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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2 Pt 2
pubmed:dateCreated
1991-3-22
pubmed:abstractText
The role of protein kinase C (PKC) in the modulation of the ubiquitous sodium-dependent phosphate transport and in adaptation of that transport to phosphate deprivation was investigated in MDCK cells. Phorbol myristate acetate (PMA) had a biphasic effect on sodium-dependent phosphate uptake characterized by early inhibition (-25% at 1 h) followed by late stimulation (2.3-fold at 15 h). Late stimulation was related to a decreased apparent affinity (Km) with unchanged maximal velocity (Vmax). The 15-h stimulation of phosphate uptake was also induced by an initial 1-h PMA treatment followed by a 14-h washout of PMA or by R59 022. The stimulation was inhibited by PKC downregulation. PMA stimulation was dependent on protein synthesis but not on transcription, as shown by the respective effects of cycloheximide, 3'-deoxyadenosine, and actinomycin D. In phosphate-deprived cells PMA had also a biphasic effect. A potentiation of PMA stimulation of phosphate uptake with phosphate deprivation was observed. Adaptation to phosphate deprivation was not prevented by PKC downregulation. Cytosolic and membranous PKC activities were not changed by 15-h phosphate deprivation. We conclude that 1) PKC modulates sodium-dependent phosphate uptake in MDCK cells, and 2) phosphate deprivation and PKC modulation of sodium-dependent phosphate uptake involve different cellular pathways; that is, phosphate deprivation acts through gene regulation, and PKC acts through translation regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
F235-42
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
PKC and Pi deprivation modulate differently the ubiquitous Na-dependent Pi uptake in MDCK cells.
pubmed:affiliation
Department of Physiology, Faculté de Médecine X. Bichat, Institut National de la Santé et de la Recherche Médicale Unité 251, Paris, France.
pubmed:publicationType
Journal Article