Volume 272, Number 11, Issue of March 14, 1997 pp. 7264-7277
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Novel Protein-Tyrosine Phosphatase Related to the Homotypically Adhering  and µ Receptors

(Received for publication, July 11, 1996, and in revised form, December 3, 1996)

Jill Cheng , Kai Wu , Mark Armanini ^§ , Nancy O'Rourke ^§ , Donald Dowbenko and Laurence A. Lasky

From the Departments of  Molecular Oncology and ^§ Neuroscience, Genentech, Inc., South San Francisco, California 94080

Here we describe a novel member of the receptor-like protein-tyrosine phosphatases (PTPs) termed PTP , which is homologous to the homotypically adherent PTPs  and µ. Murine PTP  contains MAM, IgG, fibronectin type III, and dual phosphatase domains. As has been demonstrated for PTPs  and µ, PTP  mediates homotypic adhesion in vitro, and PTP  is associated with  catenin in kidney epithelial cells. The extracellular domain of PTP  is proteolytically processed in cell culture as well as in vivo. Northern blot analysis reveals that PTP  is expressed throughout embryonic development and is predominately found in adult brain, lung, and kidney. In situ hybridization to 15.5-day old rat embryos reveals that PTP  is expressed in a variety of embryonic neuronal sites as well as in the esophagus, lung bronchiolar epithelium, kidney glomerular epithelium, olfactory epithelium, and various cartilagenous sites. Analysis of neonatal brain demonstrates expression in cells of the hippocampus, cortex, and the substantia nigra. Finally, immunohistochemical analysis reveals expression of this PTP on specific neurons of the spinal cord as well as on isolated cortical neurons.

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