Linked Life Data

1330659

Source:http://linkedlifedata.com/resource/pubmed/id/1330659

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-12-4
pubmed:abstractText
The ecto-enzyme 5'-nucleotidase isolated from chicken gizzard has previously been shown to be a potent ligand of two glycoproteins of the extracellular matrix, namely fibronectin and laminin. Using immunofluorescent labeling techniques we observed that 5'-nucleotidase codistributed with laminin during the development of chicken striated muscle. In contrast, ecto-5'-nucleotidase was only faintly detectable on cells surrounded by a matrix expressing high levels of fibronectin. This distribution pattern distinguished 5'-nucleotidase from the pluripotent extracellular matrix receptors, chicken beta 1-integrins, which are expressed equally well in muscle and connective tissue. In addition, the specific activity of striated muscle ecto-5'-nucleotidase was stable during development and increased markedly posthatching. At each age considered, this specific activity corresponded to an 80-kDa enzyme which was inhibited by alpha,beta-methyleneadenosine diphosphate or by a monoclonal antibody directed against the smooth muscle isoform of the enzyme. Previous in vitro studies have revealed that 5'-nucleotidase is involved in the spreading of various mesenchyme-derived cells, such as chicken embryonic fibroblasts and myoblasts, on a laminin substrate. A prerequisite to examining a potential in vivo role for 5'-nucleotidase as an extracellular matrix ligand was to study its distribution. In adult muscle, 5'-nucleotidase displayed a more restricted distribution than in embryo. Results show that, in vivo, 5'-nucleotidase is revealed by immunofluorescent labeling using poly- and monoclonal antibodies to chicken gizzard 5'-nucleotidase in two structures, the costameres and myotendinous junctions, which are closely related to the focal adhesion sites observed in cell culture.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
62-71
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1330659-5'-Nucleotidase, pubmed-meshheading:1330659-Animals, pubmed-meshheading:1330659-Antibodies, Monoclonal, pubmed-meshheading:1330659-Basement Membrane, pubmed-meshheading:1330659-Chick Embryo, pubmed-meshheading:1330659-Chickens, pubmed-meshheading:1330659-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1330659-Extracellular Matrix, pubmed-meshheading:1330659-Fibronectins, pubmed-meshheading:1330659-Fluorescent Antibody Technique, pubmed-meshheading:1330659-Glycoproteins, pubmed-meshheading:1330659-Integrins, pubmed-meshheading:1330659-Laminin, pubmed-meshheading:1330659-Microscopy, Electron, pubmed-meshheading:1330659-Molecular Weight, pubmed-meshheading:1330659-Muscles, pubmed-meshheading:1330659-Myosins, pubmed-meshheading:1330659-Nucleotidases, pubmed-meshheading:1330659-Sarcolemma
pubmed:year
1992
pubmed:articleTitle
Enzymatic activity and in vivo distribution of 5'-nucleotidase, an extracellular matrix binding glycoprotein, during the development of chicken striated muscle.
pubmed:affiliation
UNITE 180 INSERM, Laboratoire de Glycobiologie et Reconnaissance Cellulaires, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't