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Detection of Activity in the Conditioned Medium of Ethanol‐Treated HepG2 Cells which Stimulates Collagen Synthesis in IMR‐90 Cells
Author(s) -
Inui Noriaki,
Kato Junji,
Kohgo Yutaka,
Katsuki Shinichi,
Niitsu Yoshiro
Publication year - 1996
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1996.tb01732.x
Subject(s) - acetaldehyde , ethanol , chemistry , cell culture , trypsin , procollagen peptidase , fibroblast , biochemistry , hepatic stellate cell , fibrosis , medicine , in vitro , endocrinology , microbiology and biotechnology , biology , enzyme , genetics
Hepatic fibrosis often occurs in alcoholic liver diseases without accompanying tissue necrosis or inflammation. However, the precise mechanism of this fibrosis has not been fully clarified. In the present study, using the hepatoblastoma cell line HepG2 as a model for hepatocytes, we identified a factor that stimulates collagen synthesis of fibroblasts in a conditioned medium of HepG2 cells after treatment with ethanol. Type I procollagen peptide (PIC) in a culture of human fibroblast IMR‐90 markedly increased after incubation with the conditioned medium of ethanol‐treated HepG2 cells. The stimulating activity on the production of PIC by IMR‐90 remained after the dialysis and evaporation of the conditioned medium of HepG2 cells, indicating this factor was not as volatile from low molecular substances such as acetaldehyde, acetate, or lactate. The activity of this factor diminished with heat or trypsin treatment. A gel chromatographic analysis disclosed that the molecular weight of this factor was ˜8000 Da. These results suggest that a polypeptide factor secreted from HepG2 cells by treatment with ethanol stimulates collagen synthesis of fibroblasts.