Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In this study, aortic strips taken from mongrel dogs were used as experimental material. After preparation, the aortic strips were incubated in a designed control medium or an experimental medium (adding thrombin or epinephrine to the control medium). The pH value of each incubation medium mentioned above was adjusted with HCl or NaOH to a level of 8.0, 7.4, 7.0 and 6.6, respectively, in order to investigate the influence of medium acidity on the production of endothelin-1 from endothelial cells using aortic strips. After a designated time duration (one hour, three hours, six hours and 12 hours, respectively), the incubation media were collected for assay of endothelin-1. The results demonstrated that the endothelin-1 level of the incubation medium was elevated when: 1) the incubation time was lengthened; 2) the incubation medium was more acidic; 3) the aortic strips were incubated with a stimulant, such as thrombin and epinephrine; and 4) the endothelial cells on the aortic strips were intact. This indicates that the secretion of endothelin-1 is: 1) time-dependent, 2) pH-dependent, 3) stimulant-dependent and 4) endothelium-dependent.
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PMID:Effect of pH on endothelin-1 secretion of aortic strips. 810 71

The growth factor-activated Na+/H+ exchanger is regulated by numerous stimuli, including polypeptide hormones, phorbol esters, cell acidity, and cell shrinkage. To determine whether this regulation occurs at a common site on the cytoplasmic domain of the Na+/H+ exchanger, we microinjected polyclonal antibodies (RP1-c28) to the C-terminal 157 amino acids of the molecule and measured cell pH changes after application of a variety of stimuli known to activate the Na+/H+ exchanger. Microinjection of approximately 10 fg of RP1-c28 antibody, but not control IgG, into single cultured fibroblasts blocked subsequent activation of the exchanger by both endothelin and alpha-thrombin. In contrast, microinjected RP1-c28 did not prevent activation of Na+/H+ exchange by phorbol esters, consistent with the observation that both endothelin-1 and alpha-thrombin retained the ability to activate exchange activity in protein kinase C-depleted cells. Finally, activation of Na+/H+ exchange by both cell acidity and osmotic shrinkage was also unaffected by microinjected RP1-c28 antibody. These data indicate that activation of Na+/H+ exchange by endothelin-1 and alpha-thrombin is mechanistically distinct both from activation by protein kinase C and activation by physical factors and probably occurs at a separate site on the exchanger molecule.
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PMID:Role of cytoplasmic domain of the Na+/H+ exchanger in hormonal activation. 838 29