Luque A, Sánchez-Madrid F, Cabañas C
Departamento de Bioquímica, Facultad de Medicina, Universidad Complutense, Madrid, Spain.
FEBS Lett. 1994 Jun 13;346(2-3):278-84. doi: 10.1016/0014-5793(94)00490-0.
We have investigated the regulation by divalent cations Mg2+, Ca2+ and Mn2+ of the functional activity of the human integrin VLA-1 expressed on neuroblastoma NB100 cells. VLA-1-mediated adhesion of NB100 cells to ligand collagen type I was supported by either mM concentrations of extracellular Mg2+ or microM levels of Mn2+. In contrast, Ca2+ alone did not induce activation of VLA-1 but exerted a potent inhibitory effect on the Mg(2+)-supported cell adhesion. We have also demonstrated that VLA-1 can be directly activated by the stimulatory monoclonal antibody TS2/16 specific for the integrin beta 1 subunit, resulting in effective adhesion of NB100 cells to type I collagen. This study has been possible by using a novel blocking VLA-alpha 1 specific monoclonal antibody, 5E8D9.
我们研究了二价阳离子Mg2+、Ca2+和Mn2+对神经母细胞瘤NB100细胞上表达的人整合素VLA-1功能活性的调节作用。毫摩尔浓度的细胞外Mg2+或微摩尔水平的Mn2+均支持VLA-1介导的NB100细胞与配体I型胶原的黏附。相比之下，单独的Ca2+不会诱导VLA-1的激活，但对Mg(2+)支持的细胞黏附具有强烈的抑制作用。我们还证明，整合素β1亚基特异性刺激单克隆抗体TS2/16可直接激活VLA-1，从而使NB100细胞有效黏附于I型胶原。通过使用一种新型的阻断VLA-α1特异性单克隆抗体5E8D9，本研究得以实现。
