Molecular heterogeneity of alpha-fetoprotein secreted by primary and transplantable hepatocellular carcinomas

✍ Scribed by Philip C. Kelleher; Carol J. Smith

• Publisher: John Wiley and Sons
• Year: 1979
• Tongue: French
• Weight: 645 KB
• Volume: 24
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910240310

✦ Synopsis

Abstract

Due to differences in carbohydrate content, rat AFP exhibits concanavalin A (Con A)‐binding heterogeneity. In order to investigate the control of the glycosylation of AFP synthesized by malignant cells, the patterns of AFP Con A affinity molecular variants secreted by sixteen 3′‐methyl‐4‐dimethyl‐aminoazobenzene‐induced primary hepatocellular carcinomas were followed sequentially during growth of the primary tumors through establishment as transplantable hepatocellular carcinomas. Fourteen of the transplantable tumors showed stable patterns of serum AFP Con A affinity molecular variants. Five of these 14 tumors secreted patterns of AFP Con A affinity molecular variants similar to the patterns found in the sera of the rats bearing the primary tumor of origin; the remainder of the tumors secreted an AFP Con A affinity molecular variant pattern which bore no relationship to that of the primary hepatocellular carcinoma of origin. Two of the transplantable hepatocellular carcinomas did not secrete stable proportions of AFP Con A affinity molecular variants during the 2‐year study. In 14 transplantable hepatoma lines the patterns of AFP Con A affinity molecular variants throughout successive transplant generations were significantly different from the pattern found in newborn rat serum. The stability of AFP Con A affinity molecular variant secretion by transplantable hepatocellular carcinomas indicates that the control of glycosylation of AFP and perhaps of other proteins is a heritable phenotypic property of these tumors and is consistent with other observations that the metabolic activities of transplantable hepatocellular carcinomas are constant over a period of years.