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Publication Type J
Authors Ashihara, H., S. Wakahara, M. Suzuki, A. Kato, H. Sasamoto and S. Baba
Title Comparison of adenosine metabolism in leaves of several mangrove plants and a poplar species
Source Plant Physiology and Biochemistry
Abstract A possible increased demand for ATP in salt-tolerant mangrove plants was studied by the comparison of metabolic fates of [8-C-14] adenosine in leaf disks of several mangrove plants and of poplar. In mangrove trees, Rhizophora stylosa, Bruguiera gymnorrhiza, Kandelia candel and Sonneratia alba, 56-92% of [8-C-14]adenosine taken up by leaf disks was converted during 3 h incubation to salvage products, i.e., nucleotides and RNA. Synthesis of nucleotides including ATP was stimulated by salt stress induced by 250 mM NaCl. In leaf disks of Avicennia marina, a mangrove shrub that produces glycinebetaine as compatible solutes, 46% of radioactivity entered salvage products when [8-C-14] adenosine was continuously supplied to the leaf disks. Hydrolysis of adenosine to adenine was extremely active in this mangrove shrub. This is probably due to the high activity of adenosine nucleosidase (EC 3.2.2.7). In leaf disks of another mangrove shrub, Lumnitzera racemosa, only limited amounts of [8-C-14]adenosine were metabolised (< ca. 30% taken up by leaf disks), but synthesis of ATP and ADP was stimulated by salt stress. In Pemphis acidula leaf disks, adenosine salvage activity was low and more than 300% of adenosine was hydrolysed to adenine. In leaf disks of poplar, a non-salt-resistant plant, ca. 40% of [8-C-14] adenosine was converted to salvage products during 3 h of incubation, but the rate was slightly reduced by treatment with 250 mM NaCl. The present results suggest that large mangrove trees generally have efficient adenosine salvage ability, which is stimulated by salt. Lesser salvage activity is found in small size mangrove shrubs, although salt generally still enhances salvage activity. (C) 2002 Editions scientifiques et medicales Elsevier SAS. All rights reserved.
Publication Date Feb
Year Published 2003
Volume 41
Issue 2
Beginning Page 133-139
Unique Article Identifier ISI:000182246500005
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