Mechanisms of nitric-oxide-induced increase of free cytosolic Ca2+ concentration in Nicotiana plumbaginifolia cells
| العنوان: | Mechanisms of nitric-oxide-induced increase of free cytosolic Ca2+ concentration in Nicotiana plumbaginifolia cells |
|---|---|
| المؤلفون: | Cécile Courtois, David Wendehenne, Alain Pugin, Olivier Lamotte, Grażyna Dobrowolska, Angélique Besson |
| المصدر: | Free radical biologymedicine. 40(8) |
| سنة النشر: | 2005 |
| مصطلحات موضوعية: | Cations, Divalent, Nicotiana tabacum, Aequorin, Nitric Oxide, Biochemistry, Nitric oxide, Cell Line, chemistry.chemical_compound, Cytosol, Physiology (medical), medicine, Staurosporine, Phosphorylation, Protein kinase A, Nicotiana plumbaginifolia, Solanaceae, biology, Cell Membrane, Depolarization, biology.organism_classification, Molecular biology, Molecular Weight, chemistry, Biophysics, biology.protein, Calcium, Protein Kinases, medicine.drug |
| الوصف: | In this study, we investigated a role for nitric oxide (NO) in mediating the elevation of the free cytosolic Ca(2+) concentration ([Ca(2+)](cyt)) in plants using Nicotiana plumbaginifolia cells expressing the Ca(2+) reporter apoaequorin. Hyperosmotic stress induced a fast increase of [Ca(2+)](cyt) which was strongly reduced by pretreating cell suspensions with the NO scavenger carboxy PTIO, indicating that NO mediates [Ca(2+)](cyt) changes in plant cells challenged by abiotic stress. Accordingly, treatment of transgenic N. plumbaginifolia cells with the NO donor diethylamine NONOate was followed by a transient increase of [Ca(2+)](cyt) sensitive to plasma membrane Ca(2+) channel inhibitors and antagonist of cyclic ADP ribose. We provided evidence that NO might activate plasma membrane Ca(2+) channels by inducing a rapid and transient plasma membrane depolarization. Furthermore, NO-induced elevation of [Ca(2+)](cyt) was suppressed by the kinase inhibitor staurosporine, suggesting that NO enhances [Ca(2+)](cyt) by promoting phosphorylation-dependent events. This result was further supported by the demonstration that the NO donor induced the activation of a 42-kDa protein kinase which belongs to SnRK2 families and corresponds to Nicotiana tabacum osmotic-stress-activated protein kinase (NtOSAK). Interestingly, NtOSAK was activated in response to hyperosmotic stress through a NO-dependent process, supporting the hypothesis that NO also promotes protein kinase activation during physiological processes. |
| تدمد: | 0891-5849 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e758ac74dc0692ed3c04ce93fc33f210Test https://pubmed.ncbi.nlm.nih.gov/16631527Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....e758ac74dc0692ed3c04ce93fc33f210 |
| قاعدة البيانات: | OpenAIRE |
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Hyperosmotic stress induced a fast increase of [Ca(2+)](cyt) which was strongly reduced by pretreating cell suspensions with the NO scavenger carboxy PTIO, indicating that NO mediates [Ca(2+)](cyt) changes in plant cells challenged by abiotic stress. Accordingly, treatment of transgenic N. plumbaginifolia cells with the NO donor diethylamine NONOate was followed by a transient increase of [Ca(2+)](cyt) sensitive to plasma membrane Ca(2+) channel inhibitors and antagonist of cyclic ADP ribose. We provided evidence that NO might activate plasma membrane Ca(2+) channels by inducing a rapid and transient plasma membrane depolarization. Furthermore, NO-induced elevation of [Ca(2+)](cyt) was suppressed by the kinase inhibitor staurosporine, suggesting that NO enhances [Ca(2+)](cyt) by promoting phosphorylation-dependent events. 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