Cloning and Expression of a Widely Expressed Receptor Tyrosine Phosphatase

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 87; no. 16; pp. 6112 - 6116
• Main Authors: Sap, J., D'Eustachio, P., Givol, D., Schlessinger, J.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.08.1990; National Acad Sciences
• Subjects: Amino Acid Sequence; Amino acids; Animals; Antiserum; Base Sequence; Biological and medical sciences; Blotting, Northern; Brain - enzymology; Cell lines; Chromosome Mapping; Cloning, Molecular; Complementary DNA; COS cells; DNA - genetics; DNA - isolation & purification; Fundamental and applied biological sciences. Psychology; Gene Expression; Gene Library; Genes; Genes. Genome; Inbred strains; Messenger RNA; Mice; Mice, Inbred BALB C; Mice, Inbred Strains; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Phosphatases; Phosphoprotein Phosphatases - genetics; Protein Tyrosine Phosphatases; protein-tyrosine-phosphatase; Proteins; R-PTP- alpha protein; Receptors; Receptors, Cell Surface - genetics; Restriction Mapping; Species Specificity; Nucleotide sequence; Enzyme; Rodentia; Gene library; Gene expression; Signal transduction; Vertebrata; Membrane receptor; Mammalia; Enzymatic activity; Gene; Mouse; Restriction map; Molecular cloning; Localization; Aminoacid sequence; Protein-tyrosine-phosphatase
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.87.16.6112

We describe the identification of a widely expressed receptor-type (transmembrane) protein tyrosine phosphatase (PTPase; EC 3.1.3.48). Screening of a mouse brain cDNA library under low-stringency conditions with a probe encompassing the intracellular (phosphatase) domain of the CD45 lymphocyte antigen yielded cDNA clones coding for a 794-amino acid transmembrane protein [hereafter referred to as receptor protein tyrosine phosphatase α (R-PTP-α)] with an intracellular domain displaying clear homology to the catalytic domains of CD45 and LAR (45% and 53%, respectively). The 142-amino acid extracellular domain (including signal peptide) of R-PTP-α is marked by a high serine/threonine content (32%) as well as eight potential N-glycosylation sites but displays no similarity to known proteins. Genetic mapping assigns the gene for R-PTP-α to mouse chromosome 2, closely linked to the Il-la and Bmp-2a loci. The corresponding mRNA (3.0 kilobases) is expressed in most murine tissues and most abundantly expressed in brain and kidney. Antibodies against a synthetic peptide of R-PTP-α identified a 130-kDa protein in cells transfected with the R-PTP-α cDNA.