A HUMAN-LYMPHOCYTE HOMING RECEPTOR, THE HERMES ANTIGEN, IS RELATED TO CARTILAGE PROTEOGLYCAN CORE AND LINK PROTEINS
A HUMAN-LYMPHOCYTE HOMING RECEPTOR, THE HERMES ANTIGEN, IS RELATED TO CARTILAGE PROTEOGLYCAN CORE AND LINK PROTEINS
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DOI：
10.1016/0092-8674(89)90639-9
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发表时间：
1989-03-24
期刊：
影响因子：
64.5
通讯作者：
BUTCHER, EC
中科院分区：
文献类型：
--
作者：
GOLDSTEIN, LA;ZHOU, DFH;BUTCHER, EC
淋巴细胞与高内皮微静脉（HEV）的相互作用，在外渗到淋巴组织涉及一个85-95 kd类的淋巴细胞表面糖蛋白，gp 90 Hermes（CD 44）。我们在这里报告的gp 90 Hermes在粘膜HEV结合B类淋巴母细胞系，KCA中表达的cDNA克隆。北方杂交显示，在粘膜HEV-，淋巴结HEV-或双重结合细胞中存在1.5，2.2和4.5 kb的三个不变的RNA条带。推导的氨基酸序列预测一个成熟的蛋白质与C-末端的胞质尾，23个氨基酸的疏水跨膜结构域，和248个氨基酸的N-末端胞外区。近端胞外结构域是O-糖基化和硫酸软骨素连接的可能区域，并且显示天然gp 90 Hermes的三个免疫显性表位簇中的至少两个。远端区域包含大多数潜在的N-糖基化位点和半胱氨酸，并表现出惊人的同源性串联重复结构域的软骨连接和蛋白聚糖核心蛋白。免疫球蛋白，整合素，钙粘蛋白基因家族没有显着的相似性。因此，gp 90 Hermes代表了一类新的整合膜蛋白参与淋巴细胞-内皮细胞相互作用和淋巴细胞归巢。
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.