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. 1982 Jul 15;206(1):61–65. doi: 10.1042/bj2060061

ADP-ribosyl-protein conjugate subclasses in various tissues. Specific influence of thyroid hormone on liver conjugates.

C Lindner, H Hilz
PMCID: PMC1158549  PMID: 6289814

Abstract

The amounts of endogenous mono (ADP ribose)-protein conjugates and their hydroxyl-amine-sensitive and hydroxylamine-resistant subfractions in various tissues of the mouse were determined and compared with poly (ADP-ribose) conjugates. Total mono-(ADP-ribose) conjugates did not correlate with poly (ADP-ribose) residues or the cellularity of a tissue, but were related to the protein content and the amounts of NAD+ +NADH. The hydroxylamine-resistant subfraction, which in liver is mainly associated with the mitochondria [Adamietz, Wielckens, Bredehorst, Lengyel & Hilz (1981) Biochem. Biophys. Res, Commun. 101, 96-103], did not correlate with the tissue content of cytochrome c oxidase. In hypothyroid mice hydroxylamine-resistant mono (ADP-ribose) conjugates of the liver were increased by a factor of two while the hydroxylamine-sensitive conjugates did not change significantly under these conditions. Upon administration of thyroxine the hydroxylamine-resistant subfraction returned to normal.

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Selected References

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

  1. Adamietz P., Klapproth K., Hilz H. Isolation and partial characterization of the ADP-ribosylated nuclear proteins from Ehrlich ascites tumor cells. Biochem Biophys Res Commun. 1979 Dec 28;91(4):1232–1238. doi: 10.1016/0006-291x(79)91199-9. [DOI] [PubMed] [Google Scholar]
  2. Adamietz P., Wielckens K., Bredehorst R., Lengyel H., Hilz H. Subcellular distribution of mono(ADP-ribose) protein conjugates in rat liver. Biochem Biophys Res Commun. 1981 Jul 16;101(1):96–103. doi: 10.1016/s0006-291x(81)80015-0. [DOI] [PubMed] [Google Scholar]
  3. Bredehorst R., Klapproth K., Hilz H., Scheidegger C., Gerisch G. Protein-bound mono(ADP-ribose) residues in differentiating cells of Dictyostelium discoideum. Cell Differ. 1980 Apr;9(2):95–103. doi: 10.1016/0045-6039(80)90013-5. [DOI] [PubMed] [Google Scholar]
  4. Bredehorst R., Wielckens K., Adamietz P., Steinhagen-Thiessen E., Hilz H. Mono(ADP-ribosyl)ation and poly(ADP-ribosyl)ation of proteins in developing liver and in hepatomas: relation of conjugate subfractions to metabolic competence and proliferation rates. Eur J Biochem. 1981 Nov;120(2):267–274. doi: 10.1111/j.1432-1033.1981.tb05699.x. [DOI] [PubMed] [Google Scholar]
  5. Bredehorst R., Wielckens K., Gartemann A., Lengyel H., Klapproth K., Hilz H. Two different types of bonds linking single ADP-ribose residues covalently to proteins. Quantification in eukaryotic cells. Eur J Biochem. 1978 Dec 1;92(1):129–135. doi: 10.1111/j.1432-1033.1978.tb12730.x. [DOI] [PubMed] [Google Scholar]
  6. Gartemann A., Bredehorst R., Wielckens K., Strätling W. H., Hilz H. Mono- and poly-ADP-ribosylation of proteins in mouse kidney after castration and testosterone treatment. Biochem J. 1981 Jul 15;198(1):37–44. doi: 10.1042/bj1980037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hilz H. ADP-ribosylation of proteins--a multifunctional process. Hoppe Seylers Z Physiol Chem. 1981 Nov;362(11):1415–1425. [PubMed] [Google Scholar]
  8. Kun E., Zimber P. H., Chang A. C., Puschendorf B., Grunicke H. Macromolecular enzymatic product of NAD+ in liver mitochondria. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1436–1440. doi: 10.1073/pnas.72.4.1436. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Wielckens K., Garbrecht M., Kittler M., Hilz H. ADP-ribosylation of nuclear proteins in normal lymphocytes and in low-grade malignant non-Hodgkin lymphoma cells. Eur J Biochem. 1980 Feb;104(1):279–287. doi: 10.1111/j.1432-1033.1980.tb04426.x. [DOI] [PubMed] [Google Scholar]
  10. Wielckens K., Sachsenmaier W., Hilz H. Protein-gebundene Mono(Adenosindiphosphat-Ribose)-Spiegel während des Zellzyklus von Physarum polycephalum. Hoppe Seylers Z Physiol Chem. 1979 Jan;360(1):39–43. doi: 10.1515/bchm2.1979.360.1.39. [DOI] [PubMed] [Google Scholar]

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