Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2001-8-14
pubmed:abstractText
Excessive or premature contractions of uterine smooth muscle may contribute to preterm labor. Contractile stimuli induce myosin and actin filament interactions through calcium-dependent myosin phosphorylation. The mechanisms that maintain myometrial quiescence until term are not well established, but may include control of calcium levels by nitric oxide and cGMP signaling and thin filament (caldesmon and calponin) regulation. Previously, we reported that myometrial tissues from pregnant rats are not responsive to cGMP due to decreases in cGMP-dependent protein kinase. Considering the well documented differences in the endocrinology of parturition among species, this study was conducted to test the hypothesis that the levels and subcellular distribution of caldesmon, calponin, and cGMP-dependent protein kinase are regulated with the hormonal milieu of human pregnancy. Whereas cGMP-dependent protein kinase was significantly reduced in the human uterus during pregnancy, caldesmon expression was significantly increased, and both caldesmon and calponin were redistributed to a readily extractable subcellular pool. These data suggest that cGMP-dependent protein kinase does not mediate gestational quiescence. Redistribution of thin filament-associated proteins, however, may alter uterine smooth muscle tone or the cytoskeletal framework of myocytes to maintain gestation despite the substantial distention that accompanies all intrauterine pregnancies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3981-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11502842-Actin Cytoskeleton, pubmed-meshheading:11502842-Adult, pubmed-meshheading:11502842-Aged, pubmed-meshheading:11502842-Animals, pubmed-meshheading:11502842-Calcium-Binding Proteins, pubmed-meshheading:11502842-Calmodulin-Binding Proteins, pubmed-meshheading:11502842-Continental Population Groups, pubmed-meshheading:11502842-Cyclic GMP-Dependent Protein Kinases, pubmed-meshheading:11502842-Female, pubmed-meshheading:11502842-Humans, pubmed-meshheading:11502842-Immunohistochemistry, pubmed-meshheading:11502842-Microfilament Proteins, pubmed-meshheading:11502842-Middle Aged, pubmed-meshheading:11502842-Myometrium, pubmed-meshheading:11502842-Pregnancy, pubmed-meshheading:11502842-Rats, pubmed-meshheading:11502842-Reference Values, pubmed-meshheading:11502842-United States, pubmed-meshheading:11502842-Uterine Neoplasms, pubmed-meshheading:11502842-Uterus
pubmed:year
2001
pubmed:articleTitle
Reorganization of myofilament proteins and decreased cGMP-dependent protein kinase in the human uterus during pregnancy.
pubmed:affiliation
Department of Pathology, Division of Molecular and Cellular Pathology, University of Alabama, Birmingham, Alabama 35294-0019, USA. cornwell@path.uab.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't