The GPIIB-IIIa-like complex may function as a human melanoma cell adhesion receptor for thrombospondin.
The GPIIB-IIIa-like complex may function as a human melanoma cell adhesion receptor for thrombospondin.
复制标题
GPIIB-IIIa 样复合物可能充当血小板反应蛋白的人黑色素瘤细胞粘附受体。
DOI:
10.1016/0014-4827(89)90251-6
复制
发表时间:
1989
影响因子:
3.7
通讯作者:
Knudsen,KA
中科院分区:
文献类型:
--
作者:
Tuszynski,GP;Karczewski,J;Smith,L;Murphy,A;Rothman,VL;Knudsen,KA
The purpose of this study was to determine whether a heterodimeric complex immunologically related to the fibrinogen receptor could function as a thrombospondin (TSP) receptor in TSP-mediated cell-substratum adhesion of human melanoma cells. We found that polyclonal antibodies to the platelet GPIIb-IIIa complex, GPIIIa, and the human vitronectin receptor inhibited TSP-mediated cell adhesion by 63–68%. Immunoprecipitation of detergent extracts of125I-surface-labeled melanoma cells using either anti-human platelet GPIIb-IIla or anti-human vitronectin receptor antibody revealed the presence of a single heterodimeric complex, suggesting that both antisera recognize the same integrin receptor, GPIIb-IIIa-like antigen. Adhesion of cells to TSP is likely mediated through a region of the TSP molecule containing the arginine-glycine-aspartic (RGD) peptide sequence, since cell attachment to TSP was inhibited 50–66% in the presence of peptides containing RGD. These results strongly suggest that a GPIIb-IIIa-like/vitronectin receptor can serve as a cell binding site for TSP in mediating cell-substratum adhesion.