ASIALOGLYCOPROTEIN RECEPTOR IN HUMAN ISOLATED HEPATOCYTES FROM NORMAL LIVER AND ITS APPARENT INCREASE IN LIVER WITH HISTOLOGICAL ALTERATIONS

We have characterized a binding site for galactosyl terminal glycoproteins in hepatocytes isolated from human biopsies. The binding of asialoorosomucoid on hepatocytes previously treated by Triton X-100 was saturable, calcium-dependent and highly affine (K(a) = 1.11 +/- 0.87.10(9) M-1) thus corresponding to a ligand-receptor binding. The total number of receptors in the normal human liver was 140 000 +/- 65 000 sites per cell. This corresponded to the value obtained in the human hepatoma cell line HepG2, but was significantly lower than for isolated rat hepatocytes. Furthermore, in hepatocytes isolated from livers with histological features of either fibrosis, cirrhosis, hepatocarcinoma with cirrhosis or nodular regenerative hyperplasia, the number of asialoglycoprotein receptors per cell was increased, while the binding affinity was unchanged.