposed to restraint or air jet in either adrenal gland or aorta. A significant increase (P < .05) in systolic blood pressure developed in air jet-treated animals (120 +/- 3 mm Hg) but not in restrained rats (107 +/- 2 mm Hg) compared with unstressed controls (106 +/- 3 mm Hg).(ABSTRACT TRUNCATED AT 250 WORDS)
Hypertension 1995 Apr
PMID:Blood pressure and heat shock protein expression in response to acute and chronic stress. 772 95

The heat shock (HS) response is remarkably conserved during evolution and is evoked under many conditions of stress. There are a number of ways in which this ubiquitous response may be important for the understanding of renal pathophysiology. Ischemia, toxin exposure, and oxidative stress induce this response. Several models of hypertension are associated with increased susceptibility to environmental stress and increased accumulation of heat shock protein mRNA. HSP70 polymorphism has been demonstrated when comparing normotensive and hypertensive rats. Heat shock proteins may play a role in renal diseases through their important involvement in immunological processes. Several observations point to a role of the heat shock response in systemic lupus erythematosus (SLE). Autoantibodies against HSP70 and ubiquitin are found in many patients with this disease. Autoantibodies against ubiquitin and ubiquitinated histone H2A are localized to the kidney glomerular basement membrane of SLE patients with active disease. A better understanding of the HS response may thus provide important insight into renal pathophysiology and may suggest paradigms for therapeutic interventions.
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PMID:Heat shock proteins and the kidney. 804 58

This review focusses on the following issues: how the mammalian heart grows and ages; age-related changes in the mammalian heart before and after imposition of hemodynamic stress; and antiaging modulation in the mammalian heart. The heart and other organs grow and age together in the whole body, and interactions occur between these organs. Therefore, the age-related changes at the molecular and cellular level in the in vivo heart are the summation of the changes of the heart per se and the effects of other organs or tissues on the heart. Furthermore, myocytes grow and age under the influence of age-related changes in other myocytes and other types of cells in the myocardial tissue through autocrine or paracrine mechanisms, because myocytes are exposed to many biologically active substances which are released from those cells. Since hypertension and ischemia are very common hemodynamic events in aged hearts, the characteristics in aged hearts are discussed in terms of responses to hypertension or ischemia. The induction of proto-oncogenes and heat shock protein genes in response to milder hemodynamic stress such as pressure-overload and ischemia is diminished in aged hearts. However, the aged heart can respond to more severe stress to a level similar to that of young-adult hearts. Therefore, the senescent heart is characterized by its attenuated adaptation to hemodynamic stress and by its ability to adapt to limited environmental changes. Several interventions have antiaging effects on the heart at the molecular and cellular level.
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PMID:Age-related changes before and after imposition of hemodynamic stress in the mammalian heart. 863 97

We have previously demonstrated that acute hypertension induces heat shock protein gene expression in rat arterial wall. Here we provide evidence that this induction is mediated through the activation of heat shock transcription factor 1 in response to high blood pressure. Rats subjected to restraint or immobilization stress displayed an acute elevation in systolic pressure accompanied by an increase in heat shock protein 70 mRNA expression. Consistent with the rapid time course of mRNA induction, an increase in binding activity to an oligonucleotide encompassing a consensus heat shock element sequence was seen in protein extracts from aorta of restrained rats as assessed with gel mobility shift assays. A similar increase in DNA binding activity was also observed in aortic extracts from rats treated with various hypertensive agents, including phenylephrine, angiotensin II, and vasopressin. That the DNA binding activity was attributed to heat shock factor 1 was shown through use of antibodies to the transcription factor that retarded the DNA-protein complexes in gel mobility supershift assays. Western blot analysis of heat shock factor 1 protein expression in aortic extracts showed a slower mobility form of the protein in hypertensive rats, indicative of an activated, presumably phosphorylated, form of the transcription factor. These findings support the view that heat shock factor 1 is responsible for induction of heat shock protein 70 in the arterial wall during acute hypertension, a response that is likely to play an important role in protecting arteries during hemodynamic stress.
Hypertension 1996 Jul
PMID:Activation of heat shock transcription factor 1 in rat aorta in response to high blood pressure. 867 64

1. Genetic, common household and non-familial environmental factors contribute about 33, 15 and 50% of blood pressure (BP) variance, respectively. Although usually considered to be additive, the environmental impact on the expression of hypertension may also interact with genetic components. Even factors such as gender and age may exert an additive (subtractive) or interactive effect. These interactions usually lead to phenotypic amplification. 2. In some instances, the environmental impact is allele-dependent (putative locus of salt-sensitivity), and there are other occasions when phenotypic expression may be environmentally dependent. Environmental temperature appears to be another environmental modifier of BP. 3. Increased sensitivity to this environmental factor has been observed in hypertension, and a locus of thermosensitivity segregates with BP in mice. Candidate genes of environmental susceptibility are proposed to include tumour necrosis factor and the heat shock protein (HSP) family. An abnormal accumulation of HSP27 and HSP70 messenger RNA has been described in rodent (mice, rat) models of hypertension as well as in human subjects. Segregation of the HSP27 and HSP70 polymorphism with BP has been determined in at least some crosses. 4. These candidate genes of environmental susceptibility may also be involved in determining heart weight in addition to BP.
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PMID:Environmental stress and genes of hypertension. 884 3

RFLP in the hsp70 gene encoding a major heat shock protein was analyzed in rat strains with high and normal arterial blood pressure. Dimorphism in the sets of DNA fragments was revealed after hybridization of the hsp gene leader sequence with rat DNA digested with BamHI restriction endonuclease. Type I RFLP was represented by the fragments of 12,200, 6500, 41,000 and 1600 bp in size. Type II RFLP corresponded to the set that included the fragments of 12,200, 6500, 2900, 1600, and 1200 bp in size. Interstrain polymorphism was demonstrated for the fragments of 4100, 2900 and 1200 bp. Furthermore, analysis of different rat strains showed that the 2900- and 1200-bp fragments were linked and formed by cleavage of the 4100-bp fragment with restriction endonuclease. This polymorphism was probably caused by the point A-->T mutation occurring in the BamHI recognition site located in the leader sequence of the hsp70 gene at a distance of +35 bp from the coding sequence. Examination of interstrain RFLP in the hsp70 gene indicated that the presence of 2900-bp fragment was not associated with hypertensive status in all experimental models of inherited arterial hypertension. This confirms the assumption on genetic heterogeneity of this common disease.
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PMID:[Polymorphism of the gene of heat shock protein hsp70 in lines of rats with normal and hypertensive status]. 958 65

Heat shock proteins (HSPs) have been implicated in protecting the cardiovascular system and in the pathogenesis of hypertension in stressed animals. In the present study, we used a fructose-induced hypertension model to explore the vascular expression of HSP72, the major inducible heat shock protein, in response to stress. Normal Sprague-Dawley rats gradually developed hypertension about 2 weeks after feeding with fructose-enriched diet and the elevated blood pressure became stable 5 weeks following diet treatment. The in vivo expression of HSP72 was absent in control rats but was transiently induced in the aorta of fructose-fed rats during the development of hypertension. Aortic HSP72 was undetectable at the established phase of hypertension. The expression of HSP72 in responses to heat shock, or vasoactive agents were examined in cultured aortic smooth muscle cells. Heat shock induced the expression of HSP72 in cells from fructose-fed rats and age-matched control rats, and the expression levels were generally not significantly varied at different sampling time points in either cell source. Also, there was no apparent difference in the magnitude of HSP72 expression between two cell sources at each selected time point. Norepinephrine or angiotensin II induced a similar level of HSP72 expression in either cell source regardless of sampling time point. These data suggest that HSP72 is associated with the development of hypertension in this model and may exert protective effect on the vasculature in response to hemodynamic stress during the early stage of hypertension.
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PMID:Vascular expression of heat shock protein 72 in fructose-induced hypertensive rats. 962 79

The phylogenetically conserved nature of heat shock proteins (Hsp) has led to the proposition that they may provide a link between infection and the inflammatory component to vascular disease. Hypertension is associated with atherosclerosis. Here, we measured circulating heat shock protein and heat shock protein antibody levels in association with borderline hypertension. Seventy-two men with borderline hypertension patients and 75 normotensive control subjects (diastolic blood pressure 85 to 94 and <80 mm Hg, respectively) were selected from a population-screening program. The levels of Hsp60; Hsp70; and anti-human Hsp60, anti-human Hsp70, and anti-mycobacterial Hsp65 antibodies were determined with enzyme immunoassay. The presence of carotid atherosclerosis and the intima-media thickness values were determined with ultrasonography. A major novel observation in this report was the detection of circulating Hsp60, which was present at a significantly enhanced level in patients with borderline hypertension. Furthermore, serum Hsp60 was associated with intima-media thicknesses (P<0.01). Anti-Hsp65 antibody levels were higher in borderline hypertension (P<0.001), whereas Hsp70 and anti-Hsp70 antibody levels did not differ. In contrast to anti-Hsp65 antibody, anti-Hsp60 antibody levels were lower in borderline hypertension (P<0.03), although the difference was quantitatively small. None of the parameters evaluated were associated with atherosclerosis, metabolic factors, or smoking. We identified elevated Hsp60 levels in patients with borderline hypertension and an association between early atherosclerosis and Hsp60 levels. The physiological role of Hsp60 release has yet to be defined, but given the proinflammatory properties, these proteins could be involved in the induction/progression of both hypertension and atherosclerosis, as well as being markers for early cardiovascular disease.
Hypertension 2000 Aug
PMID:Circulating heat shock protein 60 is associated with early cardiovascular disease. 1094 94

Various renal insults result in induction of heat shock protein (HSP) expression within the kidney. Some of the HSPs induced in that manner are postulated to have renoprotective effects via either chaperoning actions or antioxidative properties. We have previously reported that long-term angiotensin (Ang) II administration induces the expression of renal HSP32, also known as heme oxygenase-1 (HO-1). Here, we investigated the regulation of expression and localization of other HSPs, including HSP70, HSP25, and alphaB-crystallin, in the kidney of rats undergoing long-term administration of Ang II (0.7 mg. kg(-1). d(-1)). Immunoblot analysis demonstrated that Ang II increased renal expression of HSP70 and HSP25, as well as HO-1, but that expression of alphaB-crystallin was unaffected by this treatment. The Ang II-induced increase in renal HSP70 and HSP25 was dependent on the angiotensin type 1 receptor activation but not on hypertension per se. Immunohistochemistry revealed that HSP70 and HSP25 were expressed in the medullar regions and in the renal arterial wall in the kidney of control rats. After Ang II infusion, signals for HSP70, HSP25, and HO-1 proteins increased in intensity in the endothelium and medial smooth muscle of the renal artery. In addition, all of these HSPs were induced in proximal renal tubular epithelial cells from the same segments, suggesting that similar mechanisms are responsible for upregulating these HSPs. Our data show that Ang II infusion induces renal HSP70 and HSP25, as well as HO-1, and that Ang II can induce expression of these HSPs in renal cells in a pressor-independent manner.
Hypertension 2002 Jan
PMID:Regulation and localization of HSP70 and HSP25 in the kidney of rats undergoing long-term administration of angiotensin II. 1179 90


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