Linked Life Data

11095474

Source:http://linkedlifedata.com/resource/pubmed/id/11095474

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2000-11-29
pubmed:databankReference
pubmed:abstractText
PGE2 is known to induce uterine contraction by increasing intracellular Ca2+. In the present study, to investigate other functions of PGE2 in human uterus, two EP3 isoforms were isolated by the RT-PCR method using human uterus polyadenylated ribonucleic acid (RNA). These EP3 isoforms, named EP3-V and EP3-VI, are composed of 402 and 393 amino acid residues, respectively, which are unique compared with EP3 isoforms of other species. Their N-terminal 359 amino acid residues are identical to those of previously reported human EP3 isoforms, whereas the two isoforms contained a novel amino acid sequence in their C-terminal tails. The dissociation constant values of EP3-V and EP3-VI for PGE2 were 3.9 and 1.4 nmol/L, respectively, which were consistent with those of previously reported EP3 isoforms. Signaling experiments revealed that M&B28767, an EP3 agonist, not only inhibited forskolin-induced cAMP concentrations, but also activated mitogen-activated protein kinase in Chinese hamster ovary cells stably expressing EP3-V and EP3-VI. These responses were abolished by treatment with pertussis toxin. In addition, M&B28767 increased cAMP concentrations in EP3-VI-expressing cells, whereas it did not in EP3-V-expressing cells. M&B28767 did not stimulate phosphoinositide turnover in EP3-V or EP3-VI-expressing cells. EP3-V and EP3-VI messenger RNAs (mRNAs) were detected abundantly in human uterus, whereas weak, but substantial, bands were detected in the lung and kidney in RT-PCR specific for each mRNA. In situ hybridization revealed EP3-V and EP3-VI mRNAs in the human myometrium, but not in the endometrium. The present study suggests that EP3-V and EP3-VI are possibly involved in the proliferation of cells in human myometrium.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4315-22
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:11095474-Alprostadil, pubmed-meshheading:11095474-Amino Acid Sequence, pubmed-meshheading:11095474-Animals, pubmed-meshheading:11095474-CHO Cells, pubmed-meshheading:11095474-Cell Membrane, pubmed-meshheading:11095474-Cricetinae, pubmed-meshheading:11095474-Cyclic AMP, pubmed-meshheading:11095474-Female, pubmed-meshheading:11095474-Forskolin, pubmed-meshheading:11095474-Humans, pubmed-meshheading:11095474-Molecular Sequence Data, pubmed-meshheading:11095474-Protein Isoforms, pubmed-meshheading:11095474-RNA, Messenger, pubmed-meshheading:11095474-Receptors, Prostaglandin E, pubmed-meshheading:11095474-Receptors, Prostaglandin E, EP3 Subtype, pubmed-meshheading:11095474-Recombinant Proteins, pubmed-meshheading:11095474-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11095474-Sequence Alignment, pubmed-meshheading:11095474-Signal Transduction, pubmed-meshheading:11095474-Transcription, Genetic, pubmed-meshheading:11095474-Transfection, pubmed-meshheading:11095474-Uterus
pubmed:year
2000
pubmed:articleTitle
Multiple signal transduction pathways through two prostaglandin E receptor EP3 subtype isoforms expressed in human uterus.
pubmed:affiliation
Department of Medicine and Clinical Science, Kyoto University Graduate School of Medicine, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't