Linked Life Data

16845676

Source:http://linkedlifedata.com/resource/pubmed/id/16845676

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-8-28
pubmed:abstractText
Matrix Metalloproteinases (MMPs) play a role in migration of many cell types outside the central nervous system (CNS). Among neural cells, astrocytes are one of the main sources of MMPs in physiological and postlesional conditions. However, no data are available on the possible role of MMPs in astrocyte motility. Using an in vitro model of 2D migration and broad spectrum and selective MMP inhibitors, the authors demonstrated that MMP-2, but not MMP-9, is a key enzyme for astrocyte migration. In support of these data, the authors found constitutive expression of MMP-2 in astrocytes, while MMP-9 was nearly undetectable by gel zymography and immunocytochemical methods. The inhibition of migration by MMP inhibitors correlated with changes in cell morphology and in the organization of the actin cytoskeleton. In parallel, the characteristic focalized distribution of MMP-2 at the migration front observed in control cells became more diffuse and internalized by treatments that inhibited migration. The disruption of actin by cytochalasin D caused the partial recruitment of MMP-2 and gelatinolytic activity into actin aggregates, indicating a connection between the proteinase and the actin cytoskeleton. Finally, the authors found a co-localization of beta1-integrin with MMP-2 at the leading edge of migrating astrocytes. Altogether, these data provide the first evidence for the implication of MMP-2 in astrocyte motility, probably through the interaction of the proteinase with beta1-integrin that could act as a linker between pericellular proteolysis and the actin cytoskeleton.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0894-1491
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
272-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16845676-Actins, pubmed-meshheading:16845676-Animals, pubmed-meshheading:16845676-Antigens, CD29, pubmed-meshheading:16845676-Astrocytes, pubmed-meshheading:16845676-Cell Adhesion, pubmed-meshheading:16845676-Cell Movement, pubmed-meshheading:16845676-Cell Proliferation, pubmed-meshheading:16845676-Cytoskeleton, pubmed-meshheading:16845676-Female, pubmed-meshheading:16845676-Fluorescent Antibody Technique, pubmed-meshheading:16845676-Gelatinases, pubmed-meshheading:16845676-Immunohistochemistry, pubmed-meshheading:16845676-Integrins, pubmed-meshheading:16845676-Male, pubmed-meshheading:16845676-Matrix Metalloproteinase 2, pubmed-meshheading:16845676-Matrix Metalloproteinase 9, pubmed-meshheading:16845676-Mice, pubmed-meshheading:16845676-Protease Inhibitors, pubmed-meshheading:16845676-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:16845676-Sepharose, pubmed-meshheading:16845676-Thymidine
pubmed:year
2006
pubmed:articleTitle
Matrix metalloproteinase-2 (MMP-2) regulates astrocyte motility in connection with the actin cytoskeleton and integrins.
pubmed:affiliation
Neurobiologie des Interactions Cellulaires et Neurophysiopathologie, CNRS UMR 6184. Université de la Méditerranée, Faculté de Médecine de Marseille, IFR Jean Roche, Pierre Dramard 13916, Marseille cedex 20, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't