@article{oai:kanazawa-u.repo.nii.ac.jp:00027426,
 author = {Sato, Hiroshi and Seiki, Motoharu},
 issue = {2},
 journal = {Journal of Biochemistry},
 month = {Feb},
 note = {Activated gelatinase A is reportedly associated with tumor spread. We identified novel matrix metalloproteinases that localize on the cell surface and mediate the activation of progelatinase A. Thus, these progelatinase A activators were named membrane-type matrix metalloproteinase-1 and -2 (MT-MMP-1 and -2, respectively). MT-MMP-1 is overexpressed in malignant tumor tissues, including lung and stomach carcinomas that contain activated gelatinase A. This suggests that MT-MMP-1 is associated with the activation of progelatinase A in these tumor tissues. The expression of MT-MMP-1 also induced binding of gelatinase A to the cell surface by functioning as a receptor. The cell surface localization of proteinases has advantages over pericellular proteolysis. MT-MMP1 and its family may play a central role in the cell surface localization and activation of progelatinase A and via this mechanism, tumor cell use exogenous progelatinase A to mediate the proteolysis associated with invasion and metastasis., 金沢大学がん研究所がん病態制御},
 pages = {209--215},
 title = {Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis},
 volume = {119},
 year = {1996}
}