Fetal Phenotypic Expression by Adult Rat Hepatocytes on Collagen Gel/Nylon Meshes

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 76; no. 1; pp. 283 - 287
• Main Authors: Sirica, Alphonse E., Richards, William, Tsukada, Yutaka, Sattler, Carol A., Pitot, Henry C.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 01.01.1979; National Acad Sciences
• Subjects: Albumins; alpha-Fetoproteins - metabolism; Animals; Cells; Cells, Cultured; Collagen; Collagens; Culture Media; Cultured cells; DNA; DNA - biosynthesis; Enzymes; Exhibitions; gamma-Glutamyltransferase - metabolism; Gels; Hepatocytes; Isoenzymes - metabolism; Liver - metabolism; Liver - ultrastructure; Liver cells; Orosomucoid - metabolism; Phenotype; Rats; Serum Albumin - metabolism; Transferrin - metabolism
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.76.1.283

Hepatocytes from adult rats were maintained in primary culture for up to 10-13 days on nylon meshes coated with a thin layer of rat tail collagen gel. Their ultrastructure closely resembled that of the liver parenchymal cell in vivo, but hepatocytes in late culture exhibited a pronounced buildup of microfilaments beneath their apical cell surface. Hepatocytes in early and late cultures secreted albumin, transferrin, and α1-acid glycoprotein into the medium; they exhibited a 7- to 10-fold induction of tyrosine aminotransferase activity by dexamethasone; and they expressed an alkaline phosphatase that was similar to that of normal rat liver with respect to its inhibition by the liver enzyme inhibitor L-homoarginine. In addition, the hepatocytes in culture demonstrated phenotypic changes characteristic of fetal liver parenchymal cells. These changes, which paralleled an increase in DNA synthesis, included the expression of and linear increase in the activity of the fetal liver cell enzyme γ -glutamyl transpeptidase, an increased production of α1-fetoprotein, and a change in the substrate specificity of fructose-bisphosphate aldolase to that of the fetal liver isozyme.