Publication: Fibroblast remodeling of adsorbed collagen type IV is altered in contact with cancer cells
Loading...
Date
2008
Authors
Maneva-Radicheva, L. ; Ebert, U. ; Dimoudis, N. ; Altankov, G.
item.page.secondaryauthor
item.page.director
Publisher
Murcia : F. Hernández
publication.page.editor
publication.page.department
DOI
item.page.type
info:eu-repo/semantics/article
Description
Abstract
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
a2 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.
publication.page.subject
Citation
item.page.embargo
Ir a Estadísticas
Sin licencia Creative Commons.