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Differences between rat liver epithelial and fibroblast cells in metabolism of purines
Author(s) -
Berman Jules J.,
Tong Charles,
Williams Gary M.
Publication year - 1980
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041030304
Subject(s) - hypoxanthine , inosine , purine nucleoside phosphorylase , biochemistry , fibroblast , purine metabolism , nucleoside , chemistry , microbiology and biotechnology , thymidine , biology , purine , adenosine , enzyme , dna , in vitro
Epithelial and fibroblast cells from adult rat liver were found to differ markedly in their metabolism of the purine hypoxanthine. Both cell types took up hypoxanthine and possessed hypoxanthine‐guanine phosphoribosyl transferase for phosphoribosylating the purine. However, in the transferase assay, lysates from epithelial cells converted hypoxanthine predominantly to inosine monophosphate, with small amounts of the nucleoside inosine as product, whereas fibroblast cell lysates converted hypoxanthine predominantly to inosine. The inosine appeared not to be produced by direct ribosylation of the base, since fibroblast cell lysates had less purine nucleoside phosphorylase activity than epithelial cell lysates. Rather, the inosine produced by fibroblast lysates appeared to be derived from inosine monophosphate through catabolism of the mononucleotide by 5′ nucleotidase. An inhibitor of 5′ nucleotidase, thymidine triphosphate, reduced the amount of inosine formed.