Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Aug;78(8):4970–4974. doi: 10.1073/pnas.78.8.4970

Immunocytochemical localization of albumin in the secretory apparatus of rat liver parenchymal cells.

S Yokota, H D Fahimi
PMCID: PMC320312  PMID: 7029527

Abstract

The localization of albumin was investigated in rat liver, fixed by perfusion, with peroxidase-labeled monospecific antibodies against rat serum albumin purified by affinity chromatography. By light microscopy, albumin is present uniformly in all parenchymal cells with no difference in the intensity of reaction in the different parts of hepatic lobules. By electron microscopy, albumin is localized in the entire secretory apparatus including the rough and smooth endoplasmic reticulum, Golgi complex, and secretory vacuoles. In the rough endoplasmic reticulum, focal negative segments are interposed between positive regions. In the Golgi region, albumin is found both in stacked cisternae and at the trans aspect in the portion called GERL (Golgi-endoplasmic reticulum--lysosome). Whereas albumin and lipoprotein particles are separated in terminal dilatations of the endoplasmic reticulum and in the cisternae on the cis face of the Golgi apparatus, they are usually intermixed in vacuoles of the trans face. Similarly, most secretion vacuoles below the sinusoidal lining contain albumin and lipoprotein particles together, although a few are also found with only one secretory product. These observations suggest that, after synthesis in the rough endoplasmic reticulum, albumin is segregated into smooth transitional elements and transported to the Golgi region where it is packaged together with other secretory products such as lipoproteins. These secretion vacuoles move up the sinusoidal surface, where they are discharged. The possible involvement of GERL in the proteolytic cleavage of proalbumin to albumin is considered.

Full text

PDF
4970

Images in this article

4971Image
on p.4971
4972Image
on p.4972
4973Image
on p.4973
4974Image
on p.4974

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. Avrameas S., Ternynck T. Peroxidase labelled antibody and Fab conjugates with enhanced intracellular penetration. Immunochemistry. 1971 Dec;8(12):1175–1179. doi: 10.1016/0019-2791(71)90395-8. [DOI] [PubMed] [Google Scholar]
  3. Bergeron J. J., Borts D., Cruz J. Passage of serum-destined proteins through the Golgi apparatus of rat liver. An examination of heavy and light Golgi fractions. J Cell Biol. 1978 Jan;76(1):87–97. doi: 10.1083/jcb.76.1.87. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chan L., Bradley W. A., Means A. R. Amino acid sequence of the signal peptide of apoVLDL-II, a major apoprotein in avian very low density lipoproteins. J Biol Chem. 1980 Nov 10;255(21):10060–10063. [PubMed] [Google Scholar]
  5. Feldhoff R. C., Taylor J. M., Jefferson L. S. Synthesis and secretion of rat albumin in vivo, in perfused liver, and in isolated hepatocytes. Effects of hypophysectomy and growth hormone treatment. J Biol Chem. 1977 Jun 10;252(11):3611–3616. [PubMed] [Google Scholar]
  6. Geuze J. J., Slot J. W., Tokuyasu K. T. Immunocytochemical localization of amylase and chymotrypsinogen in the exocrine pancreatic cell with special attention to the Golgi complex. J Cell Biol. 1979 Sep;82(3):697–707. doi: 10.1083/jcb.82.3.697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Graham R. C., Jr, Karnovsky M. J. The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J Histochem Cytochem. 1966 Apr;14(4):291–302. doi: 10.1177/14.4.291. [DOI] [PubMed] [Google Scholar]
  8. HAMASHIMA Y., HARTER J. G., COONS A. H. THE LOCALIZATION OF ALBUMIN AND FIBRINOGEN IN HUMAN LIVER CELLS. J Cell Biol. 1964 Feb;20:271–279. doi: 10.1083/jcb.20.2.271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Horikawa M., Chisaka N., Yokoyama S., Onoé T. Effect of stirring during fixation upon immunofluorescence. Results with distribution of albumin-producing cells in liver. J Histochem Cytochem. 1976 Aug;24(8):926–932. doi: 10.1177/24.8.60440. [DOI] [PubMed] [Google Scholar]
  10. Kraehenbuhl J. P., Jamieson J. D. Localization of intracellular antigens by immunoelectron microscopy. Int Rev Exp Pathol. 1974;13(0):1–53. [PubMed] [Google Scholar]
  11. Kraehenbuhl J. P., Racine L., Jamieson J. D. Immunocytochemical localization of secretory proteins in bovine pancreatic exocrine cells. J Cell Biol. 1977 Feb;72(2):406–423. doi: 10.1083/jcb.72.2.406. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LeBouton A. V., Masse J. P. A random arrangement of albumin-containing hepatocytes seen with histo-immunologic methods. I. Verification of the artifact. Anat Rec. 1980 Jun;197(2):183–194. doi: 10.1002/ar.1091970207. [DOI] [PubMed] [Google Scholar]
  13. Lin C., Chang J. Electron microscopy of albumin synthesis. Science. 1975 Oct 31;190(4213):465–467. doi: 10.1126/science.170682. [DOI] [PubMed] [Google Scholar]
  14. Novikoff A. B. DAB cytochemistry: artifact problems in its current uses. J Histochem Cytochem. 1980 Sep;28(9):1036–1038. doi: 10.1177/28.9.7410815. [DOI] [PubMed] [Google Scholar]
  15. Novikoff A. B., Novikoff P. M. Cytochemical contributions to differentiating GERL from the Golgi apparatus. Histochem J. 1977 Sep;9(5):525–551. doi: 10.1007/BF01002901. [DOI] [PubMed] [Google Scholar]
  16. Novikoff A. B., Novikoff P. M., Stockert R. J., Becker F. F., Yam A., Poruchynsky M. S., Levin W., Thomas P. E. Immunocytochemical localization of epoxide hydrase in hyperplastic nodules induced in rat liver by 2-acetylaminofluorene. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5207–5211. doi: 10.1073/pnas.76.10.5207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Novikoff P. M., Yam A. Sites of lipoprotein particles in normal rat hepatocytes. J Cell Biol. 1978 Jan;76(1):1–11. doi: 10.1083/jcb.76.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Oh Y. H., Sanders B. E. Improved chromatographic fractionation and characterization of human plasma proteins. Anal Biochem. 1966 May;15(2):232–244. doi: 10.1016/0003-2697(66)90027-3. [DOI] [PubMed] [Google Scholar]
  20. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
  22. Quinn P. S., Judah J. D. Calcium-dependent Golgi-vesicle fusion and cathepsin B in the conversion of proalbumin into albumin in rat liver. Biochem J. 1978 May 15;172(2):301–309. doi: 10.1042/bj1720301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Redman C. M., Banerjee D., Manning C., Huang C. Y., Green K. In vivo effect of colchicine on hepatic protein synthesis and on the conversion of proalbumin to serum albumin. J Cell Biol. 1978 May;77(2):400–416. doi: 10.1083/jcb.77.2.400. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Redman C. M., Cherian M. G. The secretory pathways of rat serum glycoproteins and albumin. Localization of newly formed proteins within the endoplasmic reticulum. J Cell Biol. 1972 Feb;52(2):231–245. doi: 10.1083/jcb.52.2.231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Vlasuk G. P., Ghrayeb J., Walz F. G., Jr Proalbumin is bound to the membrane of rat liver smooth microsomes. Biochem Biophys Res Commun. 1980 May 14;94(1):366–372. doi: 10.1016/s0006-291x(80)80230-0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES