Staatz W D, Walsh J J, Santoro S A
Department of Pathology, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Biochem Mol Biol Int. 1997 Jul;42(3):577-82. doi: 10.1080/15216549700202981.
The adhesion of platelets and other cells to type I collagen is mediated by the alpha 2 beta 1 integrin. A binding site for the alpha 2 beta 1 integrin within the alpha 1(I) collagen chain has previously been localized to the cyanogen bromide fragment alpha 1(I)-CB3. We noe show by use of inhibitory monoclonal antibodies against the alpha 2 beta 1 integrin, that platelets also adhere to purified alpha 2(I) collagen chains by a mechanism mediated by the alpha 2 beta 1 integrin. Moreover, following isolation of cyanogen bromide fragments of the alpha 2(I) collagen chain by HPLC, we demonstrate that alpha 2 beta 1 integrin-mediated adhesion is restricted to the CB4 fragment of the alpha 2(I) collagen polypeptide. These findings indicate the presence of at least two spatially distinct binding sites for the alpha 2 beta 1 integrin on the native type I collagen triple helix.
血小板和其他细胞与I型胶原的黏附是由α2β1整合素介导的。先前已将α1(I)胶原链内α2β1整合素的结合位点定位到溴化氰片段α1(I)-CB3。我们现在通过使用针对α2β1整合素的抑制性单克隆抗体表明,血小板也通过α2β1整合素介导的机制黏附于纯化的α2(I)胶原链。此外,通过高效液相色谱法分离α2(I)胶原链的溴化氰片段后,我们证明α2β1整合素介导的黏附仅限于α2(I)胶原多肽的CB4片段。这些发现表明,在天然I型胶原三螺旋上存在至少两个空间上不同的α2β1整合素结合位点。