Linked Life Data

2243108

Source:http://linkedlifedata.com/resource/pubmed/id/2243108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
1990-12-28
pubmed:abstractText
The terminal differentiation of Schwann cells is dependent on contact with basement membrane. The present study was undertaken to investigate the role of cell surface heparan sulfate proteoglycans (HSPGs) in mediating Schwann cell responses to extracellular matrix contact. Phosphatidylinositol-specific phospholipase C-releasable cell surface HSPGs purified from cultures of neonatal rat Schwann cells were subjected to affinity chromatography on immobilized laminin and fibronectin. Binding of the HSPG to both affinity matrices was observed. The strength of the association, however, was sensitive to the ionic strength of the buffer. In 0.1 M Tris-HCl, HSPG binding was essentially irreversible whereas in physiological ionic strength buffer (e.g. 0.142 M NaCl, 10 mM Tris), weaker binding was detected as a delay in elution of the HSPG from the affinity columns. Further studies of HSPG-laminin binding suggested that the binding was mediated by the glycosaminoglycan chains of the proteoglycans. Results of equilibrium gel filtration chromatography provided additional evidence for a reversible association of the HSPG and laminin with a Kd of approximately 1 x 10(-6) M. When Schwann cells were plated on plastic dishes coated with laminin, the cells attached and extended long slender processes. Inclusion of heparin, but not chondroitin sulfate, in the assay medium resulted in partial inhibition of process extension, but at concentrations of heparin which were higher than that needed to disrupt laminin-HSPG association in vitro. Addition of anti-integrin receptor antibodies resulted in more extensive inhibition of laminin-dependent process extension. Anti-integrin antibodies plus heparin essentially totally inhibited laminin-dependent process extension. These results demonstrate that cell surface HSPGs are capable of reversible association with extracellular matrix molecules and suggest that HSPG-laminin interactions play a role in laminin-dependent Schwann cell spreading.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20627-33
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:2243108-Animals, pubmed-meshheading:2243108-Animals, Newborn, pubmed-meshheading:2243108-Antibodies, pubmed-meshheading:2243108-Cell Membrane, pubmed-meshheading:2243108-Cells, Cultured, pubmed-meshheading:2243108-Chondroitin Sulfate Proteoglycans, pubmed-meshheading:2243108-Chromatography, Affinity, pubmed-meshheading:2243108-Chromatography, Gel, pubmed-meshheading:2243108-Extracellular Matrix, pubmed-meshheading:2243108-Extracellular Matrix Proteins, pubmed-meshheading:2243108-Heparan Sulfate Proteoglycans, pubmed-meshheading:2243108-Heparitin Sulfate, pubmed-meshheading:2243108-Laminin, pubmed-meshheading:2243108-Rats, pubmed-meshheading:2243108-Rats, Inbred Strains, pubmed-meshheading:2243108-Schwann Cells, pubmed-meshheading:2243108-Sciatic Nerve, pubmed-meshheading:2243108-Type C Phospholipases
pubmed:year
1990
pubmed:articleTitle
Association of cell surface heparan sulfate proteoglycans of Schwann cells with extracellular matrix proteins.
pubmed:affiliation
Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania 17822.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.