title: Experimentally induced colon cancer metastases in rat liver increase the proliferation rate and capacity for purine catabolism in liver cells.
abstract: Metastases in rat liver were generated experimentally by intraportal injection of colon cancer cells to investigate the effects of cancerous growth on the metabolism of surrounding liver tissue. Maximum activities (capacity) of glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, lactate dehydrogenase, succinate dehydrogenase, alkaline phosphatase, 5'-nucleotidase, xanthine oxidoreductase, purine nucleoside phosphorylase and adenosine triphosphatase have been determined. Two types of metastases were found, a small type surrounded by stroma and a larger type in direct contact with hepatocytes. Both types affected the adjacent tissue in a similar way suggesting that the interactions were not mediated by stroma. High capacity of the degradation pathway of extracellular purines released from dead cells of either tumours or host tissue was found in stroma and sinusoidal cells. Metastases induced both an increase in the number of Kupffer cells and proliferation of hepatocytes. The distribution pattern in the liver lobulus of most enzymes investigated did not change distinctly. However, activity of alkaline phosphatase, succinate dehydrogenase and phosphogluconate dehydrogenase was increased in hepatocytes directly surrounding metastases. These data imply that the overall metabolic zonation in liver lobuli is not dramatically disturbed by the presence of cancer cells despite the fact that various metabolic processes in liver cells are affected.
authors.affiliation: Laboratory of Cell Biology and Histology, University of Amsterdam, The Netherlands.
authors.forename: G N
authors.initials: GN
authors.lastname: Jonges
authors.forename: I M
authors.initials: IM
authors.lastname: Vogels
authors.forename: K S
authors.initials: KS
authors.lastname: Bosch
authors.forename: K P
authors.initials: KP
authors.lastname: Dingemans
authors.forename: C J
authors.initials: CJ
authors.lastname: Van Noorden
mesh_terms: D015720:5'-Nucleotidase / Q000378:metabolism; D000230:Adenocarcinoma / Q000473:pathology* / Q000503:physiopathology / Q000556:secondary*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000469:Alkaline Phosphatase; D000818:Animals; D002455:Cell Division / Q000502:physiology; D003094:Collagen / Q000378:metabolism; D003110:Colonic Neoplasms / Q000473:pathology*; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D008112:Liver Glycogen / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000378:metabolism* / Q000503:physiopathology* / Q000556:secondary; D010088:Oxidoreductases / Q000378:metabolism; D011685:Purine Nucleotides / Q000378:metabolism; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism; D011687:Purines / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014969:Xanthine Oxidase / Q000378:metabolism
chemical_list: D008112:Liver Glycogen; D011685:Purine Nucleotides; D011687:Purines; D003094:Collagen; D010088:Oxidoreductases; D005954:Glucosephosphate Dehydrogenase; D014969:Xanthine Oxidase; D011683:Purine-Nucleoside Phosphorylase; D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase; D000251:Adenosine Triphosphatases