Matrix-metalloproteinases in bronchopulmonary carcinomas

C. Martinella-Catusse1, B. Nawrocki1, C. Gilles2, P. Birembaut1 and M. Polette1

1I.N.S.E.R.M. U. 514 and Laboratoire Pol Bouin-C.H.U. de Reims, France, 2Laboratory of Biology of Tumours and Development-C.H.U. Sart-Tilman-Liège, Belgique

Offprint requests to: Dr. Myriam Polette, I.N.S.E.R.M. U.314, 45, rue Cognacq-Jay, 51100 Reims, France

Summary. Matrix metalloproteinases (MMPs) represent a group of enzymes involved in the degradation of most of the components of the extracellular matrix and therefore participate in tumoural invasion. MMPs, especially gelatinases A and B, MT1-MMP, the activator of gelatinase A, and stromelysin-3 were found over-expressed in many cancers including bronchopulmonary carcinomas. In vivo observations revealed that fibroblasts are the principal source of production of MMPs. Some of these enzymes such as MT1-MMP and stromelysin 3, displayed a focal stromal localisation near preinvasive and invasive tumour clusters. Futhermore, some tumour cell lines were shown to stimulate the expression of MT1-MMP by fibroblasts. All these in vivo and in vitro results suggest that certain tumour cells produce diffusible factors which could influence the MMP stromal expression. Among these factors, the TCSF (Tumor Collagenase Stimulatory Factor) which is known to upregulate some MMPs in vitro could be a good candidate for this stromal regulation, since it is produced by bronchial tumour cells in vivo. In this review, we address such a cooperation between tumour and stromal cells for the production of MMPs and emphasize their necessity for tumoural progression in bronchopulmonary carcinomas. Histol. Histopathol. 14, 839-843 (1999)

Key words: Metalloproteinases, Bronchopulmonary cancer, Tumour invasion

DOI: 10.14670/HH-14.839