Molecular cloning and expression of Pgp-1. The mouse homolog of the human H-CAM (Hermes) lymphocyte homing receptor.

摘要: Mouse phagocytic glycoprotein-1 (Pgp-1; Ly-24) is a 95-kDa glycoprotein of unknown function that has served as an important T cell/leukocyte differentiation marker. Recent work suggested it may be related to human 85- (termed variously the Hermes Ag/lymphocyte homing receptor, ECMRIII, P80, and CD44) involved in lymphocyte binding high endothelial venules process homing, been implicated other cell adhesion events. The widespread expression this molecular class diverse organ systems suggests broad role cellular adhesion, led unifying designation homing-cellular molecule (H-CAM). By using H-CAM cDNA probes, we have isolated full-length for mouse homolog. Comparison sequences reveals N-terminal domain homologous cartilage proteoglycan core link proteins, well C-terminal transmembrane cytoplasmic sequences, are highly conserved (89% 86% identity, respectively). In contrast, proximal extracellular thought serve target O-glycosylation chondroitin sulfate attachment undergone substantial divergence (only 42% identity). Transient CHO cells followed by immunologic staining confirms encodes Pgp-1.1, one two known Pgp-1 alloantigens.