Messent A J, Tuckwell D S, Knäuper V, Humphries M J, Murphy G, Gavrilovic J
Strangeways Research Laboratory, Worts Causeway, Cambridge, UK.
J Cell Sci. 1998 Apr;111 ( Pt 8):1127-35. doi: 10.1242/jcs.111.8.1127.
In this paper we show that collagenase-3 cleavage of type I collagen has a marked effect on alpha2beta1 integrin-mediated interactions with the collagen fragments generated. Isolated alpha2beta1 integrin and alpha2 integrin A-domain were found to bind to both native collagen and native 3/4 fragment and, to a lesser degree, native 1/4 fragment. Whole integrin and integrin A-domain binding were lost after heat denaturation of the collagen fragments. At physiological temperature, cell adhesion to triple-helical 3/4 fragment via alpha2beta1 integrin was still possible; however, no alpha2beta1 integrin-mediated adhesion to the 1/4 fragment was observed. Unwinding of the collagen fragment triple helices by heating to physiological temperatures prior to adsorption to plastic tissue culture plates resulted in total abrogation of HT1080 cell attachment to either fragment. These results provide significant evidence in support of a role for matrix-metalloproteinase cleavage of the extracellular matrix in modifying cell-matrix interactions.
在本文中，我们表明，I型胶原被胶原酶-3切割后，对α2β1整合素介导的与所产生的胶原片段的相互作用具有显著影响。研究发现，分离出的α2β1整合素和α2整合素A结构域既能与天然胶原结合，也能与天然3/4片段结合，与天然1/4片段的结合程度则较低。胶原片段经热变性后，完整整合素和整合素A结构域的结合能力丧失。在生理温度下，细胞仍可通过α2β1整合素与三螺旋3/4片段黏附；然而，未观察到α2β1整合素介导的与1/4片段的黏附。在吸附到塑料组织培养板之前，将胶原片段的三螺旋加热到生理温度使其解旋，导致HT1080细胞对这两种片段的黏附完全消失。这些结果为基质金属蛋白酶切割细胞外基质在改变细胞-基质相互作用中所起的作用提供了重要证据。
