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. 1982 Jan 15;202(1):211–216. doi: 10.1042/bj2020211

The role of cytosolic proteins in the intracellular transport of haem in rat liver. A dual-label approach.

D M Davies, H H Liem, E F Johnson, U Muller-Eberhard
PMCID: PMC1158093  PMID: 7082309

Abstract

After consecutive injections of delta-amino[3H]- and -[14C]-laevulinic acid, the incorporation of the two labels into haem associated with different subfractions of the liver was determined. Marked differences in the 14C/3H ratios were observed between haem associated loosely and tightly with microsomes and mitochondria and haem associated with three subfractions of the cytosol obtained by gel filtration. The effect of changing the amounts of delta-aminolaevulinic acid injected and of changing the interval between injections and killing of the animal on the ratios of labels in the haem of each subfraction was studied. The results are discussed in terms of the flow of haem from the mitochondria to other parts of the cell via putative cytosolic carrier proteins.

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Selected References

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

  1. Arias I. M., Doyle D., Schimke R. T. Studies on the synthesis and degradation of proteins of the endoplasmic reticulum of rat liver. J Biol Chem. 1969 Jun 25;244(12):3303–3315. [PubMed] [Google Scholar]
  2. Bissell D. M., Liem H. H., Muller-Eberhard U. Secretion of haem by hepatic parenchymal cells. Biochem J. 1979 Dec 15;184(3):689–694. doi: 10.1042/bj1840689. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Davies D. M., Smith A., Muller-Eberhard U., Morgan W. T. Hepatic subcellular metabolism of heme from heme-hemopexin: incorporation of iron into ferritin. Biochem Biophys Res Commun. 1979 Dec 28;91(4):1504–1511. doi: 10.1016/0006-291x(79)91235-x. [DOI] [PubMed] [Google Scholar]
  4. De Matteis F. Loss of haem in rat liver caused by the porphyrogenic agent 2-allyl-2-isopropylacetamide. Biochem J. 1971 Oct;124(4):767–777. doi: 10.1042/bj1240767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Druyan R., Kelly A. The effect of exogenous -aminolaevulinate on rat liver haem and cytochromes. Biochem J. 1972 Oct;129(5):1095–1099. doi: 10.1042/bj1291095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Eyster M. E., Edgington T. S., Liem H. H., Muller-Eberhard U. Plasma hemopexin levels following aortic valve replacement: a valuable screening test for assessing the severity of cardiac hemolysis. J Lab Clin Med. 1972 Jul;80(1):112–116. [PubMed] [Google Scholar]
  7. Farrell G. C., Gollan J. L., Schmid R. Efflux of bilirubin into plasma following hepatic degradation of exogenous heme. Proc Soc Exp Biol Med. 1980 Apr;163(4):504–509. doi: 10.3181/00379727-163-40805. [DOI] [PubMed] [Google Scholar]
  8. GREENFIELD R. E., PRICE V. E. Liver catalase. III. Isolation of catalase from mitochondrial fractions of polyvinylpyrrolidonesucrose homogenates. J Biol Chem. 1956 Jun;220(2):607–618. [PubMed] [Google Scholar]
  9. Garner R. C., McLean A. E. Separation of haem incorporation from protein synthesis in liver microsomes. Biochem Biophys Res Commun. 1969 Dec 4;37(6):883–887. doi: 10.1016/0006-291x(69)90213-7. [DOI] [PubMed] [Google Scholar]
  10. Granick S., Sinclair P., Sassa S., Grieninger G. Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and a spectrofluorometric assay for porphyrin composition. J Biol Chem. 1975 Dec 25;250(24):9215–9225. [PubMed] [Google Scholar]
  11. Habig W. H., Pabst M. J., Fleischner G., Gatmaitan Z., Arias I. M., Jakoby W. B. The identity of glutathione S-transferase B with ligandin, a major binding protein of liver. Proc Natl Acad Sci U S A. 1974 Oct;71(10):3879–3882. doi: 10.1073/pnas.71.10.3879. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hayashi N., Terasawa M., Yamauchi K., Kikuchi G. Effects of hemin on the synthesis and intracellular translocation of delta-aminolevulinate synthase in the liver of rats treated with 3,5-dicarbethoxy-1,4-dihydrocollidine. J Biochem. 1980 Nov;88(5):1537–1543. doi: 10.1093/oxfordjournals.jbchem.a133124. [DOI] [PubMed] [Google Scholar]
  13. Husby P., Müller-Eberhard U., Romslo I. Effect of hemopexin on the efflux of metalloporphyrin from isolated rat liver mitochondria. Biochem Biophys Res Commun. 1980 Jun 30;94(4):1345–1352. doi: 10.1016/0006-291x(80)90567-7. [DOI] [PubMed] [Google Scholar]
  14. Jones M. S., Jones O. T. The structural organization of haem synthesis in rat liver mitochondria. Biochem J. 1969 Jul;113(3):507–514. doi: 10.1042/bj1130507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ketterer B., Srai K. S., Christodoulides L. Haem-binding proteins of the rat liver cytosol. Biochim Biophys Acta. 1976 May 28;428(3):683–689. doi: 10.1016/0304-4165(76)90198-7. [DOI] [PubMed] [Google Scholar]
  16. Lazarow P. B., de Duve C. The synthesis and turnover of rat liver of rat liver peroxisomes. IV. Biochemical pathway of catalase synthesis. J Cell Biol. 1973 Nov;59(2 Pt 1):491–506. doi: 10.1083/jcb.59.2.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. MAUZERALL D., GRANICK S. The occurrence and determination of delta-amino-levulinic acid and porphobilinogen in urine. J Biol Chem. 1956 Mar;219(1):435–446. [PubMed] [Google Scholar]
  18. OMURA T., SATO R. THE CARBON MONOXIDE-BINDING PIGMENT OF LIVER MICROSOMES. II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES. J Biol Chem. 1964 Jul;239:2379–2385. [PubMed] [Google Scholar]
  19. Schnaitman C., Erwin V. G., Greenawalt J. W. The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol. 1967 Mar;32(3):719–735. doi: 10.1083/jcb.32.3.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Taketani S., Tokunaga R. Heme transport from rat liver mitochondria to the microsomes in vitro. Biochem Biophys Res Commun. 1980 Feb 27;92(4):1343–1347. doi: 10.1016/0006-291x(80)90433-7. [DOI] [PubMed] [Google Scholar]
  21. Watson C. J., Pierach C. A., Bossenmaier I., Cardinal R. Postulated deficiency of hepatic heme and repair by hematin infusions in the "inducible" hepatic porphyrias. Proc Natl Acad Sci U S A. 1977 May;74(5):2118–2120. doi: 10.1073/pnas.74.5.2118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. White I. N., Liem H. H., Muller-Eberhard U. Removal of exogenous haem or haemoglobin from rat liver microsomes. Anal Biochem. 1978 Sep;89(2):572–580. doi: 10.1016/0003-2697(78)90386-x. [DOI] [PubMed] [Google Scholar]
  23. Yamauchi K., Hayashi N., Kikuchi G. Translocation of delta-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by hemin in the rat liver. J Biol Chem. 1980 Feb 25;255(4):1746–1751. [PubMed] [Google Scholar]
  24. Yannoni C. Z., Robinson S. H. Early labeled heme synthesis from delta-aminolevulinic acid-4-[14C] in rats: comparison with glycine-2-[14C]. Proc Soc Exp Biol Med. 1978 Jul;158(3):466–470. doi: 10.3181/00379727-158-40227. [DOI] [PubMed] [Google Scholar]
  25. Yoda B., Israels L. G. Transfer of heme from mitochondria in rat liver cells. Can J Biochem. 1972 Jun;50(6):633–637. doi: 10.1139/o72-087. [DOI] [PubMed] [Google Scholar]

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