title: A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins.
abstract: Lymphocyte interactions with high endothelial venules (HEV) during extravasation into lymphoid tissues involve an 85-95 kd class of lymphocyte surface glycoprotein(s), gp90Hermes (CD44). We report here the cloning of cDNA for gp90Hermes expressed in a mucosal HEV-binding B lymphoblastoid cell line, KCA. Northern hybridization revealed the presence of three invariant RNA bands at 1.5, 2.2, and 4.5 kb in mucosal HEV-, lymph node HEV-, or dual-binding cells. The deduced amino acid sequence predicts a mature protein with a C-terminal cytoplasmic tail, a hydrophobic transmembrane domain of 23 amino acids, and an N-terminal extracellular region of 248 amino acids. A proximal extracellular domain is the probable region of O-glycosylation and chondroitin sulfate linkage and displays at least two of the three immunodominant epitope clusters of native gp90Hermes. A distal region contains the majority of potential N-glycosylation sites and cysteines, and exhibits a striking homology to tandemly repeated domains of the cartilage link and proteoglycan core proteins. No significant similarities were found to the immunoglobulin, integrin, or cadherin gene families. Thus gp90Hermes represents a novel class of integral membrane protein involved in lymphocyte-endothelial cell interactions and lymphocyte homing.
authors: Department of Pathology, Stanford University Medical Center, California 94305.
authors: L A
authors: LA
authors: Goldstein
authors: D F
authors: DF
authors: Zhou
authors: L J
authors: LJ
authors: Picker
authors: C N
authors: CN
authors: Minty
authors: R F
authors: RF
authors: Bargatze
authors: J F
authors: JF
authors: Ding
authors: E C
authors: EC
authors: Butcher
mesh_terms: D053674:Aggrecans; D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D002448:Cell Adhesion; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000302:isolation & purification; D016326:Extracellular Matrix Proteins; D005786:Gene Expression Regulation; D006023:Glycoproteins / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D006801:Humans; D037181:Lectins, C-Type; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D011506:Proteins / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D011509:Proteoglycans; D012313:RNA / Q000032:analysis / Q000235:genetics; D011971:Receptors, Immunologic / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D016201:Receptors, Lymphocyte Homing; D012689:Sequence Homology, Nucleic Acid; D000099249:Proteoglycan Link Protein
chemical_list: D053674:Aggrecans; D004247:DNA; D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D037181:Lectins, C-Type; D011506:Proteins; D011509:Proteoglycans; D012313:RNA; D011971:Receptors, Immunologic; D016201:Receptors, Lymphocyte Homing; D000099249:Proteoglycan Link Protein