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作 者:MENGFanxia MIAOLong ZHANGShuqiu LOUChenghou
出 处:《Chinese Science Bulletin》2004年第5期471-475,共5页
摘 要:Acetyicholine (ACh) is an important neuro-chemical transmitter in animals; it also exists in plants and plays a significant role in various kinds of physiological functions in plants. ACh has been known to induce the stomatal opening. By monitoring the changes of cytusolic Ca^2+ with fluorescent probe Fiuo-3 AM under the confocal microscopy, we found that exogenous ACh increased cytosolic Ca^2+ concentration of guard cells of Vicia faba L. Muscarlne, an agonist of muscarine acetyicholine receptor (mAChR), could do so as well. In contrast, atropine, the antagonist of mAChR abolished the ability of ACh to increase Ca^2+ in guard cells. This mechanism is similar to mAChR in animals. When EGTA was used to chelate Ca^2+ or ruthenium red to block Ca^2+ released from vacuole respectively, the results showed that the increased cytosolic Ca^2+ mainly come from intracellular Ca^2+ store. The evidence supports that Ca^2+ is involved in guard-cell response to ACh and that Ca^2+ sigual is coupled to mAChRs in ACh signal transduction in guard cells.Acetylcholine (ACh) is an important neuro-chemical transmitter in animals; it also exists in plants and plays a significant role in various kinds of physiological functions in plants. ACh has been known to induce the stomatal opening. By monitoring the changes of cytosolic Ca2+ with fluorescent probe Fluo-3 AM under the confocal microscopy, we found that exogenous ACh increased cytosolic Ca2+ concentration of guard cells of Vicia faba L. Muscarine, an agonist of muscarine acetylcholine receptor (niAChR), could do so as well. In contrast, atropine, the antagonist of niAChR abolished the ability of ACh to increase Ca2+ in guard cells. This mechanism is similar to mAChR in animals. When EGTA was used to chelate Ca2+ or ruthenium red to block Ca2+ released from vacuole respectively, the results showed that the increased cytosolic Ca2+ mainly come from intracel-lular Ca2+ store. The evidence supports that Ca2+ is involved in guard-cell response to ACh and that Ca2+ signal is coupled to mAChRs in ACh signal transduction in guard cells.
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