Haruo Saito

TL;DR: The structural diversity of receptor‐like PTPases was examined by isolated human cDNA clones that cross‐hybridized to a Drosophila PTPase cDNA clone, DPTP12, under non‐stringent hybridization conditions and found partial sequences of HPTP gamma and zeta indicate that they are highly homologous and contain two P TPase‐like domains.

TL;DR: It is shown here that LAR is expressed on the cell surface as a complex of two non‐covalently associated subunits derived from a proprotein, suggesting that LAR receptor shedding may be a mechanism for regulating PTPase function.

TL;DR: Ten genomic DNA clones encoding the human leukocyte common Ag (LCA, CD45) gene were isolated by screening human genomic DNA libraries with LCA cDNA probes and indicated that the homologous domains were generated by duplication of several exons.

TL;DR: The mechanism by which HL-60 cells acquire sensitivity to VacA is examined, in particular, looking for expression of RPTPβ, a VacA-binding protein postulated to be the VacA receptor, and data are consistent with the conclusion that acquisition of VacA sensitivity by PMA-treated HL- 60 cells results from induction ofRPTPβ.

TL;DR: Three thiophosphotyrosyl peptides have been prepared and act as substrates and competitive inhibitors of these PTPase catalytic domains and assess pY sequence context recognition by HPTPβ catalytic domain.