Formation of intercellular collagen matrix by cultured liver epithelial cells and loss of its ability in hepatocarcinogenesis in vitro.
Epithelial cells of normal rat liver origin (strain RL34) synthesized the alpha 1 peptide of type I collagen. In nononcogenic cultures (RL34 and RL34EC) and a marginally oncogenic culture (RL34HII), the peptide was continuously secreted from the proliferating cells. Part of the soluble peptide was incorporated into the intercellular matrix of contact-inhibited cells after confluency, while the remainder was degraded. The intercellular matrix contained characteristic collagen fibrils which were argyrophilic and revealed a 64 nm axial periodicity. Epithelial cells of an oncogenic culture (RL34HT) secreted procollagen into the medium continuously throughout their proliferative phases and were unable to accumulate collagen fibrils in the intercellular matrix. The depletion of collagen accumulation in the hepatocarcinoma cell culture was ascribed to lack of the binding of native collagen molecules to the cell membrane and the persistence of high proteolytic activity on the cell surface.
D000818:Animals; D002455:Cell Division; D002460:Cell Line; D003094:Collagen / Q000096:biosynthesis*; D008099:Liver / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D051381:Rats
D003094:Collagen