Water and nonelectrolyte permeability of plant cell membranes after short term application of amino acids and phosphorylated amino acids |
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Authors: | Yong-Fang Li Yu-Fen Zhao In-Sup So Ok Young Lee-Stadelmann |
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Affiliation: | (1) Department of Chemistry, Tsing hua University, 100084 Beijing, China;(2) Department of Biology, Cheju National University, Cheju City, Korea;(3) Department of Horticulture, Cheju National University, Cheju City, Korea;(4) Department of Horticultural Science, University of Minnesota, 55108 St. Paul, MN, USA |
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Abstract: | The effects of amino acids (aa) and N-(diisopropyloxyphosphoryl)-amino acids (DIPP-aa) on cell membranes were investigated by evaluating water and methyl urea permeability. Permeability coefficients Pf and Ps were determined by standard osmotic methods for cells ofPisum sativum stem base epidermis after 20 min exposure to a 5 mM solution of each aa and DIPP-aa. The Pf value ofP. sativum epidermal cells (untreated controls) was 1.3 ± 0.4 × 10-3 μm s-1. Treat ments with the diisopropyl-oxyphosphoryl derivatives of three one charged and three polar amino acids (serine, threonine, asparagine, and aspartic acid) and unsubstituted (free) serine and threonine increased water permeability up to about two fold of the control value. Serine and threonine and their DIPP-derivatives increased methyl urea permeability (controls 1.03 ± 0.09 × 10-3 μm s-1) 30 to 80 percent Other amino acids and their DIPP-derivatives caused small or insignificant changes of water permeability. Only certain polar amino acids and their DIPP-derivatives increased the osmotic water and methyl urea permeation through the plasma membrane. The specificity of these molecules on plasma membranes suggests that the active amino acids (serine and threonine) and their DIPP-derivatives interact with charged membrane molecules. The relatively small changes in water and methyl urea permeability may indicate that the effective aa’s and their DIPP-derivatives interact with phospholipids rather than aquaporin. A concurring alteration of water channel proteins, however, cannot excluded. |
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Keywords: | Permeability coefficient Plasmamembrane serine solute permeability threonine water transport |
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