Skip to main content
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
. 1971 Nov;68(11):2674–2677. doi: 10.1073/pnas.68.11.2674

Hormonal Control of Lecithin Synthesis in Barley Aleurone Cells: Regulation of the CDP-Choline Pathway by Gibberellin

Kenneth D Johnson 1,*, Hans Kende 1
PMCID: PMC389498  PMID: 16591952

Abstract

The enzymes of the cytidine diphosphate-choline pathway, which is involved in lecithin biosynthesis, are present in imbibed barley aleurone cells. The first enzyme, choline kinase (EC 2.7.1.32), is found in the soluble protein fraction. Its activity is not affected by prior treatment of aleurone layers with gibberellin. The second and third enzymes of the pathway, phosphorylcholine-cytidyl (EC 2.7.7.15) and phosphorylcholine-glyceride (EC 2.7.8.2) transferases, are associated with the particulate fractions. Their activities are greatly increased by gibberellin treatment during the lag phase (0-8 hr) of gibberellin-effected α-amylase synthesis. The hormonal effects are evident two hours after gibberellin treatment. Inhibitors that block gibberellin-effected α-amylase formation also inhibit the stimulation of these membrane-bound enzymes by the hormone.

Keywords: membrane synthesis, rough endoplasmic reticulum, enzyme induction, abscisic acid, actinomycin D

Full text

PDF
2674

Selected References

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

  1. BORKENHAGEN L. F., KENNEDY E. P. The enzymatic synthesis of cytidine diphosphate choline. J Biol Chem. 1957 Aug;227(2):951–962. [PubMed] [Google Scholar]
  2. Chrispeels M. J., Varner J. E. Gibberellic Acid-enhanced synthesis and release of alpha-amylase and ribonuclease by isolated barley and aleurone layers. Plant Physiol. 1967 Mar;42(3):398–406. doi: 10.1104/pp.42.3.398. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chrispeels M. J., Varner J. E. Hormonal control of enzyme synthesis: on the mode of action of gibberellic Acid and abscisin in aleurone layers of barley. Plant Physiol. 1967 Jul;42(7):1008–1016. doi: 10.1104/pp.42.7.1008. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Evins W. H., Varner J. E. Hormone-controlled synthesis of endoplasmic reticulum in barley aleurone cells. Proc Natl Acad Sci U S A. 1971 Jul;68(7):1631–1633. doi: 10.1073/pnas.68.7.1631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Filner P., Varner J. E. A test for de novo synthesis of enzymes: density labeling with H2O18 of barley alpha-amylase induced by gibberellic acid. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1520–1526. doi: 10.1073/pnas.58.4.1520. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ganoza M. C., Williams C. A. In vitro synthesis of different categories of specific protein by membrane-bound and free ribosomes. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1370–1376. doi: 10.1073/pnas.63.4.1370. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hokin L. E. Dynamic aspects of phospholipids during protein secretion. Int Rev Cytol. 1968;23:187–208. doi: 10.1016/s0074-7696(08)60272-7. [DOI] [PubMed] [Google Scholar]
  8. Jacobsen J. V., Varner J. E. Gibberellic Acid-induced synthesis of protease by isolated aleurone layers of barley. Plant Physiol. 1967 Nov;42(11):1596–1600. doi: 10.1104/pp.42.11.1596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Mills E. S., Topper Y. J. Some ultrastructural effects of insulin, hydrocortisone, and prolactin on mammary gland explants. J Cell Biol. 1970 Feb;44(2):310–328. doi: 10.1083/jcb.44.2.310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Morré D. J., Nyquist S., Rivera E. Lecithin Biosynthetic Enzymes of Onion Stem and the Distribution of Phosphorylcholine-Cytidyl Transferase among Cell Fractions. Plant Physiol. 1970 Jun;45(6):800–804. doi: 10.1104/pp.45.6.800. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Redman C. M. The synthesis of serum proteins on attached rather than free ribosomes of rat liver. Biochem Biophys Res Commun. 1968 Jun 28;31(6):845–850. doi: 10.1016/0006-291x(68)90528-7. [DOI] [PubMed] [Google Scholar]
  13. SIEKEVITZ P., PALADE G. E. A cytochemical study on the pancreas of the guinea pig. 5. In vivo incorporation of leucine-1-C14 into the chymotrypsinogen of various cell fractions. J Biophys Biochem Cytol. 1960 Jul;7:619–630. doi: 10.1083/jcb.7.4.619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Siekevitz P., Palade G. E. Distribution of newly synthesized amylase in microsomal subfractions of guinea pigs pancreas. J Cell Biol. 1966 Sep;30(3):519–530. doi: 10.1083/jcb.30.3.519. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Tanaka K., Tolbert N. E., Gohlke A. F. Choline kinase and phosphorylcholine phosphatase in plants. Plant Physiol. 1966 Feb;41(2):307–312. doi: 10.1104/pp.41.2.307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Tata J. R. Hormonal regulation of growth and protein synthesis. Nature. 1968 Jul 27;219(5152):331–337. doi: 10.1038/219331a0. [DOI] [PubMed] [Google Scholar]
  17. Tomkins G. M., Gelehrter T. D., Granner D., Martin D., Jr, Samuels H. H., Thompson E. B. Control of specific gene expression in higher organisms. Expression of mammalian genes may be controlled by repressors acting on the translation of messenger RNA. Science. 1969 Dec 19;166(3912):1474–1480. doi: 10.1126/science.166.3912.1474. [DOI] [PubMed] [Google Scholar]
  18. Varner J. E., Chandra G. R. HORMONAL CONTROL OF ENZYME SYNTHESIS IN BARLEY ENDOSPERM. Proc Natl Acad Sci U S A. 1964 Jul;52(1):100–106. doi: 10.1073/pnas.52.1.100. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. WEISS S. B., SMITH S. W., KENNEDY E. P. The enzymatic formation of lecithin from cytidine diphosphate choline and D-1,2-diglyceride. J Biol Chem. 1958 Mar;231(1):53–64. [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