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. 1970 Jul;118(3):401–404. doi: 10.1042/bj1180401

Plasma protein catabolism by the perfused rat liver. The effect of alteration of albumin concentration and dietary protein depletion

R Hoffenberg 1, A H Gordon 1, E G Black 1, L N Louis 1
PMCID: PMC1179205  PMID: 5472166

Abstract

1. The isolated perfused rat liver was used to study degradation rates of plasma albumin, transferrin and fibrinogen. 2. Constant fractional rates were observed for all three proteins even when the albumin concentration was drastically increased by the addition of large amounts to the perfusate pool. 3. Livers taken from rats deprived of dietary protein for 14–18 days showed greatly diminished fractional catabolic rates for albumin when perfused with blood from similarly deprived animals. 4. These rates could be restored to near-normal values by adding albumin or by perfusing with blood from normally fed rats. 5. These findings are consistent with the theory of pinocytosis as a step in the degradation of plasma proteins by hepatic parenchymal cells.

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Selected References

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

  1. Bertini F., Mego J. L., McQueen J. D. Distribution in tissue homogenates, and the nature of the linkage of injected proteins to subcellular particles. J Cell Physiol. 1967 Aug;70(1):105–114. doi: 10.1002/jcp.1040700114. [DOI] [PubMed] [Google Scholar]
  2. Bocci V., Masti L., Pacini A., Viti A. Catabolism of native and denatured serum 131-I-proteins by polymorphonuclear leucocytes. Exp Cell Res. 1968 Sep;52(1):129–139. doi: 10.1016/0014-4827(68)90552-1. [DOI] [PubMed] [Google Scholar]
  3. Brownstone A. D. A versatile system for preparative electrophoresis in acrylamide gel. Anal Biochem. 1969 Jan;27(1):25–46. doi: 10.1016/0003-2697(69)90216-4. [DOI] [PubMed] [Google Scholar]
  4. COHEN S., GORDON A. H. Catabolism of plasma albumin by the perfused rat liver. Biochem J. 1958 Dec;70(4):544–551. doi: 10.1042/bj0700544. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Coffey J. W., De Duve C. Digestive activity of lysosomes. I. The digestion of proteins by extracts of rat liver lysosomes. J Biol Chem. 1968 Jun 25;243(12):3255–3263. [PubMed] [Google Scholar]
  6. Dunnigan M. G., Fyfe T., McKiddie M. T., Crosbie S. M. The effects of isocaloric exchange of dietary starch and sucrose on glucose tolerance, plasma insulin and serum lipids in man. Clin Sci. 1970 Jan;38(1):1–9. doi: 10.1042/cs0380001. [DOI] [PubMed] [Google Scholar]
  7. FREEMAN T., GORDON A. H., HUMPHREY J. H. Distinction between catabolism of native and denatured proteins by the isolated perfused liver after carbon loading. Br J Exp Pathol. 1958 Oct;39(5):459–471. [PMC free article] [PubMed] [Google Scholar]
  8. FREEMAN T., GORDON A. H. METABOLISM OF ALBUMIN AND GAMMA-GLOBULIN IN PROTEIN DEFICIENT RATS. Clin Sci. 1964 Feb;26:17–26. [PubMed] [Google Scholar]
  9. FRIEDBERG W. Relation between pool size and catabolism of albumin in the mouse. Am J Physiol. 1963 Mar;204:501–504. doi: 10.1152/ajplegacy.1963.204.3.501. [DOI] [PubMed] [Google Scholar]
  10. Fernandez A., Sobel C., Goldenberg H. An improved method for determination of serum albumin and globulin. Clin Chem. 1966 Apr;12(4):194–205. [PubMed] [Google Scholar]
  11. GORDON A. H., LOUIS L. N. PREPARATION AND PROPERTIES OF RAT TRANSFERRIN. Biochem J. 1963 Sep;88:409–414. doi: 10.1042/bj0880409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. GORDON A. H. The catabolic rate of albumin doubly labelled with 131-I and 14-C in the isolated perfused rat liver. Biochem J. 1962 Mar;82:531–540. doi: 10.1042/bj0820531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hoffenberg R., Black E., Brock J. F. Albumin and gamma-globulin tracer studies in protein depletion states. J Clin Invest. 1966 Jan;45(1):143–152. doi: 10.1172/JCI105319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MATTHEWS C. M. Effects of plasmapheresis on albumin pools in rabbits. J Clin Invest. 1961 Mar;40:603–610. doi: 10.1172/JCI104290. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. MCFARLANE A. S. Labelling of plasma proteins with radioactive iodine. Biochem J. 1956 Jan;62(1):135–143. doi: 10.1042/bj0620135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MEGO J. L., MCQUEEN J. D. THE UPTAKE AND DEGRADATION OF INJECTED LABELED PROTEINS BY MOUSE-LIVER PARTICLES. Biochim Biophys Acta. 1965 Apr 12;100:136–143. doi: 10.1016/0304-4165(65)90436-8. [DOI] [PubMed] [Google Scholar]
  17. McFARLANE A. S. Efficient trace-labelling of proteins with iodine. Nature. 1958 Jul 5;182(4627):53–53. doi: 10.1038/182053a0. [DOI] [PubMed] [Google Scholar]
  18. Mego J. L., Bertini F., McQueen J. D. The use of formaldehyde-treated 131-I-albumin in the study of digestive vacuoles and some properties of these particles from mouse liver. J Cell Biol. 1967 Mar;32(3):699–707. doi: 10.1083/jcb.32.3.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. ROTHSCHILD M. A., ORATZ M., EVANS C., SCHREIBER S. S. ALTERATIONS IN ALBUMIN METABOLISM AFTER SERUM AND ALBUMIN INFUSIONS. J Clin Invest. 1964 Oct;43:1874–1880. doi: 10.1172/JCI105061. [DOI] [PMC free article] [PubMed] [Google Scholar]

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