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)

Water accumulation in the heart is important in ischemia-reperfusion injury and operations performed by using cardiopulmonary bypass, with cardiac dysfunction associated with myocardial edema being the principal determinant of clinical outcome. As an initial step in determining the role of aquaporin (AQP) water channels in myocardial edema, we have assessed the myocardial expression of AQPs in humans, rats, and mice. RT-PCR revealed expression of AQP-1, -4, -6, -7, -8, and -11 transcripts in the mouse heart. AQP-1, -6, -7, and -11 mRNAs were found in the rat heart as well as low levels of AQP-4 and -9. Human hearts contained AQP-1, -3, -4, -5, -7, -9, -10, and -11 mRNAs. AQP-1 protein expression was confirmed by Western blot analysis in all three species. AQP-4 protein was detected in the mouse heart but not in the rat or human heart. To determine the potential functional consequences of myocardial AQP expression, water permeability was measured in plasma membrane vesicles from myocardial cells of wild-type versus various AQP knockout mice. Water permeability was reduced by AQP-1 knockout but not by AQP-4 or AQP-8 knockout. With the use of a model of isolated rat heart perfusion, it was found that osmotic and ischemic stresses are not associated with changes in AQP-1 or AQP-4 expression. These studies support a possible functional role of AQP-1 in myocardium but indicate that early adaptations to osmotic and ischemic stress do not involve transcriptional or posttranslational AQP-1 regulation.
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PMID:Cardiac aquaporin expression in humans, rats, and mice. 1658 23

Aquaporins (AQPs) are widely-expressed small water channel proteins that provide the major route for water transport across plasma membranes in various cell types. Although the quantity of water transported in the intestinal tract is second only to that in the kidney, the precise role of AQPs in this organ remains largely uncertain. The present study reports the effects of hypertonic stress and ischemia/reperfusion injury on the expression of AQPs in intestinal epithelial cells. Cultured rat intestinal epithelial cells were incubated in 300 mM mannitol-containing, hypertonic culture medium or subjected to simulated ischemia/reperfusion treatment. The cell viability was evaluated by MTT assay, and the expression of AQPs was determined by semi-quantitative reverse transcription polymerase chain reaction and western blotting. Despite reduced viability, the cells exposed to hypertonic stress for 16 h demonstrated enhanced expression of AQP1 mRNA and protein. AQP9 and glycosylated AQP11 proteins were also markedly upregulated. Ischemia alone did not affect the cell viability, but subsequent reperfusion significantly reduced viability. The mRNA expression levels of all the tested AQPs were not altered by ischemia alone or by ischemia/reperfusion; however, AQP8 protein was markedly reduced by ischemic injury. In addition, treatment with ischemia alone eradicated the normally-expressed, non-glycosylated AQP11 protein whilst inducing pronounced expression of the glycosylated form. These observations may indicate that AQPs function in the intestinal epithelia in response to stress.
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PMID:Stress alters the expression of aquaporins in cultured rat intestinal epithelial cells. 2664 May 81