Relationship between paxillin and myosin phosphorylation during muscarinic stimulation of smooth muscle.
Relationship between paxillin and myosin phosphorylation during muscarinic stimulation of smooth muscle.
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DOI:
10.1152/ajpcell.1998.274.3.c741
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发表时间:
1998-03
期刊:
影响因子:
--
通讯作者:
Dolly Mehta;Zhonglin Wang;M. Wu;S. Gunst
中科院分区:
文献类型:
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作者:
Dolly Mehta;Zhonglin Wang;M. Wu;S. Gunst
The tyrosine phosphorylation of paxillin increases in association with force development during tracheal smooth muscle contraction, suggesting that paxillin plays a role in the contractile activation of smooth muscle [Z. L. Wang, F. M. Pavalko, and S. J. Gunst. Am. J. Physiol. 271 ( Cell Physiol. 40): C1594-C1602, 1996]. We compared the Ca2+ sensitivity of the tyrosine phosphorylation of paxillin and myosin light chain (MLC) phosphorylation in tracheal muscle and evaluated whether MLC phosphorylation is necessary to induce paxillin phosphorylation. Ca2+-depleted muscle strips were stimulated with 10-7-10-4M acetylcholine (ACh) in 0, 0.05, 0.1, or 0.5 mM extracellular Ca2+. In the absence of extracellular Ca2+, 10-4 M ACh induced a maximal increase in paxillin phosphorylation without increasing MLC phosphorylation or force. Increases in extracellular Ca2+ concentration did not further increase paxillin phosphorylation. However, during stimulation with 10-6 M ACh, paxillin phosphorylation increased with increases in extracellular Ca2+ concentration. We conclude that the tyrosine phosphorylation of paxillin can be stimulated by signaling pathways that do not depend on Ca2+ mobilization and that the activation of contractile proteins is not required to elicit paxillin phosphorylation.