Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-10-7
pubmed:abstractText
The nitric oxide (NO)-cGMP pathway has been proposed as a mechanism for relaxation of myometrium during pregnancy and as a modulator of labor. Carbon monoxide (CO), produced by hemeoxygenases (HO-1 and HO-2), also activates soluble guanylate cyclase to increase cGMP. A recent study reported a large increase in HO-1 and HO-2 proteins during pregnancy, suggesting that the HO-CO pathway may be important in the maintenance of uterine quiescence during pregnancy. In this study we used Western blotting, reverse transcription-polymerase chain reaction, and immunohistochemistry to determine HO-1 and HO-2 expression in nonpregnant, pregnant, and laboring myometrium. Immunolocalization of HO was also compared with endothelial and inducible nitric oxide synthases (eNOS and iNOS). In contrast to HO-1 protein, which was not detected in myometrium, HO-2 protein and mRNA were constitutively expressed, although there were no differences in expression between the groups. eNOS was expressed in endothelial cells but not in myometrial smooth muscle. iNOS protein was not detected in myometrium. These data do not support an up-regulation of HO-1 and HO-2 during pregnancy and are not consistent with a role for NO or a major role for CO in human myometrial quiescence. Our results are also in keeping with HO-2 being an noninducible protein.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-1575508, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-2910857, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-2911585, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-2912370, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-3031846, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-3345742, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-3654594, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7641971, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7678352, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7755075, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7878003, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7910325, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7988434, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-7989491, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8317458, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8392811, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8423544, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8455037, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8504751, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8570637, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8739305, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-8921128, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-9070147, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-9486963, http://linkedlifedata.com/resource/pubmed/commentcorrection/10487841-9645709
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0002-9440
pubmed:author
pubmed:issnType
Print
pubmed:volume
155
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
831-40
pubmed:dateRevised
2011-10-27
pubmed:meshHeading
pubmed-meshheading:10487841-Blotting, Western, pubmed-meshheading:10487841-Cell Membrane, pubmed-meshheading:10487841-Cells, Cultured, pubmed-meshheading:10487841-Cytosol, pubmed-meshheading:10487841-Densitometry, pubmed-meshheading:10487841-Female, pubmed-meshheading:10487841-Heme Oxygenase (Decyclizing), pubmed-meshheading:10487841-Heme Oxygenase-1, pubmed-meshheading:10487841-Humans, pubmed-meshheading:10487841-Immunohistochemistry, pubmed-meshheading:10487841-Labor, Obstetric, pubmed-meshheading:10487841-Membrane Proteins, pubmed-meshheading:10487841-Molecular Weight, pubmed-meshheading:10487841-Myometrium, pubmed-meshheading:10487841-Nitric Oxide Synthase, pubmed-meshheading:10487841-Nitric Oxide Synthase Type II, pubmed-meshheading:10487841-Nitric Oxide Synthase Type III, pubmed-meshheading:10487841-Pregnancy, pubmed-meshheading:10487841-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10487841-Uterus
pubmed:year
1999
pubmed:articleTitle
Hemoxygenase and nitric oxide synthase do not maintain human uterine quiescence during pregnancy.
pubmed:affiliation
Maternal and Fetal Medicine Section,(*) Institute of Medical Genetics, Yorkhill, Glasgow Royal Victoria Infirmary, Newcastle upon Tyne, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't