Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells
Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells
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骨髓细胞上 E-和 P-选择素的单特异性和常见糖蛋白配体
DOI：
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发表时间：
1994
影响因子：
7.8
通讯作者：
D. Vestweber
中科院分区：
文献类型：
--
作者：
M. Lenter;A. Levinovitz;S. Isenmann;D. Vestweber
E-和p -选择素是内皮细胞上的诱导细胞粘附分子，作为Ca（2+）依赖性凝集素，介导中性粒细胞和单核细胞的结合。我们最近在小鼠髓细胞上发现了一个150- kD的e -选择素糖蛋白配体，使用了一种重组抗体样的小鼠e -选择素。在这里，我们报道该配体不结合类似的p选择素融合蛋白。相反，嵌合的p选择igg蛋白识别小鼠中性粒细胞祖细胞32dcl3、成熟小鼠中性粒细胞和人HL60细胞上的160- kD糖蛋白。这种结合依赖于Ca(2+)，并且需要在配体上存在唾液酸。这种p选择配体不被e选择素识别。从150-kD和160-kD单特异性选择素配体上去除n -链碳水化合物侧链可以消除这两种配体与各自选择素的结合。用N-糖苷酶F处理HL60细胞可抑制细胞与P-和e -选择素的结合。此外，在成熟小鼠中性粒细胞上发现了230和130 kD的糖蛋白，它们以Ca（2+）依赖的方式与E-和p -选择素结合。这些配体检测到的信号比单特异性配体弱15-20倍。这两种蛋白都被唾液酸严重化，并且选择蛋白结合被唾液酸的去除所阻断，但不被n-连接碳水化合物的去除所阻断。我们的数据显示，E-和p -选择素识别两类糖蛋白配体：一种类型需要N-连接的碳水化合物结合，对两种选择素都是单特异性的；另一种类型的结合不依赖于N-连接的碳水化合物，对两种内皮选择素都是常见的。
E- and P-selectin are inducible cell adhesion molecules on endothelial cells, which function as Ca(2+)-dependent lectins and mediate the binding of neutrophils and monocytes. We have recently identified a 150- kD glycoprotein ligand for E-selectin on mouse myeloid cells, using a recombinant antibody-like form of mouse E-selectin. Here, we report that this ligand does not bind to an analogous P-selectin fusion protein. Instead, the chimeric P-selectin-IgG protein recognizes a 160- kD glycoprotein on the mouse neutrophil progenitor 32D cl 3, on mature mouse neutrophils and on human HL60 cells. The binding is Ca(2+)- dependent and requires the presence of sialic acid on the ligand. This P-selectin-ligand is not recognized by E-selectin. Removal of N-linked carbohydrate side chains from the 150-kD and the 160-kD monospecific selectin ligands abolishes the binding of both ligands to the respective selectin. Treatment of HL60 cells with Peptide: N- glycosidase F inhibited cell binding to P- and E-selectin. In addition, glycoproteins of 230 and 130 kD were found on mature mouse neutrophils, which bound both to E- and P-selectin in a Ca(2+)-dependent fashion. The signals detected for these ligands were 15-20-fold weaker than those for the monospecific ligands. Both proteins were heavily sialylated and selectin-binding was blocked by removal of sialic acid, but not by removal of N-linked carbohydrates. Our data reveal that E- and P-selectin recognize two categories of glycoprotein ligands: one type requires N-linked carbohydrates for binding and is monospecific for each of the two selectins and the other type binds independent of N- linked carbohydrates and is common for both endothelial selectins.
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影响因子：
4.4
作者：
T. Tedder;Ann C. Penta;H. Levine;A. Freedman
通讯作者：
T. Tedder;Ann C. Penta;H. Levine;A. Freedman
影响因子：
4.4
作者：
M. Valtieri;D. Tweardy;D. Caracciolo;Keith R. Johnson;F. Mavilio;S. Altmann;D. Santoli;G. Rovera
通讯作者：
M. Valtieri;D. Tweardy;D. Caracciolo;Keith R. Johnson;F. Mavilio;S. Altmann;D. Santoli;G. Rovera
影响因子：
4.4
作者：
D. Lewinsohn;R. Bargatze;E. Butcher
通讯作者：
D. Lewinsohn;R. Bargatze;E. Butcher
DOI：
10.1016/s0021-9258(19)49881-5
发表时间：
1992-06
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Glenn R. Larsen;Dianne S. Sako;T. J. Ahern;M. Shaffer;John K. Erban;S. Sajer;R. Gibson;Denisa D. Wagner;Bruce Furie;Bruce Furie
通讯作者：
Glenn R. Larsen;Dianne S. Sako;T. J. Ahern;M. Shaffer;John K. Erban;S. Sajer;R. Gibson;Denisa D. Wagner;Bruce Furie;Bruce Furie
影响因子：
56.9
作者：
BEVILACQUA, MP;STENGELIN, S;SEED, B
通讯作者：
SEED, B