The influence of nerve section on the metabolism of polyamines in rat diaphragm muscle
- PMID: 7316998
- PMCID: PMC1163034
- DOI: 10.1042/bj1960603
The influence of nerve section on the metabolism of polyamines in rat diaphragm muscle
Abstract
Concentrations of spermidine, spermine and putrescine have been measured in rat diaphragm muscle after unilateral nerve section. The concentration of putrescine increased approx. 10-fold 2 days after nerve section, that of spermidine about 3-fold by day 3, whereas an increase in the concentration of spermine was only observed after 7-10 days. It was not possible to show enhanced uptake of either exogenous putrescine or spermidine by the isolated tissue during the hypertrophy. Consistent with the accumulation of putrescine, activity of ornithine decarboxylase increased within 1 day of nerve section, was maximally elevated by the second day and then declined. Synthesis of spermidine from [14C]putrescine and either methionine or S-adenosylmethionine bt diaphragm cytosol rose within 1 day of nerve section, but by day 3 had returned to normal or below normal values. Activity of adenosylmethionine decarboxylase similarly increased within 1 day of nerve section, but by day 3 had declined to below normal values. Activity of methionine adenosyltransferase was elevated throughout the period studied. The concentration of S-adenosylmethionine was likewise enhanced during hypertrophy. Administration of methylglyoxal bis(guanylhydrazone) produced a marked increase in adenosylmethionine decarboxylase activity and a large increase in putrescine concentration, but did not prevent the rise in spermidine concentration produced by denervation. Possible regulatory mechanisms of polyamine metabolism consistent with the observations are discussed.
Similar articles
-
Effects of inhibitors of ornithine and S-adenosylmethionine decarboxylases on L6 myoblast proliferation.J Cell Physiol. 1982 Feb;110(2):161-8. doi: 10.1002/jcp.1041100209. J Cell Physiol. 1982. PMID: 6802862
-
The role of polyamine depletion and accumulation of decarboxylated S-adenosylmethionine in the inhibition of growth of SV-3T3 cells treated with alpha-difluoromethylornithine.Biochem J. 1984 Nov 15;224(1):29-38. doi: 10.1042/bj2240029. Biochem J. 1984. PMID: 6439194 Free PMC article.
-
Polyamine regulation of ornithine decarboxylase and its antizyme in intestinal epithelial cells.Am J Physiol Gastrointest Liver Physiol. 2001 Jan;280(1):G130-8. doi: 10.1152/ajpgi.2001.280.1.G130. Am J Physiol Gastrointest Liver Physiol. 2001. PMID: 11123206
-
S-adenosylmethionine decarboxylase as target of chemotherapy.Adv Enzyme Regul. 1985;24:125-39. doi: 10.1016/0065-2571(85)90073-1. Adv Enzyme Regul. 1985. PMID: 3939095 Review.
-
On the development of specific inhibitors of animal polyamine biosynthetic enzymes.Ital J Biochem. 1976 Jan-Feb;25(1):5-32. Ital J Biochem. 1976. PMID: 5386 Review. No abstract available.
Cited by
-
Differences between tissues in response of S-adenosylmethionine decarboxylase to administration of polyamines.Biochem J. 1981 Dec 15;200(3):629-37. doi: 10.1042/bj2000629. Biochem J. 1981. PMID: 7342972 Free PMC article.
-
Early events in the response of fast skeletal muscle to chronic low-frequency stimulation. Polyamine biosynthesis and protein phosphorylation.Biochem J. 1982 Aug 15;206(2):211-9. doi: 10.1042/bj2060211. Biochem J. 1982. PMID: 7150242 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous