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. 1973 Dec;70(12 Pt 1-2):3674–3678. doi: 10.1073/pnas.70.12.3674

Changes in Rabbit-Liver Lysosomes and Fructose 1,6-Bisphosphatase Induced by Cold and Fasting

S Pontremoli 1,2, E Melloni 1,2, F Salamino 1,2, A T Franzi 1,2,*, A De Flora 1,2, B L Horecker 1,2
PMCID: PMC427304  PMID: 4357886

Abstract

Exposure of rabbits to cold or fasting results in marked increases in the number and size of liver lysosomes, associated with increases in the total and “free” proteolytic activity. Changes in lysosomal morphology also indicate increased activity and fragility. These effects of cold and fasting are correlated with decreases in the levels of liver fructose bisphosphatase (EC 3.1.3.11) activity and changes in the molecular properties of the purified enzyme, including the loss of a small peptide containing the only tryptophan residue in the peptide chain.

Keywords: gluconeogenesis, environmental effects, subunit modification, lysosomes, proteolysis

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Selected References

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

  1. Arstila A. U., Trump B. F. Studies on cellular autophagocytosis. The formation of autophagic vacuoles in the liver after glucagon administration. Am J Pathol. 1968 Nov;53(5):687–733. [PMC free article] [PubMed] [Google Scholar]
  2. Deter R. L., De Duve C. Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes. J Cell Biol. 1967 May;33(2):437–449. doi: 10.1083/jcb.33.2.437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  4. Pontremoli S., Melloni E., Balestrero F., Franzi A. T., De Flora A., Horecker B. L. Fructose 1,6-bisphosphatase: the role of lysosomal enzymes in the modification of catalytic and structural properties. Proc Natl Acad Sci U S A. 1973 Feb;70(2):303–305. doi: 10.1073/pnas.70.2.303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Pontremoli S., Melloni E., De Flora A., Horecker B. L. Conversion of neutral to alkaline liver fructose 1,6-bisphosphatase: changes in molecular properties of the enzyme. Proc Natl Acad Sci U S A. 1973 Mar;70(3):661–664. doi: 10.1073/pnas.70.3.661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Rosa F. Ultrastructural changes produced by glucagon, cyclic 3'5'-AMP and epinephrine on perfused rat livers. J Ultrastruct Res. 1971 Feb;34(3):205–213. doi: 10.1016/s0022-5320(71)80068-0. [DOI] [PubMed] [Google Scholar]
  7. SABATINI D. D., BENSCH K., BARRNETT R. J. Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J Cell Biol. 1963 Apr;17:19–58. doi: 10.1083/jcb.17.1.19. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Traniello S., Melloni E., Pontremoli S., Sia C. L., Horecker R. L. Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin. Arch Biochem Biophys. 1972 Mar;149(1):222–231. doi: 10.1016/0003-9861(72)90317-7. [DOI] [PubMed] [Google Scholar]

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