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Abscisic acid activates a Ca2+-calmodulin-stimulated protein kinase involved in antioxidant defense in maize leaves.
Acta Biochim Biophys Sin (Shanghai). 2010 Sep; 42(9):646-55.AB

Abstract

The role of a calcium-dependent and calmodulin (CaM)-stimulated protein kinase in abscisic acid (ABA)-induced antioxidant defense was determined in leaves of maize (Zea mays). In-gel kinase assays showed that treatments with ABA or H(2)O(2) induced the activation of a 49-kDa protein kinase and a 52-kDa protein kinase significantly. Furthermore, we showed that the 52-kDa protein kinase has the characteristics of CaM-stimulating activity and is sensitive to calcium-CaM-dependent protein kinase II (CaMK II) inhibitor KN-93 or CaM antagonist W-7. Treatments with ABA or H(2)O(2) not only induced the activation of the 52-kDa protein kinase, but also enhanced the total activities of the antioxidant enzymes, including catalase, ascorbate peroxidase, glutathione reductase, and superoxide dismutase. Such enhancements were blocked by pretreatment with a CaMK inhibitor and a reactive oxygen species (ROS) inhibitor or scavenger. Pretreatment with the CaMK inhibitor also substantially arrested the ABA-induced H(2)O(2) production. Kinase activity enhancements induced by ABA were attenuated by pretreatment with an ROS inhibitor or scavenger. These results suggest that the 52-kDa CaMK is involved in ABA-induced antioxidant defense and that cross-talk between CaMK and H(2)O(2) plays a pivotal role in ABA signaling. We infer that CaMK acts both upstream and downstream of H(2)O(2), but mainly acts between ABA and H(2)O(2) in ABA-induced antioxidant-defensive signaling.

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Authors+Show Affiliations

Xu S
Fuyang Teachers College, China. xscjack@tom.com

MeSH

Abscisic AcidAntioxidantsAscorbate PeroxidasesBenzylaminesCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCatalaseDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEnzyme ActivationEnzyme AssaysGlutathione ReductaseHydrogen PeroxideMolecular WeightOxidantsPeroxidasesPlant Growth RegulatorsPlant LeavesProtein Kinase InhibitorsSulfonamidesSuperoxide DismutaseTime FactorsZea mays

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20702465

Citation

Xu, Shucheng. "Abscisic Acid Activates a Ca2+-calmodulin-stimulated Protein Kinase Involved in Antioxidant Defense in Maize Leaves." Acta Biochimica Et Biophysica Sinica, vol. 42, no. 9, 2010, pp. 646-55.
Xu S. Abscisic acid activates a Ca2+-calmodulin-stimulated protein kinase involved in antioxidant defense in maize leaves. Acta Biochim Biophys Sin (Shanghai). 2010;42(9):646-55.
Xu, S. (2010). Abscisic acid activates a Ca2+-calmodulin-stimulated protein kinase involved in antioxidant defense in maize leaves. Acta Biochimica Et Biophysica Sinica, 42(9), 646-55. https://doi.org/10.1093/abbs/gmq064
Xu S. Abscisic Acid Activates a Ca2+-calmodulin-stimulated Protein Kinase Involved in Antioxidant Defense in Maize Leaves. Acta Biochim Biophys Sin (Shanghai). 2010;42(9):646-55. PubMed PMID: 20702465.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Abscisic acid activates a Ca2+-calmodulin-stimulated protein kinase involved in antioxidant defense in maize leaves. A1 - Xu,Shucheng, Y1 - 2010/08/11/ PY - 2010/8/13/entrez PY - 2010/8/13/pubmed PY - 2011/2/8/medline SP - 646 EP - 55 JF - Acta biochimica et biophysica Sinica JO - Acta Biochim Biophys Sin (Shanghai) VL - 42 IS - 9 N2 - The role of a calcium-dependent and calmodulin (CaM)-stimulated protein kinase in abscisic acid (ABA)-induced antioxidant defense was determined in leaves of maize (Zea mays). In-gel kinase assays showed that treatments with ABA or H(2)O(2) induced the activation of a 49-kDa protein kinase and a 52-kDa protein kinase significantly. Furthermore, we showed that the 52-kDa protein kinase has the characteristics of CaM-stimulating activity and is sensitive to calcium-CaM-dependent protein kinase II (CaMK II) inhibitor KN-93 or CaM antagonist W-7. Treatments with ABA or H(2)O(2) not only induced the activation of the 52-kDa protein kinase, but also enhanced the total activities of the antioxidant enzymes, including catalase, ascorbate peroxidase, glutathione reductase, and superoxide dismutase. Such enhancements were blocked by pretreatment with a CaMK inhibitor and a reactive oxygen species (ROS) inhibitor or scavenger. Pretreatment with the CaMK inhibitor also substantially arrested the ABA-induced H(2)O(2) production. Kinase activity enhancements induced by ABA were attenuated by pretreatment with an ROS inhibitor or scavenger. These results suggest that the 52-kDa CaMK is involved in ABA-induced antioxidant defense and that cross-talk between CaMK and H(2)O(2) plays a pivotal role in ABA signaling. We infer that CaMK acts both upstream and downstream of H(2)O(2), but mainly acts between ABA and H(2)O(2) in ABA-induced antioxidant-defensive signaling. SN - 1745-7270 UR - https://www.unboundmedicine.com/medline/citation/20702465/Abscisic_acid_activates_a_Ca2+_calmodulin_stimulated_protein_kinase_involved_in_antioxidant_defense_in_maize_leaves_ L2 - https://academic.oup.com/abbs/article-lookup/doi/10.1093/abbs/gmq064 DB - PRIME DP - Unbound Medicine ER -