Document Detail


Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves. Evidence from the effects of okadaic acid and microcystin.
MedLine Citation:
PMID:  2171989     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sucrose-phosphate synthase (SPS) purified from spinach leaves harvested in the dark, was activated by mammalian protein phosphatase 2A (PP2A). Activation of SPS in a fraction from darkened spinach leaves was largely prevented by either okadaic acid or microcystin-LR (specific inhibitors of PPI and PP2A), while inhibitor-2 (a PP1 inhibitor) or Mg2+ (essential for PP2C) were ineffective. In vivo, okadaic acid and microcystin-LR prevented the light-induced activation of SPS and decreased sucrose biosynthesis and CO2 fixation. It is concluded that PP2A is the major SPS phosphatase in spinach. This study is the first to employ microcystin-LR for modulating protein phosphorylation in vivo.
Authors:
G Siegl; C MacKintosh; M Stitt
Related Documents :
3931969 - Characterization of fe2+-activated acid phosphatase in rat epidermis.
6101549 - Rate of decrease of glutamyltransferase and acid phosphatase activities in the human va...
3385809 - Determination of deoxymononucleotides and deoxynucleosides as a tool for toxicological ...
24996939 - Vertical distributions of bound saturated fatty acids and compound-specific stable carb...
11108009 - Characterization of acid phosphatase activities in the equine pathogen streptococcus equi.
10494879 - Contribution of mdr1b-type p-glycoprotein to okadaic acid resistance in rat pituitary g...
7913139 - In vivo acidosis reduces extracellular concentrations of taurine and glutamate in the r...
12494309 - Fatty acid and sn-2 fatty acid composition in human milk from granada (spain) and in in...
3412119 - Hydroxyacid derivatives in human epidermis.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  270     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1990 Sep 
Date Detail:
Created Date:  1990-12-10     Completed Date:  1990-12-10     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  198-202     Citation Subset:  IM    
Affiliation:
Lehrstuhl für Pflanzenphysiologie, Universität Bayreuth, FRG.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Cyanobacteria
Enzyme Activation
Ethers, Cyclic / pharmacology
Glucosyltransferases / isolation & purification,  metabolism*
Marine Toxins / pharmacology
Microcystins
Okadaic Acid
Peptides, Cyclic / pharmacology
Phosphoprotein Phosphatases / physiology*
Phosphorylation / drug effects
Photosynthesis / physiology
Plants / enzymology*
Protein Phosphatase 2
Chemical
Reg. No./Substance:
0/Ethers, Cyclic; 0/Marine Toxins; 0/Microcystins; 0/Peptides, Cyclic; 101043-37-2/cyanoginosin LR; 78111-17-8/Okadaic Acid; EC 2.4.1.-/Glucosyltransferases; EC 2.4.1.14/sucrose-phosphate synthase; EC 3.1.3.16/Phosphoprotein Phosphatases; EC 3.1.3.16/Protein Phosphatase 2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Functional involvement of calcium in the homologous up-regulation of the 1,25-dihydroxyvitamin D3 re...
Next Document:  Light-dependent delta mu Na-generation and utilization in the marine cyanobacterium Oscillatoria bre...