Lipoprotein-X (Lp-X) is an abnormal low-density lipoprotein frequently found in liver disease. It is regarded as the most sensitive and specific biochemical parameter for the diagnosis of intra-and extrahepatic cholestasis. Moreover, Lp-X is supposed to contribute to the development of hypercholesterolemia in cholestatic liver disease, because it fails to inhibit de novo cholesterol synthesis. This investigation will focus on the relationship between the presence of Lp-X and serum lipid concentrations in cirrhosis. The significance of Lp-X in the diagnosis of cholestasis, compared with alkaline phosphatase (AP), ␥-glutamyl transferase (GGT), and bilirubin levels, will be assessed as well. The present cross-sectional study includes 212 patients with histopathologically proven cirrhosis. The detection of Lp-X and the quantification of ␣-, -, and pre--cholesterol was based on agar gel electrophoresis and polyanion precipitation. For the characterization of liver function, the concentrations of albumin and bilirubin, the activities of liver enzymes, and coagulation times were assessed. In a subgroup of 40 individuals, liver biopsies were re-evaluated to confirm or exclude intrahepatic cholestasis. As a result, there was no association between the appearance of Lp-X and total cholesterol concentrations. While all patients with Lp-X showed intrahepatic cholestasis (predictive value of the positive test Lipoprotein-X (Lp-X), an abnormal low-density lipoprotein, is present in patients with intra-or extrahepatic cholestasis, 1-3 in patients with familial lecithin:cholesterol acyltransferase (LCAT) deficiency, 4,5 and in newborn infants with immature liver function. 6 Lp-X is a lamellar particle of 30 to 70 nm in diameter as revealed by electron microscopy. It is characterized by its high content of phospholipids (66% by weight) and unesterified cholesterol (22%), and its low content of proteins (6%), cholesterol esters (3%), and triglycerides (3%). 7 The protein component is dominated by albumin, located in the core, and by apolipoprotein C, located on the surface of the particle. 8 Using zonal ultracentrifugation, Lp-X can be divided into three distinct populations: Lp-X 1 , Lp-X 2 , and Lp-X 3 , differing in density and apolipoprotein composition. 9 Unlike all other lipoproteins, Lp-X migrates to the cathode on agar gel electrophoresis. 7