Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1972 Feb 1;52(2):478–487. doi: 10.1083/jcb.52.2.478

SECRETION OF ACID HYDROLASES AND ITS INTRACELLULAR SOURCE IN TETRAHYMENA PYRIFORMIS

Miklós Müller 1
PMCID: PMC2108638  PMID: 4333453

Abstract

Axenic Tetrahymena pyriformis, syngen 1, mating type II cells were grown in Cox's defined medium. When washed and transferred into nonnutrient dilute salt solution or resuspended in the defined medium, the intact cells secrete acid hydrolases into the medium. Cells starving in the salt solution release in 5 hr about two-thirds of their β-glucosidase, β-N-acetylglucosaminidase, α-glucosidase, and amylase activities, about one-third of their deoxyribonuclease and phosphatase activities, smaller amounts of ribonuclease, and only a negligible fraction of their proteinase activity and protein content. During this period there is practically no change in the enzyme activities (except for a sudden increase of ribonuclease activity) and protein content of cells and medium together. Cells resuspended in the nutrient medium secrete enzymes as do the starved cells, but replace this loss, so that there is a continuous increase of the activities in the total system. According to isopycnic centrifugation experiments performed in sucrose gradients, the source of the hydrolases is a special population of lysosomes which disappear from the cells during starvation. This population equilibrates in the high density region of the gradients and contains the various acid hydrolases in about the proportion in which these enzymes appear in the medium.

Full Text

The Full Text of this article is available as a PDF (537.7 KB).

Selected References

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

  1. BEAUFAY H., BENDALL D. S., BAUDHUIN P., DE DUVE C. Tissue fractionation studies. 12. Intracellular distribution of some dehydrogenases, alkaline deoxyribonuclease and iron in rat-liver tissue. Biochem J. 1959 Dec;73:623–628. doi: 10.1042/bj0730623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BEAUFAY H., BENDALL D. S., BAUDHUN P., WATTIAUX R., DE DUVE C. Tissue fractionation studies. 13. Analysis of mitochondrial fractions from rat liver by density-gradient centrifuging. Biochem J. 1959 Dec;73:628–637. doi: 10.1042/bj0730628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cox D., Frank O., Hutner S. H., Baker H. Growth of Tetrahymena in carbohydate-free high-glutamate media. J Protozool. 1968 Nov;15(4):713–716. doi: 10.1111/j.1550-7408.1968.tb02199.x. [DOI] [PubMed] [Google Scholar]
  4. DICKIE N., LIENER I. E. A study of the proteolytic system of Tetrahymena pyriformis W. I. Purification and partial characterization of the constituent proteinases. Biochim Biophys Acta. 1962 Oct 8;64:41–51. doi: 10.1016/0006-3002(62)90758-8. [DOI] [PubMed] [Google Scholar]
  5. DICKIE N., LIENER I. E. A study of the proteolytic system of tetrahymena pyriformis W. II. Substrate specificity of constituent proteinases. Biochim Biophys Acta. 1962 Oct 8;64:52–59. doi: 10.1016/0006-3002(62)90759-x. [DOI] [PubMed] [Google Scholar]
  6. HAESSLER H. A., CUNNINGHAM L. A comparison of several deoxyribonucleases of type II. Exp Cell Res. 1957 Oct;13(2):304–311. doi: 10.1016/0014-4827(57)90009-5. [DOI] [PubMed] [Google Scholar]
  7. HOGG J. F., KORNBERG H. L. The metabolism of C2-compounds in micro-organisms. 9. Role of the glyoxylate cycle in protozoal glyconeogenesis. Biochem J. 1963 Mar;86:462–468. doi: 10.1042/bj0860462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Leighton F., Poole B., Beaufay H., Baudhuin P., Coffey J. W., Fowler S., De Duve C. The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with triton WR-1339. Improved isolation procedures, automated analysis, biochemical and morphological properties of fractions. J Cell Biol. 1968 May;37(2):482–513. doi: 10.1083/jcb.37.2.482. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Levy M. R., Elliott A. M. Biochemical and ultrastructural changes in Tetrahymena pyriformis during starvation. J Protozool. 1968 Feb;15(1):208–222. doi: 10.1111/j.1550-7408.1968.tb02113.x. [DOI] [PubMed] [Google Scholar]
  10. Lloyd D., Brightwell R., Venables S. E., Roach G. I., Turner G. Subcellular fractionation of Tetrahymena pyriformis ST by zonal centrifugation: changes in activities and distribution of enzymes during the growth cycle and on starvation. J Gen Microbiol. 1971 Feb;65(2):209–223. doi: 10.1099/00221287-65-2-209. [DOI] [PubMed] [Google Scholar]
  11. Müller M., Baudhuin P., De Duve C. Lysosomes in Tetrahymena pyriformis. I. Some properties and lysosomal localization of acid hydrolases. J Cell Physiol. 1966 Oct;68(2):165–175. doi: 10.1002/jcp.1040680211. [DOI] [PubMed] [Google Scholar]
  12. Müller M., Hogg J. F., De Duve C. Distribution of tricarboxylic acid cycle enzymes and glyoxylate cycle enzymes between mitochondria and peroxisomes in Tetrahymena pyriformis. J Biol Chem. 1968 Oct 25;243(20):5385–5395. [PubMed] [Google Scholar]
  13. Müller M. Lysosomes in Tetrahymena pyriformis. II. Intracellular distribution of several acid hydrolases. Acta Biol Acad Sci Hung. 1971;22(2):179–186. [PubMed] [Google Scholar]
  14. PRESCOTT D. M. Mass and clone culturing of Amoeba proteus and Chaos chaos. C R Trav Lab Carlsberg Chim. 1956;30(1):1–12. [PubMed] [Google Scholar]

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

RESOURCES