Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Heat shock proteins (HSPs), which have been shown to be induced in the kidney by a variety of stress conditions, including ischemia, inflammation, oxidative stress, and toxin exposure, are believed to protect the cells from injury. In the present study, we demonstrated that administration of vasopressin i.v. to Wistar rats leads to HSP70 induction in the kidney. The effect was specific to the kidney (i.e., absent in brain, heart, lung, muscle, etc.) and selective for the HSP70 gene family (HSP27, HSP60, and HSP90 were not induced). Western blot analysis demonstrated that HSP70 protein expression peaked between 6 and 12 hours after vasopressin administration. Immunohistochemical staining revealed that induction was localized to renal tubule lining cells, with no expression seen in glomerular or interstitial regions. The elevated protein levels were preceded by the induction of HSP70 mRNA within 30 minutes after vasopression injection. The induction of HSP70 mRNA was associated with the activation of heat shock transcription factor 1 (HSF1), suggesting that the response was regulated at the level of transcription. This HSP70 expression was completely blocked in the presence of both a general vasopressin receptor antagonist (V1 and V2 receptors) and an antidiuretic antagonist (V2), but not in the presence of a vasopressor antagonist (V1). These observations could be significant for understanding the possible involvement of HSP70 in physiological processes of the kidney, as well as pathophysiologic conditions associated with either elevated or deficient levels of vasopressin.
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PMID:Vasopressin-induced heat shock protein expression in renal tubular cells. 856 80

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.
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PMID:Activation of heat shock transcription factor 1 in rat aorta in response to high blood pressure. 867 64