Abstract:

Excision and dark incubation of oat (Avena sativa L., var. Victory) leaves cause a sharp increase in protease activity, which precedes Chl loss. Both these senescence processes are inhibited by exogenously applied 1,3-diaminopropane (Dap), which occurs naturally in leaf segments. The inhibition of protease activity is much greater in vivo than in vitro, suggesting inhibition of protease synthesis as well as protease action by Dap. Chl breakdown in leaves of radish and broccoli, which also senesce rapidly in the dark, is only slightly inhibited by DaP. These differences between cereal and dicotyledonous plants are correlated with the natural occurrence of Dap in cereals. In the light, Dap promotes, rather than retards, the loss of Chl in oat leaves. This resembles previously described effects of other polyamines. Addition of Mg(2+) to the medium does not antagonize this effect. In the dark, the accumulated Dap also inhibits ethylene production and decreases titer of other polyamines. Addition of Ca(2+) to the incubation medium containing Dap competitively reduces the effects of Dap. Thus, Dap, like other polyamines, seems to require an initial attachment to a membrane site shared with Ca(2+) before exerting its antisenescence action.

Open in

PUBMED | PMC | Google Scholar | Wikipedia

Relations:

Content

Citations

(7)

References

(19)

Drugs

(2)

Affiliates

(1)

Effects of Exogenous 1,3-Diaminopropane and Spermidine on Senescence of Oat Leaves <sup><a href="#fn1" rid="fn1" class=" fn">1</a></sup>

Abstract

Excision and dark incubation of oat (Avena sativa L., var. Victory) leaves cause a sharp increase in protease activity, which precedes Chl loss. Both these senescence processes are inhibited by exogenously applied 1,3-diaminopropane (Dap), which occurs naturally in leaf segments. The inhibition of protease activity is much greater in vivo than in vitro, suggesting inhibition of protease synthesis as well as protease action by Dap. Chl breakdown in leaves of radish and broccoli, which also senesce rapidly in the dark, is only slightly inhibited by DaP. These differences between cereal and dicotyledonous plants are correlated with the natural occurrence of Dap in cereals. In the light, Dap promotes, rather than retards, the loss of Chl in oat leaves. This resembles previously described effects of other polyamines. Addition of Mg^{to the medium does not antagonize this effect. In the dark, the accumulated Dap also inhibits ethylene production and decreases titer of other polyamines. Addition of Ca}^{to the incubation medium containing Dap competitively reduces the effects of Dap. Thus, Dap, like other polyamines, seems to require an initial attachment to a membrane site shared with Ca}^{before exerting its antisenescence action.}

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (896K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

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

Altman A, Kaur-Sawhney R, Galston AW. Stabilization of Oat Leaf Protoplasts through Polyamine-mediated Inhibition of Senescence. Plant Physiol. 1977 Oct;60(4):570–574.[PMC free article] [PubMed] [Google Scholar]
Apelbaum A, Burgoon AC, Anderson JD, Lieberman M. Polyamines inhibit biosynthesis of ethylene in higher plant tissue and fruit protoplasts. Plant Physiol. 1981 Aug;68(2):453–456.[PMC free article] [PubMed] [Google Scholar]
Boller T, Kende H. Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 1979 Jun;63(6):1123–1132.[PMC free article] [PubMed] [Google Scholar]
Cohen AS, Popovic RB, Zalik S. Effects of Polyamines on Chlorophyll and Protein Content, Photochemical Activity, and Chloroplast Ultrastructure of Barley Leaf Discs during Senescence. Plant Physiol. 1979 Nov;64(5):717–720.[PMC free article] [PubMed] [Google Scholar]
Even-Chen Z, Mattoo AK, Goren R. Inhibition of ethylene biosynthesis by aminoethoxyvinylglycine and by polyamines shunts label from 3,4-[C]methionine into spermidine in aged orange peel discs. Plant Physiol. 1982 Feb;69(2):385–388.[PMC free article] [PubMed] [Google Scholar]
Flores HE, Galston AW. Analysis of polyamines in higher plants by high performance liquid chromatography. Plant Physiol. 1982 Mar;69(3):701–706.[PMC free article] [PubMed] [Google Scholar]
Fuhrer J, Kaur-Sawhney R, Shih LM, Galston AW. Effects of Exogenous 1,3-Diaminopropane and Spermidine on Senescence of Oat Leaves : II. Inhibition of Ethylene Biosynthesis and Possible Mode of Action. Plant Physiol. 1982 Dec;70(6):1597–1600.[PMC free article] [PubMed] [Google Scholar]
Gepstein S, Thimann KV. The role of ethylene in the senescence of oat leaves. Plant Physiol. 1981 Aug;68(2):349–354.[PMC free article] [PubMed] [Google Scholar]
Kaur-Sawhney R, Altman A, Galston AW. Dual Mechanisms in Polyamine-mediated Control of Ribonuclease Activity in Oat Leaf Protoplasts. Plant Physiol. 1978 Jul;62(1):158–160.[PMC free article] [PubMed] [Google Scholar]
Kaur-Sawhney R, Flores HE, Galston AW. Polyamine-induced DNA Synthesis and Mitosis in Oat Leaf Protoplasts. Plant Physiol. 1980 Feb;65(2):368–371.[PMC free article] [PubMed] [Google Scholar]
Kaur-Sawhney R, Flores HE, Galston AW. Polyamine oxidase in oat leaves: a cell wall-localized enzyme. Plant Physiol. 1981 Aug;68(2):494–498.[PMC free article] [PubMed] [Google Scholar]
Kaur-Sawhney R, Shih LM, Flores HE, Galston AW. Relation of polyamine synthesis and titer to aging and senescence in oat leaves. Plant Physiol. 1982 Feb;69(2):405–410.[PMC free article] [PubMed] [Google Scholar]
Kotaka S, Krueger AP. Some observations on the bleaching of ethylenediaminetetraacetic acid on green barley leaves. Plant Physiol. 1969 Jun;44(6):809–815.[PMC free article] [PubMed] [Google Scholar]
LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
Peterson LW, Huffaker RC. Loss of Ribulose 1,5-Diphosphate Carboxylase and Increase in Proteolytic Activity during Senescence of Detached Primary Barley Leaves. Plant Physiol. 1975 Jun;55(6):1009–1015.[PMC free article] [PubMed] [Google Scholar]
Pösö H, Jänne J. Inhibition of polyamine accumulation and deoxyribonucleic acid synthesis in regenerating rat liver. Biochem J. 1976 Aug 15;158(2):485–488.[PMC free article] [PubMed] [Google Scholar]
Ramakrishna S, Guarino L, Cohen SS. Polyamines of Anacystis nidulans and metabolism of exogenous spermidine and spermine. J Bacteriol. 1978 Jun;134(3):744–750.[PMC free article] [PubMed] [Google Scholar]
Tuomi K, Raina A, Mäntyjärvi R. 1,3-Diaminopropane rapidly inhibits protein synthesis and virus production in BKT-1 cells. FEBS Lett. 1980 Mar 10;111(2):329–332. [PubMed] [Google Scholar]
Yu YB, Adams DO, Yang SF. 1-Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene biosynthesis. Arch Biochem Biophys. 1979 Nov;198(1):280–286. [PubMed] [Google Scholar]

Department of Biology, Yale University, New Haven, Connecticut 06511

^{Present address: Calgene Inc., Davis, CA 95616.}

^{Present address: Institute of Plant Physiology, University of Bern, Altenbergrain 21, CH-3013 Bern, Switzerland.}

^{Supported by grant DAR 7813294 from the National Science Foundation and I-44-79 from the Binational Agricultural Research and Development (BARD) agency to A. W. G.}

Copyright notice

Abstract

Excision and dark incubation of oat (Avena sativa L., var. Victory) leaves cause a sharp increase in protease activity, which precedes Chl loss. Both these senescence processes are inhibited by exogenously applied 1,3-diaminopropane (Dap), which occurs naturally in leaf segments. The inhibition of protease activity is much greater in vivo than in vitro, suggesting inhibition of protease synthesis as well as protease action by Dap. Chl breakdown in leaves of radish and broccoli, which also senesce rapidly in the dark, is only slightly inhibited by DaP. These differences between cereal and dicotyledonous plants are correlated with the natural occurrence of Dap in cereals. In the light, Dap promotes, rather than retards, the loss of Chl in oat leaves. This resembles previously described effects of other polyamines. Addition of Mg^{to the medium does not antagonize this effect. In the dark, the accumulated Dap also inhibits ethylene production and decreases titer of other polyamines. Addition of Ca}^{to the incubation medium containing Dap competitively reduces the effects of Dap. Thus, Dap, like other polyamines, seems to require an initial attachment to a membrane site shared with Ca}^{before exerting its antisenescence action.}

Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.

Learn More