Linked Life Data

2111319

Source:http://linkedlifedata.com/resource/pubmed/id/2111319

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1990-6-27
pubmed:abstractText
At different concentrations, prostaglandin E2 (PGE2) can either stimulate or inhibit cAMP formation in freshly isolated rabbit cortical collecting tubule (RCCT) cells, but in cultured RCCT cells PGE2 can only stimulate cAMP synthesis (Sonnenburg, W. K., and Smith W. L. (1989) J. Biol. Chem. 263, 6155-6160). Here, we report characteristics of [3H]PGE2 binding to membrane receptor preparations from both freshly isolated and cultured RCCT cells. [3H]PGE2 binding to membranes from freshly isolated RCCT cells was saturable and partially reversible. Equilibrium binding analyses indicated that in the absence of guanosine 5'-3-O-(thio)triphosphate (GTP gamma S) there is a single class of PGE2 binding sites (KD = 4.2 +/- 0.4 nM; Bmax = 583 +/- 28 fmol/mg); in the presence of 100 microM GTP gamma S, there is also only one class of binding sites but with a somewhat lower KD = 1.2 +/- 0.5 nM (Bmax = 370 +/- 40 fmol/mg). This stimulatory effect of GTP gamma S was blocked by pretreatment of the freshly isolated RCCT cells with pertussis toxin. The relative affinities of prostanoids for the [3H]PGE2-binding site were determined to be 17,18,19,20-tetranor-16-phenoxy-PGE2-methylsulfonylamide (sulprostone) approximately PGE2 approximately PGE1 approximately 16,16-dimethyl-PGE2 greater than carbacyclin approximately PGF2 alpha greater than PGD2. This is the order of potency with which prostaglandins inhibit arginine vasopressin-induced cAMP formation in fresh RCCT cells. Interestingly, [3H]PGE2 binding to membranes from cultured cells, which, unlike fresh cells, fail to show an inhibitory response to PGE2, was only 10-20% of that observed with membranes from fresh cells; moreover, binding of [3H]PGE2 to membranes from cultured cells was neither stimulated by GTP gamma S nor inhibited by sulprostone. The prostanoid binding specificities and the unusual pertussis toxin-sensitive, stimulatory effect of GTP gamma S on binding of [3H]PGE2 to membranes from freshly isolated RCCT cells are characteristics shared by a Gi-linked PGE receptor from renal medulla (Watanabe, T., Umegaki, K., and Smith, W. L. (1986) J. Biol. Chem. 261, 14340-14349). Our results suggest that the [3H]PGE2 binding site of freshly isolated RCCT cells is the PGE receptor which is coupled to a Gi to attenuate arginine vasopressin-induced cAMP synthesis in the renal collecting tubule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8479-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2111319-Animals, pubmed-meshheading:2111319-Binding, Competitive, pubmed-meshheading:2111319-Cell Membrane, pubmed-meshheading:2111319-Cells, Cultured, pubmed-meshheading:2111319-Dinoprostone, pubmed-meshheading:2111319-GTP-Binding Proteins, pubmed-meshheading:2111319-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:2111319-Guanosine Triphosphate, pubmed-meshheading:2111319-Kidney Cortex, pubmed-meshheading:2111319-Kidney Tubules, pubmed-meshheading:2111319-Kidney Tubules, Collecting, pubmed-meshheading:2111319-Kinetics, pubmed-meshheading:2111319-Pertussis Toxin, pubmed-meshheading:2111319-Prostaglandins, pubmed-meshheading:2111319-Rabbits, pubmed-meshheading:2111319-Receptors, Prostaglandin, pubmed-meshheading:2111319-Thionucleotides, pubmed-meshheading:2111319-Virulence Factors, Bordetella
pubmed:year
1990
pubmed:articleTitle
A prostaglandin E receptor coupled to a pertussis toxin-sensitive guanine nucleotide regulatory protein in rabbit cortical collecting tubule cells.
pubmed:affiliation
Department of Biochemistry, Michigan State University, East Lansing 48824.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't