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The Effects of Progesterone Administration on Hepatic Endoplasmic Reticulum: An Electron Microscopic and Biochemical Study

  • A. L. Jones
  • J. B. Emans

Abstract

It is now well known that there are tiny membrane-limited channels ramifying throughout the cytoplasm of most cells. Porter (24) was the first to describe this lace-like reticulum of membranes with the electron microscope. Because of its association with the endoplasmic portion of the cell rather than the ectoplasm, it was referred to as the “endoplasmic reticulum” (25,26). In 1955, Fawcett (7) noted that two forms of the endoplasmic reticulum existed in the hepatic parenchymal cell. One form consisted of a system of membranes studded with ribosomes (rough-surfaced endoplasmic reticulum) and the other consisted of only a membranous network (smooth-surfaced endoplasmic reticulum).

Keywords

Endoplasmic Reticulum Microsomal Enzyme Smooth Endoplasmic Reticulum Male Hamster Hepatic Parenchymal Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Cardell, R.R. Subcellular alterations in rat liver following hypophysectory. Biochem. Biophys. Acta 148:539 (1967).PubMedCrossRefGoogle Scholar
  2. 2.
    Conney, A.H. Pharmacological implications of microsomal enzyme induction. Pharm. Rev. 19: 317 (1967).PubMedGoogle Scholar
  3. 3.
    Conney, A.H., Schneidman, K., Jacobson, M., and Kuntzman, R. Drug induced changes in steroid metabolism. Am. N.Y. Acad. Sci. 123: (Art. 1) 98 (1965).Google Scholar
  4. 4.
    Dallner, D., and Emster, L. Sub fractionation and composition of microsomal membranes: A review. J. Histochem. Cytochem. 16:611 (1968).PubMedCrossRefGoogle Scholar
  5. 5.
    Emans, J.B., and Jones, A.L. Hypertrophy of liver cell smooth surfaced reticulum following progesterone administration. J. Histochem. Cytochem. 16:561 (1968).PubMedCrossRefGoogle Scholar
  6. 6.
    Fouts, J.R., Rogers, L.A., and Gram, T.E. The metabolism of drugs by hepatic microsomal enzymes. Studies on intramicroso- mal distribution of enzymes and relationships between enzyme activity and structure of the hepatic endoplasmic reticulum. Exp. Molec. Path. 5:475 (1966).PubMedCrossRefGoogle Scholar
  7. 7.
    Fawcett, D.W. Obsearvations on the cytology and electron microscopy of hepatic cells. J. Nat. Cancer Inst. 15:1475 (1955).PubMedGoogle Scholar
  8. 8.
    Fawcett, D.W. Structural and functional variations in the membranes of the cytoplasm. In Intracellular Membraneous Structure, p. 15. Japan Society for Cell Biology, Okayama (1965).Google Scholar
  9. 9.
    Glaumann, H., and Dallner, G. Lipid composition and turnover of rough and smooth microsomal membranes in rat liver. J. Lipid Res. 1:720 (1968).Google Scholar
  10. 10.
    Granick, S. The induction in vitro of the synthesis of δ aminolevulinic acid synthetase in chemical porphyria: a response to certain drugs, sex hormones, and foreign chemicals. J. Biol. Chem. 241: 1359 (1966).PubMedGoogle Scholar
  11. 11.
    Hutterer, F., Schaffner, F., Klion, F.M., and Popper, H. Hypertrophie, hypoactive smooth endoplasmic reticulum: a sensitive indicator of hepatotoxicity exemplified by Dieldrin. Science 161:1017 (1968).PubMedCrossRefGoogle Scholar
  12. 12.
    Jick, H., and Shuster, L. The turnover of microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome reductase in the livers of mice treated with phenobarbital. J. Biol. Chem. 241:5366 (1966).PubMedGoogle Scholar
  13. 13.
    Jones, A.L., and Armstrong, D.T. Increased cholesterol biosynthesis following phenobarbital induced hypertrophy of agranular reticulum in liver. Proc. Soc. Exp. Biol. Med. 119: 1136 (1965).PubMedGoogle Scholar
  14. 14.
    Jones, A.L., and Fawcett, D.W. Hypertrophy of the agranular endoplasmic reticulum in hamster liver induced by phenobarbital (with a review on the function of this organelle in liver). J. Histochem. Cytochem. 14: 215 (1966).PubMedCrossRefGoogle Scholar
  15. 15.
    Jones, A.L., Ruderman, N.B., and Herrera, M.G. Electron microscopic and biochemical study of lipoprotein synthesis in the isolated perfused rat liver. J. Lipid Research 8: 429 (1967).Google Scholar
  16. 16.
    Kadenback, B. Synthesis of mitochondrial proteins: demonstration of a transfer of proteins from microsomes into mitochondria. Biochem. Biophys. Acta 134:430 (1966).Google Scholar
  17. 17.
    Kuntzman, R., Lawrence, D., and Conney, A.H. Michaelis constants for the hydroxylation of steroid hormones and drugs by rat liver microsomes. Molec. Pharmacol. 1:163 (1965).Google Scholar
  18. 18.
    Marver, H.S., Tschudy, D.P., Perlroth, M.G., and Collins, A. 6 aminolevulinic acid synthetase: I. Studies in liver homogenates. J. Biol. Chem. 241:2803 (1966).PubMedGoogle Scholar
  19. 19.
    Marver, H.S., Tschudy, D.P., Perlroth, M.G., and Collins, A. 6 aminolevulinic acid synthetase: II. Induction in rat liver. J. Biol. Chem. 241:4323 (1966).PubMedGoogle Scholar
  20. 20.
    McKay, R., Druyan, R., and Rabinowity, M. Intramitochondrial loci for 6 aminoleuvulinic acid synthetase and ferrochelatase. Fed. Proceed. 27: 774 (1968).Google Scholar
  21. 21.
    Omura, T., and Sato, R. The carbon monoxide binding pigment of liver microsomes. J. Biol. Chem. 239:2370 (1964).PubMedGoogle Scholar
  22. 22.
    Orrenius, S., and Ericsson, J.L.E. Enzyme-menibrane relationship in phenobarbital induction of synthesis of drug- metabolizing enzyme system and proliferation of endoplasmic reticulum. J. Cell Biol. 28: 181 (1966).PubMedCrossRefGoogle Scholar
  23. 23.
    Orrenius S., and Ericsson, J.L.E. On the relationship of liver glucose-6-phosphatase to the proliferation of endoplasmic reticulum in phenobarbital induction. J. Cell Biol. 31:243 (1966).PubMedCrossRefGoogle Scholar
  24. 24.
    Porter, K.R., Clause, A., and Fullam, E.F. A study tissue of culture cells by electron microscopy. J. Exp. Med. 81:233 (1945).PubMedCrossRefGoogle Scholar
  25. 25.
    Porter, K.R., and Thompson, H.P. A particulate body associated with epithelial cells cultured from mammary carcinomas of mice of a milk-factor strain. J. Exp. Med. 88:15 (1948).PubMedCrossRefGoogle Scholar
  26. 26.
    Porter, K.R. Observations on a submicroscopic basophilic component of cytoplasm. J. Exp. Med. 27:727 (1953).CrossRefGoogle Scholar
  27. 27.
    Posalaki, Z., and Barka, T. Alterations of hepatic endoplasmic reticulum in porphyric rats. J. Histochem. Cytochem. 16:337 (1968).PubMedCrossRefGoogle Scholar
  28. 28.
    Schimke, R.T., Ganschow, R., Doyle, D., and Arias, I.M. Regulation of protein turnover in mammalian tissues. Fed. Proceed. 27: 1223 (1968).Google Scholar
  29. 29.
    Shuster, L., and Jick, H. The turnover of microsomal protein in the livers of phenobarbital-treated mice. J. Biol. Chem. 241:5361 (1966).Google Scholar

Copyright information

© Plenum Press, New York 1969

Authors and Affiliations

  • A. L. Jones
    • 1
    • 2
  • J. B. Emans
    • 1
    • 2
  1. 1.Departments of Medicine and AnatomyUniversity of CaliforniaSan FranciscoUSA
  2. 2.Department of AnatomyHarvard Medical SchoolBostonUSA

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