J. Biochem, 1998, Vol. 123, No. 3 458-467
© 1998 Japanese Biochemical Society
research-article |
Characterization and Developmental Regulation of Proteoglycan-Type Protein Tyrosine Phosphatase 
/RPTP ß Isoforms1
Division of Molecular Neurobiology, National Institute for Basic Biology, and Department of Molecular Biomechanics, The Graduate University for Advanced Studies 38 Nishigonaka, Myodaiji-cho, Okazaki 444-8585
2To whom correspondence should be addressed at: Division of Molecular Neurobiology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji-cho, Okazaki 444-8585. Tel: +81-564-55-7590, Fax: +81-564-55-7595, E-mail: madon{at}nibb.ac.jp
Protein tyrosine phosphatase 
(PTP/RPTPß) is a receptor-like protein tyrosine phosphatase specifically expressed in the brain. Alternative splicing produces three isoforms of this molecule: PTP-A, the full-length form of PTP; PTP-B, the short form of PTP; and PTPS, an extracellular variant. Here, we identified all these isoforms, including PTP-B, as chondroitin sulfate proteoglycans, and characterized their carbohydrate modification and expression profiles in the rat brain. The level of PTP-A expression was maintained during the prenatal period and decreased rapidly after birth. PTP-S was expressed in a similar manner, although the postnatal decrease was gradual. In contrast, relatively constant amounts of PTP-B were observed from embryonic day 13 (E13) through adulthood. PTP-A and -S were constantly expressed only as proteoglycans during development, but a substantial amount of PTP-B was detected in a non-proteoglycan form at E13–15. Moreover, PTP-B did not contain Lex, HNK-1 carbohydrate, or keratan sulfate, although PTP-A and -S were generally modified with these carbohydrates. L cells transfected with PTP-A and -B cDNAs expressed these proteins as enzymatically active chondroitin sulfate proteoglycans. The PTP-A and -B in L cells showed essentially similar localizations in cell cortical structures on immunofluorescence microscopy, although immature or processed forms of PTP-A were accumulated additively in intracellular patchy structures. These results show that the three isoforms of PTP are differentially regulated during development, and that the extracellular deleted region in PTP-B is important for determination of carbohydrate modification.
1This work was supported by grants from the Ministry of Education, Science, Sports and Culture of Japan, and from CREST of the Japan Science and Technology Corporation.
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