Biosynthesis of abnormally glycosylated hepatoma secretory proteins in cell cultures.
We studied, by electrophoretic techniques, the physiochemical properties of 4 glycoproteins, alpha 1-antitrypsin, alpha 1-antichymotrypsin, alpha 1-acid glycoprotein and transferrin synthesized by three different human hepatoma cell lines. A common feature was the export of glycoproteins with retarded electrophoretic mobility, indicating incomplete sialylation, and a predominance of atypical, highly branched carbohydrate chains. The abnormal glycosylation pattern may be specific for malignant transformation of hepatocytes and possibly related to the intracellular accumulation of some of these proteins in malignant cells.
D006528:Carcinoma, Hepatocellular / Q000378:metabolism*; D002460:Cell Line; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000096:biosynthesis; D006023:Glycoproteins / Q000096:biosynthesis*; D006801:Humans; D007118:Immunoassay / Q000379:methods; D007123:Immunoelectrophoresis, Two-Dimensional; D008113:Liver Neoplasms / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000096:biosynthesis*; D009961:Orosomucoid / Q000096:biosynthesis; D014168:Transferrin / Q000096:biosynthesis; D000514:alpha 1-Antichymotrypsin; D000515:alpha 1-Antitrypsin / Q000096:biosynthesis
D006023:Glycoproteins; D009363:Neoplasm Proteins; D009961:Orosomucoid; D014168:Transferrin; D000514:alpha 1-Antichymotrypsin; D000515:alpha 1-Antitrypsin; D002918:Chymotrypsin