TY - JOUR
T1 - A human lymphocyte homing receptor, the Hermes antigen, is related to cartilage proteoglycan core and link proteins
AU - Goldstein, Leslie A.
AU - Zhou, David F.H.
AU - Picker, Louis J.
AU - Minty, Catherine N.
AU - Bargatze, Robert F.
AU - Ding, Jie F.
AU - Butcher, Eugene C.
N1 - Funding Information:
We thank Drs. E. Berg, G. Crabtree, D. Goeddel, and T. Kishimoto for critical reading of the manuscript and M. Bevilacqua, L. Lasky, S. Rosen, 8. Seed, and I. L. Weissman for sharing unpublished results. Also, J. Jang and J. Twelves for cell culture, J. Streeter and l? Verlota for assistance in producing the figures, and S. Grossman for her secretarial assistance. We thank Genentech for providing primers and support. This work was carried out under National Institutes of Health grant Al-19957 and National Science Foundation grant DC6 8408079. Louis Picker is a Career Development Awardee of the Veterans Administration. Eugene Butcher is an Established Investigator of the American Heart Association.
PY - 1989/3/24
Y1 - 1989/3/24
N2 - 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.
AB - 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.
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U2 - 10.1016/0092-8674(89)90639-9
DO - 10.1016/0092-8674(89)90639-9
M3 - Article
C2 - 2466576
AN - SCOPUS:0024517268
VL - 56
SP - 1063
EP - 1072
JO - Cell
JF - Cell
SN - 0092-8674
IS - 6
ER -