Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2003-4-28
pubmed:abstractText
The identities of ligands interacting with protein tyrosine phosphatase (PTP) receptors to regulate neurite outgrowth remain mainly unknown. Analysis of cDNA and genomic clones encoding the rat leukocyte common antigen-related (LAR) PTP receptor predicted a small, approximately 11 kDa ectodomain isoform, designated LARFN5C, containing a novel N terminal followed by a C-terminal segment of the LAR fifth fibronectin type III domain. RT-PCR and Northern blot analysis confirmed the presence of LARFN5C transcripts in brain. Transfection of COS cells with LARFN5C-Fc cDNA resulted in expression of the predicted protein, and Western blot analysis verified expression of approximately 11 kDa LARFN5C protein in vivo and its developmental regulation. Beads coated with rLARFN5C demonstrated aggregation consistent with homophilic binding, and pull-down and immunoprecipitation assays demonstrated that rLARFN5C associates with the LAR receptor. rLARFN5C binding to COS cells was dependent on LAR expression, and rLARFN5C binding to LAR +/+ hippocampal neurons was fivefold greater than that found by using LAR-deficient (-/-) neurons. Substratum-bound rLARFN5C had potent neurite-promoting effects on LAR +/+ neurons, with a fivefold loss in potency with the use of LAR -/- neurons. rLARFN5C in solution at low nanomolar concentrations inhibited neurite outgrowth induced by substratum-bound rLARFN5C, consistent with receptor-based function. These studies suggest that a small ectodomain isoform of a PTP receptor can function as a ligand for the same receptor to promote neurite outgrowth.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3353-63
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12716943-Alternative Splicing, pubmed-meshheading:12716943-Animals, pubmed-meshheading:12716943-Brain, pubmed-meshheading:12716943-COS Cells, pubmed-meshheading:12716943-Cell Adhesion, pubmed-meshheading:12716943-Cells, Cultured, pubmed-meshheading:12716943-Dose-Response Relationship, Drug, pubmed-meshheading:12716943-Gene Expression Regulation, Developmental, pubmed-meshheading:12716943-Hippocampus, pubmed-meshheading:12716943-Ligands, pubmed-meshheading:12716943-Mice, pubmed-meshheading:12716943-Mice, Knockout, pubmed-meshheading:12716943-Microspheres, pubmed-meshheading:12716943-Nerve Tissue Proteins, pubmed-meshheading:12716943-Neurites, pubmed-meshheading:12716943-Neurons, pubmed-meshheading:12716943-Protein Binding, pubmed-meshheading:12716943-Protein Isoforms, pubmed-meshheading:12716943-Protein Structure, Tertiary, pubmed-meshheading:12716943-Protein Tyrosine Phosphatases, pubmed-meshheading:12716943-Rats, pubmed-meshheading:12716943-Rats, Sprague-Dawley, pubmed-meshheading:12716943-Receptor-Like Protein Tyrosine Phosphatases, Class 2, pubmed-meshheading:12716943-Receptors, Cell Surface, pubmed-meshheading:12716943-Transfection
pubmed:year
2003
pubmed:articleTitle
Leukocyte antigen-related protein tyrosine phosphatase receptor: a small ectodomain isoform functions as a homophilic ligand and promotes neurite outgrowth.
pubmed:affiliation
Department of Neurology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.