Plant and Cell Physiology, 2000, Vol. 41, No. 8 960-967
© 2000 Oxford University Press
Are Isocitrate Lyase and Phosphoenolpyruvate Carboxykinase Involved in Gluconeogenesis during Senescence of Barley Leaves and Cucumber Cotyledons?
1 Robert Hill Institute and Department of Animal and Plant Sciences, University of Sheffield, Sheffield S10 2TN, U.K. 2 Department of Biological Sciences, Lancaster University, Lancaster LA1 4YQ, U.K.
The aim of this study was to investigate whether gluconeogenesis catalysed by phosphoenolpyruvate carboxykinase (PEPCK) occurs during leaf senescence. This was addressed by determining changes in the abundance and intercellular location of enzymes necessary for gluconeogenesis during the senescence of barley leaves and cucumber cotyledons. PEPCK was never present in barley leaves, despite the presence of large amounts of isocitrate lyase (ICL), a key enzyme of the glyoxylate cycle, and of its product, glyoxylate. Although PEPCK was present in non-senescent cucumber cotyledons, its abundance declined during senescence. Throughout senescence, PEPCK was only present in the trichomes and vasculature, whereas ICL was located in mesophyll cells. Pyruvate,Pi dikinase (PPDK) which, in concert with NAD(P)-malic enzyme, is also capable of catalysing gluconeogenesis, was present in non-senescent barley leaves and cucumber cotyledons, but in both plants its abundance decreased greatly during senescence. The abundance of ICL was greatly reduced in senescing detached barley leaves by either illumination or by co-incubation with sucrose, and greatly increased in darkened attached barley leaves. These results argue against the large-scale occurrence of gluconeogenesis during senescence catalysed either by PEPCK or PPDK. In cucumber cotyledons, PEPCK may play a role in metabolic processes linked to the export of amino acids, a role in which phosphoenolpyruvate carboxylase may also be involved. The amount of ICL was increased by starvation and during senescence may function in the conversion of lipids to organic acids, which are then utilised in the mobilisation of amino acids from leaf protein.
4 Present address: Botanisches Institut der Universität Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland.
5 Corresponding author: E-mail, r.leegood@shef.ac.uk; Fax, +44-114-222-0050; Phone, +44-114-222-0040.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  F. Famiani and R. P. Walker Changes in Abundance of Enzymes Involved in Organic Acid, Amino Acid and Sugar Metabolism, and Photosynthesis during the Ripening of Blackberry Fruit J. Amer. Soc. Hort. Sci., March 1, 2009; 134(2): 167 - 175. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. C. Leegood Roles of the bundle sheath cells in leaves of C3 plants J. Exp. Bot., May 1, 2008; 59(7): 1663 - 1673. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. G. van Doorn and E. J. Woltering Physiology and molecular biology of petal senescence J. Exp. Bot., March 3, 2008; (2008) erm356v2. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Famiani, N. G. M. Cultrera, A. Battistelli, V. Casulli, P. Proietti, A. Standardi, Z.-H. Chen, R. C. Leegood, and R. P. Walker Phosphoenolpyruvate carboxykinase and its potential role in the catabolism of organic acids in the flesh of soft fruit during ripening J. Exp. Bot., November 1, 2005; 56(421): 2959 - 2969. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. P. Walker, Z.-H. Chen, K. E. Johnson, F. Famiani, L. Tecsi, and R. C. Leegood Using immunohistochemistry to study plant metabolism: the examples of its use in the localization of amino acids in plant tissues, and of phosphoenolpyruvate carboxykinase and its possible role in pH regulation J. Exp. Bot., April 1, 2001; 52(356): 565 - 576. [Abstract] [Full Text] [PDF]
|
|