Fibroblast remodeling of adsorbed collagen type IV is altered in contact with cancer cells.
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 beta1 and alpha2 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.
Maneva-Radicheva
L
L
Institute of Biophysics, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Ebert
U
U
Dimoudis
N
N
Altankov
G
G
D000230:Adenocarcinoma / Q000378:metabolism* / Q000473:pathology; D000327:Adsorption; D018920:Coculture Techniques; D024141:Collagen Type IV / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D004789:Enzyme Activation; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000378:metabolism; D008175:Lung Neoplasms / Q000378:metabolism* / Q000473:pathology; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism; D008856:Microscopy, Fluorescence; D012867:Skin / Q000166:cytology / Q000378:metabolism
D024141:Collagen Type IV; D016023:Integrins; D020778:Matrix Metalloproteinase 2