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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6 Pt 2
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pubmed:dateCreated |
1990-2-2
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pubmed:abstractText |
Sodium-phosphate (Na-Pi) cotransport is principally regulated by parathyroid hormone (PTH) and by the intrinsic ability to "adapt" to ambient phosphate concentration. In the present study, these two control mechanisms were examined in a cloned opossum kidney (OK) cell line. PTH inhibited Na-Pi cotransport, half-maximal inhibition at 5 x 10(-12) M, by fractionally similar amounts irrespective of the initial transport rates predetermined by "adaptation" to media phosphate concentration. At maximal concentrations of PTH (10(-8) M), the residual Na-Pi cotransport activity was higher in cells exposed to low-phosphate media. Cells preexposed to PTH (10(-8) M) or dibutyryl adenosine 3'-5'-cyclic monophosphate (DBcAMP) (10(-5) M) and forskolin (10(-5) M) increase transport (adaptation) by fractionally similar amounts as control cells for any given external phosphate concentration. The protein kinase C inhibitor, staurosporine, prevented PTH action but did not alter the ability to adapt Na-Pi cotransport in response to low media phosphate concentration. These data support the notion that regulation of Na-Pi cotransport by PTH and the adaptive response to available media phosphate concentration are distinct regulatory control mechanisms.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Bucladesine,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/Parathyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Phosphate Cotransporter...,
http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/Teriparatide,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0002-9513
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
F967-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2557766-Alkaloids,
pubmed-meshheading:2557766-Animals,
pubmed-meshheading:2557766-Bucladesine,
pubmed-meshheading:2557766-Carrier Proteins,
pubmed-meshheading:2557766-Cell Line,
pubmed-meshheading:2557766-Forskolin,
pubmed-meshheading:2557766-Kidney,
pubmed-meshheading:2557766-Kinetics,
pubmed-meshheading:2557766-Parathyroid Hormone,
pubmed-meshheading:2557766-Peptide Fragments,
pubmed-meshheading:2557766-Phosphates,
pubmed-meshheading:2557766-Sodium-Phosphate Cotransporter Proteins,
pubmed-meshheading:2557766-Staurosporine,
pubmed-meshheading:2557766-Symporters,
pubmed-meshheading:2557766-Teriparatide,
pubmed-meshheading:2557766-Tetradecanoylphorbol Acetate
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pubmed:year |
1989
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pubmed:articleTitle |
Sodium-phosphate cotransport in OK cells: inhibition by PTH and "adaptation" to low phosphate.
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pubmed:affiliation |
Department of Medicine, University of British Columbia, Vancouver, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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