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. 1974 Oct;144(1):115–122. doi: 10.1042/bj1440115

Activities of prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase in the liver of rats with hepatic injury

Juha Risteli 1, Kari I Kivirikko 1
PMCID: PMC1168471  PMID: 4376954

Abstract

The activities of four enzymes catalysing post-translational modifications of the collagen polypeptide chains were assayed in the livers of rats with experimental hepatic injury. The liver injury was induced by injecting carbon tetrachloride twice weekly, and assays of the enzymic activities were carried out 2 and 4 weeks after commencement of administration of carbon tetrachloride. The liver homogenates were preincubated with Triton X-100 before the assays, because such treatment was found to increase the activities of all four enzymes in the supernatants of liver homogenates. The activities of all four enzymes had increased by 2 weeks after commencement of carbon tetrachloride administration. No increase was found in the collagen content of the livers at this stage and thus an increase in all four enzyme activities preceded an increase in the collagen content of the liver. A further slight increase was found in three of the enzyme activities during the subsequent 2 weeks of the experiment, whereas no further increase was found in the collagen galactosyltransferase activity. A statistically significant correlation was found between all four enzyme activities, but the magnitude of the increases varied considerably. The largest increase was found in lysyl hydroxylase activity, and at 4 weeks the magnitude of this was about three times that of the collagen galactosyltransferase activity. The results thus indicate that the increased enzyme activities cannot be explained simply by an increase in the number of collagen-producing cells having similar enzyme activity patterns to those of the cells initially present in the liver.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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