Brassica juncea nitric oxide synthase like activity is stimulated by PKC activators and calcium suggesting modulation by PKC-like kinase

Copyright © 2012 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 60(2012) vom: 28. Nov., Seite 157-64
1. Verfasser: Talwar, Pooja Saigal (VerfasserIn)
Weitere Verfasser: Gupta, Ravi, Maurya, Arun Kumar, Deswal, Renu
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Enzyme Activators Enzyme Inhibitors Oxyhemoglobins Plant Proteins Citrulline 29VT07BGDA Nitric Oxide 31C4KY9ESH mehr... NADP 53-59-8 Nitric Oxide Synthase EC 1.14.13.39 Protein Kinase C EC 2.7.11.13 Calcium SY7Q814VUP NG-Nitroarginine Methyl Ester V55S2QJN2X
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100 1 |a Talwar, Pooja Saigal  |e verfasserin  |4 aut 
245 1 0 |a Brassica juncea nitric oxide synthase like activity is stimulated by PKC activators and calcium suggesting modulation by PKC-like kinase 
264 1 |c 2012 
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500 |a Date Completed 24.12.2013 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2012 Elsevier Masson SAS. All rights reserved. 
520 |a Nitric oxide (NO) is an important signaling molecule having varied physiological and regulatory roles in biological systems. The fact that nitric oxide synthase (NOS) is responsible for NO generation in animals, prompted major search for a similar enzyme in plants. Arginine dependent NOS like activity (BjNOSla) was detected in Brassica juncea seedlings using oxyhemoglobin and citrulline assays. BjNOSla showed 25% activation by NADPH (0.4 mM) and 40% by calcium (0.4 mM) but the activity was flavin mononucleotide (FMN), flavin dinucleotide (FAD) and calmodulin (CaM) independent. Pharmacological approach using mammalian NOS inhibitors, NBT (300 μM) and l-NAME (5 mM), showed significant inhibition (100% and 67% respectively) supporting that the BjNOSla operates via the oxidative pathway. Most of the BjNOSla activity (80%) was confined to shoot while root showed only 20% activity. Localization studies by NADPH-diaphorase and DAF-2DA staining showed the presence of BjNOSla in guard cells. Kinetic analysis showed positive cooperativity with calcium as reflected by a decreased K(m) (∼13%) and almost two fold increase in V(max). PMA (438 nM), a kinase activator, activated BjNOSla ∼1.9 fold while its inactive analog 4αPDD was ineffective. Calcium and PMA activated the enzyme to ∼3 folds. Interestingly, 1,2-DG6 (2.5 μM) and PS (1 μM) with calcium activated the enzyme activity to ∼7 fold. A significant inhibition of BjNOSla by PKC inhibitors-staurosporine (∼90%) and calphostin-C (∼40%), further supports involvement of PKC-like kinase. The activity was also enhanced by abiotic stress conditions (7-46%). All these findings suggest that BjNOSla generates NO via oxidative pathway and is probably regulated by phosphorylation 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Enzyme Activators  |2 NLM 
650 7 |a Enzyme Inhibitors  |2 NLM 
650 7 |a Oxyhemoglobins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Citrulline  |2 NLM 
650 7 |a 29VT07BGDA  |2 NLM 
650 7 |a Nitric Oxide  |2 NLM 
650 7 |a 31C4KY9ESH  |2 NLM 
650 7 |a NADP  |2 NLM 
650 7 |a 53-59-8  |2 NLM 
650 7 |a Nitric Oxide Synthase  |2 NLM 
650 7 |a EC 1.14.13.39  |2 NLM 
650 7 |a Protein Kinase C  |2 NLM 
650 7 |a EC 2.7.11.13  |2 NLM 
650 7 |a Calcium  |2 NLM 
650 7 |a SY7Q814VUP  |2 NLM 
650 7 |a NG-Nitroarginine Methyl Ester  |2 NLM 
650 7 |a V55S2QJN2X  |2 NLM 
700 1 |a Gupta, Ravi  |e verfasserin  |4 aut 
700 1 |a Maurya, Arun Kumar  |e verfasserin  |4 aut 
700 1 |a Deswal, Renu  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 60(2012) vom: 28. Nov., Seite 157-64  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:60  |g year:2012  |g day:28  |g month:11  |g pages:157-64 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2012.08.005  |3 Volltext 
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