Linked Life Data

8107049

Source:http://linkedlifedata.com/resource/pubmed/id/8107049

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-24
pubmed:abstractText
Lectin histochemistry was used to demonstrate changes in the surface glycan distribution of uterine stromal cells as they differentiate to form decidual cells. Decidualization was induced in hormone-treated, ovariectomized rat uteri by needle scratch. Uterine tissue from days 2 to 8 of deciduoma development was examined with a panel of lectins specific for terminal non-reducing structures in N- and O-linked classes of glycoprotein glycan, including alpha 2,3- and alpha 2,6-linked sialic acid residues. Immunostaining for desmin was used to identify decidual cells. An increase in N-linked glycans associated with the cell surface and recognized by lectins from Phaseolus vulgaris (leukoagglutinin) (l-PHA), Pisum sativum (PSA) and Triticum vulgaris (WGA) was found during the early growth of decidual cells. As decidualization progressed regionally from the antimesometrial to mesometrial uterus, an increase in alpha 2,3-linked sialic acid residues was followed by a loss of the alpha 2,6-linked form. The results suggest that as stromal cells differentiate, glycoprotein biosynthesis and glycosyl transferase activity are altered. These changes in patterns of glycosylation may give rise to altered decidual cell-matrix and cell-cell interactions during differentiation and play a role in the modulation of decidual cell interactions with trophoblast during early placentation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-4251
pubmed:author
pubmed:issnType
Print
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
635-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Patterns of sialylation in differentiating rat decidual cells as revealed by lectin histochemistry.
pubmed:affiliation
Department of Pathological Sciences, University of Manchester, UK.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.