Linked Life Data

8396152

Source:http://linkedlifedata.com/resource/pubmed/id/8396152

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-10-6
pubmed:abstractText
The myoblast cell surface activity of ecto-5'-nucleotidase was stimulated by a laminin substrate, whereas fibronectin and gelatin did not increase the AMPase activity of ecto-5'-nucleotidase. This increase was related to a higher expression of ecto-5'-nucleotidase on the surface of cells seeded on a laminin substrate, but without the mobilization of an intracellular pool of enzyme. Furthermore, laminin and its fragments E'1 and E8 modified the AMPase activity of the ecto-5'-nucleotidase purified from chicken striated muscle and reconstituted in liposomes. Over the range of concentrations used, intact laminin and its fragment E8, consisting of the distal half of the long arm, stimulated the AMPase activity of ecto-5'-nucleotidase. By contrast, the large fragment derived from the short arms, designated E'1, inhibited the AMPase activity. Furthermore, the monoclonal anti-ecto-5'-nucleotidase antibody, CG37, abolished the stimulatory effect of fragment E8 on the AMPase activity of ecto-5'-nucleotidase but did not reverse the inhibitory effect of fragment E'1. In conclusion, laminin stimulates the AMPase activity of ecto-5'-nucleotidase by two mechanisms: inducing the expression of ecto-5'-nucleotidase to the cell surface and direct modulation of the enzymatic activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0730-2312
pubmed:author
pubmed:issnType
Print
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
266-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Dual mechanism of laminin modulation of ecto-5'-nucleotidase activity.
pubmed:affiliation
INSERM Unité 180, Laboratoire de Glycobiologie et Reconnaissance Cellulaire, Université René-Descartes, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't