| pubmed-article:2147426 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C0005595 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C0006376 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C0069389 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C1152564 | lld:lifeskim |
| pubmed-article:2147426 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2147426 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:2147426 | pubmed:dateCreated | 1991-1-17 | lld:pubmed |
| pubmed-article:2147426 | pubmed:abstractText | The Na/K/2Cl cotransport system in the avian erythrocyte can be activated by agents that raise intracellular cAMP suggesting the involvement of cAMP-dependent protein kinase (cAMP-PK) in its regulation. Another group of stimuli including fluoride and hypertonicity stimulate cotransport via cAMP-independent means. To further investigate the role of phosphorylation in these processes, we examined the effects of protein kinase inhibitors of 8 (p-Cl-phenylthio)-cAMP (cpt-cAMP), fluoride and hypertonic activation of cotransport in duck red cells, and [3H]bumetanide binding to isolated membranes. Preincubation of cells with the kinase inhibitors K-252a (Ki approximately 1.6 microM) and H-9 (Ki approximately 100 microM) blocked cpt-cAMP activation of bumetanide-sensitive 86Rb influx and bumetanide binding. These inhibitors also led to a rapid deactivation of cotransport and decrease in bumetanide binding when added to cells maximally stimulated by cpt-cAMP. K-252a and H-9 inhibited cotransport activation by cAMP-independent stimuli, but 10-fold higher concentrations were required, implying the involvement of a cAMP-independent phosphorylation process in the mechanism of action of these agents. Removal of stimuli that elevate cAMP leads to a rapid reversal of cotransport indicating the presence of active protein phosphatases in these cells. The protein phosphatase inhibitor okadaic acid (OA, EC50: 630 nM) stimulated both Na/K/2Cl cotransport and bumetanide binding to membranes. As with fluoride and hypertonic stimulation, the OA effect was inhibited only at relatively high concentrations of K-252a. Phosphorylation of the membrane skeletal protein goblin (Mr 230,000) at specific cAMP-dependent sites was used as an in situ marker for the state of activation of cAMP-PK. Goblin phosphorylation at these sites was increased by norepinephrine and cpt-cAMP and rapidly reversed by K-252a and H-9, confirming that both inhibitors do block cAMP-PK activity. While OA markedly increased overall phosphorylation of many erythrocyte membrane proteins, including goblin, it did not affect goblin phosphorylation at specific cAMP-dependent sites. These results implicate a cAMP-independent protein kinase in the mediation of the OA effect on cotransport and bumetanide binding. The bumetanide-binding component of the avian erythrocyte cotransporter, an Mr approximately 150,000 protein that can be photolabeled with the bumetanide analog [3H]4-benzoyl-5-sulfamoyl-3-(3-thenyloxy)-benzoic acid was found to be a phosphoprotein. These results strongly support the hypothesis that phosphorylation and dephosphorylation, possibly of the Na/K/2Cl cotransporter itself, regulates the activity of | lld:pubmed |
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| pubmed-article:2147426 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2147426 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2147426 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2147426 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2147426 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2147426 | pubmed:author | pubmed-author:HaasMM | lld:pubmed |
| pubmed-article:2147426 | pubmed:author | pubmed-author:HegdeR SRS | lld:pubmed |
| pubmed-article:2147426 | pubmed:author | pubmed-author:PalfreyH CHC | lld:pubmed |
| pubmed-article:2147426 | pubmed:author | pubmed-author:PewittE BEB | lld:pubmed |
| pubmed-article:2147426 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2147426 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2147426 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:2147426 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2147426 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2147426 | pubmed:pagination | 20747-56 | lld:pubmed |
| pubmed-article:2147426 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:2147426 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2147426 | pubmed:articleTitle | The regulation of Na/K/2Cl cotransport and bumetanide binding in avian erythrocytes by protein phosphorylation and dephosphorylation. Effects of kinase inhibitors and okadaic acid. | lld:pubmed |
| pubmed-article:2147426 | pubmed:affiliation | Department of Pharmacological and Physiological Sciences, University of Chicago, Illinois 60637. | lld:pubmed |
| pubmed-article:2147426 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2147426 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2147426 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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