Receptor tyrosine phosphatase beta is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin.
作者： Gilad Barnea , Martin Grumet , Peter Milev , Joseph Schlessinger , Olli Silvennoinen
DOI: 10.1016/S0021-9258(17)36625-5
关键词:
摘要: The extracellular domain of receptor type protein tyrosine phosphatase beta (RPTP beta) exhibits striking sequence similarity with a soluble, rat brain chondroitin sulfate proteoglycan (3F8 PG). Immunoprecipitation experiments cells transfected RPTP expression vector and metabolically labeled [35S]sulfate [35S]methionine indicate that the transmembrane form is indeed proteoglycan. 3F8 PG therefore variant composed entire probably generated by alternative RNA splicing. Previous immunohistochemical studies indicated both matrix tenascin are localized in similar regions central nervous system. We have performed co-aggregation assays red green Co-vaspheres coated PG, respectively, showing PG) binds specifically to tenascin. interaction between an may role development mammalian
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