腫瘤細胞可降解細胞外間質(Extracell ular matrix,ECM)成分以侵入其週遭組織。已知不正常的腫瘤細胞可分泌不同的ECM降解酵素包括賴金屬蛋白質酵素(Matrix metalloproteinase,MMP)、serine分解酵素及cathepsins。精確控制此等MMP之表現為許多正常過程所需。於MMP家族中膠原蛋白酵素A(gelatinase A)的調節方式與其他成分不同,因此建議其於細胞與間質間之相互作用中可能扮演獨特的角色,包括細胞侵入。為了探討於口腔癌細胞中MMP2對細胞附著性所扮演之角色,我們測定了細胞分泌於培養液中之MMP-2活性。結果顯示於72 kDa之膠原蛋白酵素原及64kDa活化型酵素活性可能為細胞癌化及附著能力之因子。
Tumor cells degrade extracellular matrix (ECM) components to invade surrounding tissue. Malignant tumor cells are known to produce various ECM-degrading enzymes including matrix metalloproteinases (MMPs), also called matrixins, serine proteinases and cathepsins. These Zn/sup +2/ and Ca/sup +2/-dependent MMPs precise regulation of their expression is crucial in many normal processes. One member of the matrixin family, gelatinase A, is regulated differently from other MMPs, suggesting that it may play a unique role in cell-matrix interactions, including cell inva sion. To study the role of MMP2 in adhesion of human oral cacinoma, we examined MMP -2 activity in medium. The data suggest that the enzyme activity of 72 kDa progelatinase A and active 64 kDa species may be a key event in the processing of cacinoma and acquisition of adhesion potential.
