Article
Immunohistochemical localization of matrix metalloproteinase 2 and its specific inhibitor TIMP-2 in neoplastic tissues with monoclonal antibodies.
International journal of cancer - 15 Feb 1994
Höyhtyä M, Fridman R, Komarek D, Porter-Jordan K, Stetler-Stevenson W G, Liotta L A, Liang C M
Abstract excerpt
Matrix metalloproteinase-2 (MMP-2), synthesized as a 631 amino-acid proenzyme, is activated by cleavage of the first 80 amino acids and naturally inhibited by tissue inhibitor of metalloproteinase-2 (TIMP-2). We report here the production of MAbs against MMP-2 and TIMP-2 and their use in localizing the respective antigens on tumor tissues. The anti-MMP-2 MAb recognized the latent and activated MMP-2 mutant...
Topics
- Animals
- Antibodies, Monoclonal
- Binding Sites, Antibody
- Breast Neoplasms
- Cell Membrane
- Colonic Neoplasms
- Cytoplasm
- Enzyme Activation
- Female
- Gelatinases
- Humans