Linked Life Data

9019243

Source:http://linkedlifedata.com/resource/pubmed/id/9019243

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-12
pubmed:abstractText
We report the expression pattern of hemidesmosome-associated proteins laminin-5, composed of alpha 3 beta 3 gamma 2 chains, and HD1 in the developing mouse and human intestine, an organ in which variations in structure and function parallel morphogenesis and differentiation. Immunocytochemistry analysis revealed the coexpression of laminin-5 and HD1 at the basal pole of differentiating epithelial cells. Distinct noticeable variations occurring in the location of laminin alpha 3 chain in development of mouse gut were stressed by the reverse transcriptase-polymerase chain reaction data. A peculiar finding was also the location of laminin gamma 2 chain in the intestinal muscle coat. The cellular origin of laminin gamma 2 chain was examined by immunocytochemistry on interspecies hybrid intestines with specific antibodies recognizing mouse antigens. Complementary and sequential production of laminin gamma 2 chain was observed, by epithelial cells as establishment of the basement membrane occurs and by mesenchymal cells in the more differentiated organ. These results support the concept of mesenchymal involvement in deposition of basement membrane molecules, a crucial process for intestinal differentiation. Taken together these data provide the first evidence for the coexpression of hemidesmosome-associated proteins in the gut, a non-stratified tissue.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1058-8388
pubmed:author
pubmed:issnType
Print
pubmed:volume
206
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Developmental expression of laminin-5 and HD1 in the intestine: epithelial to mesenchymal shift for the laminin gamma-2 chain subunit deposition.
pubmed:affiliation
INSERM U. 381, Nice, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't