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The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system.

Publication ,  Journal Article
Levy, JB; Canoll, PD; Silvennoinen, O; Barnea, G; Morse, B; Honegger, AM; Huang, JT; Cannizzaro, LA; Park, SH; Druck, T
Published in: J Biol Chem
May 15, 1993

We have isolated cDNA clones and deduced the complete amino acid sequence of a large receptor-type protein tyrosine phosphatase containing 2307 amino acids. The human gene encoding this phosphatase, denoted RPTP beta (or PTP zeta), has been localized to chromosome 7q31-33. RPTP beta is composed of a large extracellular domain, a single transmembrane domain, and a cytoplasmic portion with two tandem catalytic domains. We have also cloned a variant of RPTP beta lacking 859 amino acids from the extracellular domain but with intact transmembrane and cytoplasmic domains. Interestingly, the amino-terminal region of the extracellular domain of RPTP beta contains a stretch of 266 amino acids with striking homology to the enzyme carbonic anhydrase. Immunoprecipitation experiments from a human neuroblastoma cell line indicate that the apparent molecular mass of the core and glycosylated forms of RPTP beta are approximately 250 and 300 kDa, respectively. Northern blot analysis shows that RPTP beta is strictly expressed in the central nervous system. In situ hybridization was used to further localize the expression to different regions of the adult brain including the Purkinje cell layer of the cerebellum, the dentate gyrus, and the subependymal layer of the anterior horn of the lateral ventricle. Hence, RPTP beta represents the first mammalian tyrosine phosphatase whose expression is restricted to the nervous system. The high level of expression of RPTP beta transcripts in the ventricular and subventricular zones of the embryonic mouse brain suggests the importance of this tyrosine phosphatase in the development of the central nervous system.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

May 15, 1993

Volume

268

Issue

14

Start / End Page

10573 / 10581

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Sequence Homology, Amino Acid
  • Receptors, Cell Surface
  • Purkinje Cells
  • Protein Tyrosine Phosphatases
  • Neuroblastoma
  • Molecular Sequence Data
  • Mice
  • Infant
  • In Situ Hybridization
 

Citation

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Levy, J. B., Canoll, P. D., Silvennoinen, O., Barnea, G., Morse, B., Honegger, A. M., … Druck, T. (1993). The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system. J Biol Chem, 268(14), 10573–10581.
Levy, J. B., P. D. Canoll, O. Silvennoinen, G. Barnea, B. Morse, A. M. Honegger, J. T. Huang, L. A. Cannizzaro, S. H. Park, and T. Druck. “The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system.J Biol Chem 268, no. 14 (May 15, 1993): 10573–81.
Levy JB, Canoll PD, Silvennoinen O, Barnea G, Morse B, Honegger AM, et al. The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system. J Biol Chem. 1993 May 15;268(14):10573–81.
Levy, J. B., et al. “The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system.J Biol Chem, vol. 268, no. 14, May 1993, pp. 10573–81.
Levy JB, Canoll PD, Silvennoinen O, Barnea G, Morse B, Honegger AM, Huang JT, Cannizzaro LA, Park SH, Druck T. The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system. J Biol Chem. 1993 May 15;268(14):10573–10581.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

May 15, 1993

Volume

268

Issue

14

Start / End Page

10573 / 10581

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Sequence Homology, Amino Acid
  • Receptors, Cell Surface
  • Purkinje Cells
  • Protein Tyrosine Phosphatases
  • Neuroblastoma
  • Molecular Sequence Data
  • Mice
  • Infant
  • In Situ Hybridization