Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-6-8
pubmed:abstractText
Receptor protein tyrosine phosphatases (RPTPs) comprise a family of proteins that feature intracellular phosphatase domains and an ectodomain with putative ligand-binding motifs. Several RPTPs are expressed in the brain, including RPTP-kappa which participates in homophilic cell-cell interactions in vitro [Y.-P. Jiang, H. Wang, P. D'Eustachio, J.M. Musacchio, J. Schlessinger, J. Sap, Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region, Mol. Cell. Biol. 13 (1993) 2942-2951; J. Sap, Y.-P. Jiang, D. Friedlander, M. Grumet, J. Schlessinger, Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding, Mol. Cell. Biol. 14 (1994) 1-9]. The homology of RPTP-kappa's ectodomain to neural cell adhesion molecules indicates potential roles in developmental processes such as axonal growth and target recognition, as has been demonstrated for certain Drosophila RPTPs. The brain distribution of RPTP-kappa-expressing cells has not been determined, however. In a gene-trap mouse model with a beta-gal+neo (beta-geo) insertion in the endogenous RPTP-kappa gene, the consequent loss of RPTP-kappa's enzymatic activity does not produce any obvious phenotypic defects [W.C. Skarnes, J.E. Moss, S.M. Hurtley, R.S.P. Beddington, Capturing genes encoding membrane and secreted proteins important for mouse development, Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 6592-6596]. Nevertheless, since the transgene's expression is driven by the endogenous RPTP-kappa promoter, distribution of the truncated RPTP-kappa/beta-geo fusion protein should reflect the regional and cellular expression of wild-type RPTP-kappa, and thus may identify sites where RPTP-kappa is important. Towards that goal, we have used this mouse model to map the distribution of the truncated RPTP-kappa/beta-geo fusion protein in the adult mouse brain using beta-galactosidase as a marker enzyme. Visualization of the beta-galactosidase activity revealed a non-random pattern of expression, and identified cells throughout the CNS that display RPTP-kappa promoter activity. Several neural systems highly expressed the transgene-most notably cortical, olfactory, hippocampal, hypothalamic, amygdaloid and visual structures. These well-characterized brain regions may provide a basis for future studies of RPTP-kappa function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-8993
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Elsevier Science B.V.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
826
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-71
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10224293-Age Factors, pubmed-meshheading:10224293-Animals, pubmed-meshheading:10224293-Blotting, Northern, pubmed-meshheading:10224293-Brain Chemistry, pubmed-meshheading:10224293-Gene Expression Regulation, Enzymologic, pubmed-meshheading:10224293-Lac Operon, pubmed-meshheading:10224293-Mesencephalon, pubmed-meshheading:10224293-Mice, pubmed-meshheading:10224293-Mice, Inbred C57BL, pubmed-meshheading:10224293-Mice, Transgenic, pubmed-meshheading:10224293-Promoter Regions, Genetic, pubmed-meshheading:10224293-Prosencephalon, pubmed-meshheading:10224293-Protein Tyrosine Phosphatases, pubmed-meshheading:10224293-RNA, Messenger, pubmed-meshheading:10224293-Receptor-Like Protein Tyrosine Phosphatases, Class 2, pubmed-meshheading:10224293-Retina, pubmed-meshheading:10224293-Rhombencephalon, pubmed-meshheading:10224293-Spinal Cord, pubmed-meshheading:10224293-Transgenes, pubmed-meshheading:10224293-beta-Galactosidase
pubmed:year
1999
pubmed:articleTitle
Expression of a truncated receptor protein tyrosine phosphatase kappa in the brain of an adult transgenic mouse.
pubmed:affiliation
Department of Pharmacology, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't