Linked Life Data

10723056

Source:http://linkedlifedata.com/resource/pubmed/id/10723056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-3-29
pubmed:abstractText
Growth cones from rat dorsal root ganglia plated on laminin contain integrin clusters over the entire growth cone surface, and growth cones make transient adhesions at sites called point contacts. We examined, by immunocytochemistry and confocal microscopy, the composition and distribution of point contacts in neuronal growth cones. Vinculin was concentrated in the central domain of growth cones and at the tips of filopodia. Vinculin was specifically associated with integrin clusters at the membrane-substrate interface and thus marked point contacts. The cytoskeletal proteins paxillin and talin colocalized with beta1 integrin in a subpopulation of clusters restricted to the central domain of the growth cone and to the tips of filopodia. The neuron-specific kinase, FAK+ also distributed with the vinculin-positive clusters. The Rho family proteins RhoA, RhoB, and Cdc42 were present in growth cones, and a few Rho clusters were colocalized with vinculin. Examination of proteins resistant to detergent extraction in PC12 cells confirmed the retention of beta1 integrin, paxillin, talin, and vinculin with the cytoskeleton. Moreover, we detected FAK+ and RhoA in the detergent-resistant cytoskeleton, supporting their distribution to point contacts. Our observations indicate that two types of integrin clusters are present in growth cones: those associated with vinculin at the cell substratum interface, and those not associated with vinculin. Point contacts are mature adhesion sites defined by the presence of both beta1 integrin and vinculin, and they are associated with signaling proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0360-4012
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
458-71
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10723056-Animals, pubmed-meshheading:10723056-Antigens, CD29, pubmed-meshheading:10723056-Brain Chemistry, pubmed-meshheading:10723056-CHO Cells, pubmed-meshheading:10723056-Cells, Cultured, pubmed-meshheading:10723056-Cricetinae, pubmed-meshheading:10723056-Cytoskeletal Proteins, pubmed-meshheading:10723056-Cytoskeleton, pubmed-meshheading:10723056-Ganglia, Spinal, pubmed-meshheading:10723056-Growth Cones, pubmed-meshheading:10723056-Immunohistochemistry, pubmed-meshheading:10723056-Microscopy, Confocal, pubmed-meshheading:10723056-Neurons, pubmed-meshheading:10723056-Paxillin, pubmed-meshheading:10723056-Phosphoproteins, pubmed-meshheading:10723056-Protein-Tyrosine Kinases, pubmed-meshheading:10723056-Rats, pubmed-meshheading:10723056-Schwann Cells, pubmed-meshheading:10723056-Surface Properties, pubmed-meshheading:10723056-Talin, pubmed-meshheading:10723056-Vinculin, pubmed-meshheading:10723056-rho GTP-Binding Proteins
pubmed:year
1999
pubmed:articleTitle
Organization of point contacts in neuronal growth cones.
pubmed:affiliation
Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't