HISTOLOGY AND HISTOPATHOLOGY

Cellular and Molecular Biology

 

Fibroblast remodeling of adsorbed collagen type IV is altered in contact with cancer cells

L. Maneva-Radicheva1,4, U. Ebert2, N. Dimoudis2 and G. Altankov1,3

1Institute of Biophysics, Bulgarian Academy of Sciences, Sofia, Bulgaria, 2Roche Diagnostics GmbH, Pharma Research Penzberg, Penzberg, Germany, 3Institució Catalana de Recerca i Estudis Avançats (ICREA) and Institut de Bioenginyeria de Catalunya (IBEC) Parc Scientific de Barcelona, Josep Samitier 1-5, Barcelona, Spain and 4Medical University, Medical Faculty, Sofia, Bulgaria.

Offprint requests to: Prof. Dr. G. Altankov, MD, PhD, Parc Scientific de Barcelona, Josep Samitier 1-5, 08028-Barcelona, Spain. e-mail: altankov@bio21.bas.bg


Summary. A series of co-culture experiments between fibroblasts and H-460 human lung carcinoma cells were performed to learn more about the fate of adsorbed type IV collagen (Coll IV). Fibroblasts were able to spatially rearrange Coll IV in a specific linear pattern, similar but not identical to the fibronectin (FN) fibrils. Coll IV partly co-aligns with fibroblast actin cytoskeleton and transiently co-localize with FN, as well as with ß1 and α2 integrin clusters, suggesting a cell-dependent process. We further found that this Coll IV reorganization is suppressed in contact with H460 cells. Zymography revealed strongly elevated MMP-2 activity in supernatants of co-cultures, but no activity when fibroblasts or cancer cells were cultured alone. Thus, we provide evidence that reorganization of substrate associated Coll IV is a useful morphological approach for in vitro studies on matrix remodeling activity during tumorigenesis. Histol Histopathol 23, 833-842 (2008)

Key words: Adsorbed collagen IV reorganization, Fibroblasts and cancer cells co-culture, MMP-2

DOI: 10.14670/HH-23.833