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Publication : Isolation and characterization of murine orthologue of PTP-BK.

First Author  Tomemori T Year  2000
Journal  Biochem Biophys Res Commun Volume  276
Issue  3 Pages  974-81
PubMed ID  11027578 Mgi Jnum  J:65083
Mgi Id  MGI:1891757 Doi  10.1006/bbrc.2000.3584
Citation  Tomemori T, et al. (2000) Isolation and characterization of murine orthologue of PTP-BK. Biochem Biophys Res Commun 276(3):974-81
abstractText  We isolated and characterized a murine orthologue of PTP-BK, a receptor-type protein tyrosine phosphatase expressed in brain and kidney. The deduced amino acid sequences showed 89, 95, and 92% identities with human, rabbit, and chicken homologues of PTP-BK. Mouse PTP-BK encodes a polypeptide of 1,226 amino acids with calculated molecular weight of 138,598 Da. The mature form of PTP-BK constitutes of 3 domain structures including extracellular, transmembrane, and a single intracellular PTPase domain. Western blot analysis indicated that anti-PTP-BK antibody specifically immunoreacted to 2 distinct molecules of 200 kDa and 220 kDa in COS cells, possibly due to differential glycosylation. The recombinant PTP-BK showed the phosphatase activity specific for the phosphotyrosine, but not for the phosphoserine residue of phosphopeptides in vitro. Radiation hybrid panel assigned mouse PTP-BK gene to 5.02cR distal to from the marker D6Mit339 on chromosome 6. Mouse PTP-BK was classified in PTPRO family in novel nomenclature. We discuss here the diversity and physiological functions of PTPRO family of PTP. Copyright 2000 Academic Press.
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