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P-Selectin, called CD62 in this paper, is a membrane protein of endothelial cells and platelets and expressed on the cell surface following exposure to thrombin, histamine or complement components. This adhesion molecule mediates the recruitment of neutrophils to sites of inflammation and the attachment of myelomonocytes to platelets. CD62, like other members of the selectin family, possesses a lectin motif at the extracellular domain which is postulated to recognize the carbohydrate ligands. Fucosyl N-acetyllactosamine(CD15, Lewisx determinant) has been advanced as one of the candidates (Larsen, S. et al, Cell63, 467-474,1990), but sialic acid might also be involved in CD62 ligand(Moore, K.L. et al., J. Cell. Biol. 112, 491-499). This paper shows that CD62 binds to sulfatide on granulocytes and tumor cells. It also demonstrated that granulocytes excrete sulfatide at a rate that allows them to get rid of endothelial cells. First, CD62 soluble protein chimeras were prepared by genetic fusion of the extracellular domains of CD62 to the human IgGl. This soluble CD62 was called CD62Rg. This CD62Rg was successfully applied to analyze the binding between CD62Rg and target cells (or ligands). Studies using flow cytometry showed CD62Rg reacts with a cell surface ligand on freshly isolated human granulocytes and human myelogenous leukemia cell line HL60. Interestingly, CD62Rg binds to breast carcinoma cell lines H3630 and H3396. However, cell surface binding was not observed with leukemic T cell lines, melanoma cells and murine fibroblast cells. The lipid extracts of HL60 cells were subjected to thin layer chromatography (TLC) and incubated with the radiolabeled CD62, followed by fluorography. Suflatide, 3-sulfated galactosyl ceramide, of HL60 cells reached strongly with CD62. Neither glycolipids bearing CD 15 nor gangliosides from a bovine brain were detected to react with CD62Rg under the conditions used. Lysosulfatide, lacking the fatty acyl substitution, was not recognized, either. This is not explained according to the primary structure of the sugar chain. Aglycon(iipid) portion may have influenced the three dimensional structure of the glycosphingolipid on a TLC plate. The authors determined whether sulfatP-セ レクチン(本論文ではCD62と 呼ばれている)は トロンビ ン、 ヒスタミン及び補体 などの刺激によって血管内皮細胞お よ び血小板に発現される細胞接着分子の一つで、炎症時における 好中球や単球の集合、活性化 された血小板の白血球への結合に 関与 しているらしい。CD62は 細胞外領域 にレクチン様構造を 持っているので、白血球との結合 には糖 を介 した特異的認識機 構が働いているのではないかと考えられている。そのリガン ド としてフコシルN-ア セチルラク トサ ミン構造(CD15,Lewisx)が 最初の候補 として登場 した(Larsen,S.et al.,Cell63,467-474, 1990)が 、シアル酸が重要であるという報告 もなされていて

Sulfatide on Granulocytes and Tumor Cells Responsive to Binding to Endothelial Cells Is Excreted from the Cell Surface