Immunocytochemical investigation of catalase and peroxisomal lipid β-oxidation enzymes in human hepatocellular tumors and liver cirrhosis

• Published in: Virchows Archiv : an international journal of pathology Vol. 435; no. 5; pp. 486 - 495
• Main Authors: LITWIN, J. A, BEIER, K, VÖLKL, A, HOFMANN, W. J, FAHIMI, H. D
• Format: Journal Article
• Language: English
• Published: Berlin Springer 01.11.1999
• Subjects: 3-Hydroxyacyl CoA Dehydrogenases - metabolism; Acetyl-CoA C-Acyltransferase - metabolism; Acyl-CoA Oxidase; Adenoma, Liver Cell - enzymology; Adenoma, Liver Cell - ultrastructure; Biological and medical sciences; Carcinoma, Hepatocellular - enzymology; Carcinoma, Hepatocellular - ultrastructure; Catalase - metabolism; Enoyl-CoA Hydratase - metabolism; Gastroenterology. Liver. Pancreas. Abdomen; Humans; Immunohistochemistry; Isomerases - metabolism; Lipid Metabolism; Liver Cirrhosis - enzymology; Liver Cirrhosis - pathology; Liver Neoplasms - enzymology; Liver Neoplasms - ultrastructure; Liver. Biliary tract. Portal circulation. Exocrine pancreas; Medical sciences; Multienzyme Complexes - metabolism; Oxidoreductases - metabolism; Peroxisomal Bifunctional Enzyme; Peroxisomes - enzymology; Tumors; Human; Immunohistochemistry; Enzyme; Liver; Hepatic disease; Hepatocellular carcinoma; Lipids; Malignant tumor; Carcinogenesis; Pathology; Cirrhosis; Peroxidases; Catalase; Peroxisome; Digestive diseases; Oxidation; Oxidoreductases
• ISSN: 0945-6317; 1432-2307
• DOI: 10.1007/s004280050432

A significant reduction of catalase activity, a peroxisomal marker enzyme, occurs in human hepatic neoplasias, but no information is available on other peroxisomal proteins. We have studied by means of immunohistochemistry four specific proteins of peroxisomes (catalase and three enzymes of lipid beta-oxidation) in human hepatocellular tumors of various differentiation grades from adenoma to anaplastic carcinoma. In all tumors, except the adenomas, the tumor cells contained fewer peroxisomes than extrafocal hepatocytes and the reduction of antigenic sites in the tumor types generally correlated with the degree of tumor dedifferentiation as assessed by classical histopathological criteria. Two poorly differentiated tumors had no detectable peroxisomes at all. There were no major differences in the intensities of the immunocytochemical staining for all four studied peroxisomal antigens in different tumors, suggesting that the neoplastic transformation affects the biogenesis of the entire organelle and not merely the individual peroxisomal enzyme proteins. Some tumors exhibited a distinct peripheral distribution of peroxisomes. In cases with associated liver cirrhosis, the hepatocytes in the adjacent liver showed marked peroxisome proliferation, forming large perinuclear aggregates, occupying occasionally the entire cytoplasm. Taken together, our observations indicate that peroxisomes are significantly altered in both hepatocellular tumors and liver cirrhosis and, thus, could be responsible for some of the metabolic derangements observed in those disease processes.