Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1978 Jan 1;76(1):1–11. doi: 10.1083/jcb.76.1.1

Sites of lipoprotein particles in normal rat hepatocytes

PMCID: PMC2109971  PMID: 201645

Abstract

Very low density lipoprotein (VLDL) particles are packaged by the Golgi apparatus into vacuoles which move to the plasma membrane and empty the particles into the space of Disse, via exocytosis. Traditionally, all lipoprotein-containing cisternae and vacuoles are thought to be parts of this pathway. Observations reported here demonstrate that there is a second population of lipoprotein-containing cisternae and vacuoles. This population is part of GERL, an organelle we consider to be a specialized hydrolase-rich region of the endoplasmic reticulum (ER). To our knowledge, this is the first systematic study of GERL in normal rat hepatocytes.

Full Text

The Full Text of this article is available as a PDF (3.5 MB).

Selected References

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

  1. Alexander C. A., Hamilton R. L., Havel R. J. Subcellular localization of B apoprotein of plasma lipoproteins in rat liver. J Cell Biol. 1976 May;69(2):241–263. doi: 10.1083/jcb.69.2.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bentfeld M. E., Bainton D. F. Cytochemical localization of lysosomal enzymes in rat megakaryocytes and platelets. J Clin Invest. 1975 Dec;56(6):1635–1649. doi: 10.1172/JCI108246. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chapman M. J., Mills G. L., Taylaur C. E. Lipoprotein particles from the Golgi apparatus of guinea-pig liver. Biochem J. 1972 Jul;128(4):779–787. doi: 10.1042/bj1280779. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cheetham R. D., Morré D. J., Pannek C., Friend D. S. Isolation of a Golgi apparatus-rich fraction from rat liver. IV. Thiamine pyrophosphatase. J Cell Biol. 1971 Jun;49(3):899–905. doi: 10.1083/jcb.49.3.899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Claude A. Growth and differentiation of cytoplasmic membranes in the course of lipoprotein granule synthesis in the hepatic cell. I. Elaboration of elements of the Golgi complex. J Cell Biol. 1970 Dec;47(3):745–766. doi: 10.1083/jcb.47.3.745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Debeer L. J., Thomas J., Mannaerts G., DeSchepper P. J. Effect of sulfonylureas on triglyceride metabolism in the rat liver: possible role of the lysosomes in hepatic lipolysis. J Clin Invest. 1977 Feb;59(2):185–192. doi: 10.1172/JCI108628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Decker R. S. Lysosomal packaging in differentiating and degenerating anuran lateral motor column neurons. J Cell Biol. 1974 Jun;61(3):599–612. doi: 10.1083/jcb.61.3.599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ehrenreich J. H., Bergeron J. J., Siekevitz P., Palade G. E. Golgi fractions prepared from rat liver homogenates. I. Isolation procedure and morphological characterization. J Cell Biol. 1973 Oct;59(1):45–72. doi: 10.1083/jcb.59.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Eisenberg S., Levy R. I. Lipoprotein metabolism. Adv Lipid Res. 1975;13:1–89. [PubMed] [Google Scholar]
  10. Farquhar M. G., Bergeron J. J., Palade G. E. Cytochemistry of Golgi fractions prepared from rat liver. J Cell Biol. 1974 Jan;60(1):8–25. doi: 10.1083/jcb.60.1.8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Goldfischer S., Essner E., Schiller B. Nucleoside diphosphatase and thiamine pyrophosphatase activities in the endoplasmic reticulum and golgi apparatus. J Histochem Cytochem. 1971 Jun;19(6):349–360. doi: 10.1177/19.6.349. [DOI] [PubMed] [Google Scholar]
  12. Gonatas N. K., Kim S. U., Stieber A., Avrameas S. Internalization of lectins in neuronal GERL. J Cell Biol. 1977 Apr;73(1):1–13. doi: 10.1083/jcb.73.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hamilton R. L., Regen D. M., Gray M. E., LeQuire V. S. Lipid transport in liver. I. Electron microscopic identification of very low density lipoproteins in perfused rat liver. Lab Invest. 1967 Feb;16(2):305–319. [PubMed] [Google Scholar]
  14. Hand A. R., Oliver C. Cytochemical studies of GERL and its role in secretory granule formation in exocrine cells. Histochem J. 1977 Jul;9(4):375–392. doi: 10.1007/BF01002972. [DOI] [PubMed] [Google Scholar]
  15. Hand A. R., Oliver C. Relationship between the Golgi apparatus, GERL, and secretory granules in acinar cells of the rat exorbital lacrimal gland. J Cell Biol. 1977 Aug;74(2):399–413. doi: 10.1083/jcb.74.2.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Jackson R. L., Morrisett J. D., Gotto A. M., Jr Lipoprotein structure and metabolism. Physiol Rev. 1976 Apr;56(2):259–316. doi: 10.1152/physrev.1976.56.2.259. [DOI] [PubMed] [Google Scholar]
  17. Jones A. L., Ruderman N. B., Herrera M. G. Electron microscopic and biochemical study of lipoprotein synthesis in the isolated perfused rat liver. J Lipid Res. 1967 Sep;8(5):429–446. [PubMed] [Google Scholar]
  18. Ma M. H., Biempica L. The normal human liver cell. Cytochemical and ultrastructural studies. Am J Pathol. 1971 Mar;62(3):353–390. [PMC free article] [PubMed] [Google Scholar]
  19. Miller F., Herzog V. Die Lokalisation von Peroxydase und saurer Phosphatase in eosinophilen Leukocyten während der Reifung. Elek. Elektronenmikroskopisch-cytochemische Untersuchungen am Knochenmark von Ratte und Kaninchen. Z Zellforsch Mikrosk Anat. 1969;97(1):84–110. [PubMed] [Google Scholar]
  20. NOVIKOFF A. B., GOLDFISCHER S. Nucleosidediphosphatase activity in the Golgi apparatus and its usefulness for cytological studies. Proc Natl Acad Sci U S A. 1961 Jun 15;47:802–810. doi: 10.1073/pnas.47.6.802. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nakai T., Otto P. S., Kennedy D. L., Whayne T. F., Jr Rat high density lipoprotein subfraction (HDL3) uptake and catabolism by isolated rat liver parenchymal cells. J Biol Chem. 1976 Aug 25;251(16):4914–4921. [PubMed] [Google Scholar]
  22. Novikoff A. B., Mori M., Quintana N., Yam A. Studies of the secretory process in the mammalian exocrine pancreas. I. The condensing vacuoles. J Cell Biol. 1977 Oct;75(1):148–165. doi: 10.1083/jcb.75.1.148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Novikoff A. B. The endoplasmic reticulum: a cytochemist's view (a review). Proc Natl Acad Sci U S A. 1976 Aug;73(8):2781–2787. doi: 10.1073/pnas.73.8.2781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Novikoff A. B., Yam A., Novikoff P. M. Cytochemical study of secretory process in transplantable insulinoma of syrian golden hamster. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4501–4505. doi: 10.1073/pnas.72.11.4501. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Novikoff P. M., Novikoff A. B., Quintana N., Hauw J. J. Golgi apparatus, GERL, and lysosomes of neurons in rat dorsal root ganglia, studied by thick section and thin section cytochemistry. J Cell Biol. 1971 Sep;50(3):859–886. doi: 10.1083/jcb.50.3.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Novikoff P. M., Roheim P. S., Novikoff A. B., Edelstein D. Production and prevention of fatty liver in rats fed clofibrate and orotic acid diets containing sucrose. Lab Invest. 1974 Jun;30(6):732–750. [PubMed] [Google Scholar]
  27. Palade G. E., Bruns R. R. Structural modulations of plasmalemmal vesicles. J Cell Biol. 1968 Jun;37(3):633–649. doi: 10.1083/jcb.37.3.633. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES