钙调蛋白和钙调蛋白的一个20 kDa肌动蛋白结合片段可抑制去皮砂囊肌纤维束中的张力发展。
Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles.
作者信息
Pfitzer G, Zeugner C, Troschka M, Chalovich J M
机构信息
II, Physiologisches Institut, Universität Heidelberg, Germany.
出版信息
Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):5904-8. doi: 10.1073/pnas.90.13.5904.
Abstract
Caldesmon is known to inhibit actin-activated myosin ATPase activity in solution, to inhibit force production when added to skeletal muscle fibers, and to alter actin movement in the in vitro cell motility assay. It is less clear that caldesmon can inhibit contraction in smooth muscle cells in which caldesmon is abundant. We now show that caldesmon and its 20-kDa actin-binding fragment are able to inhibit force in chemically skinned gizzard fiber bundles, which are activated by a constitutively active myosin light-chain kinase in the presence and absence of okadaic acid. This inhibitory effect is reversed by high concentrations of Ca2+ and calmodulin. Therefore, caldesmon may act by increasing the level of myosin phosphorylation required to obtain full activation. Our results also suggest that caldesmon does not act to maintain force in smooth muscle by cross-linking myosin with actin since competition of binding of caldesmon with myosin does not cause a reduction in tension.
摘要
已知钙调蛋白能在溶液中抑制肌动蛋白激活的肌球蛋白ATP酶活性，添加到骨骼肌纤维时能抑制力的产生，并能在体外细胞运动分析中改变肌动蛋白的运动。目前尚不清楚钙调蛋白是否能抑制富含钙调蛋白的平滑肌细胞的收缩。我们现在表明，钙调蛋白及其20 kDa的肌动蛋白结合片段能够抑制化学去表皮的砂囊纤维束中的力，在有无冈田酸的情况下，这些纤维束由组成型活性肌球蛋白轻链激酶激活。高浓度的Ca2+和钙调蛋白可逆转这种抑制作用。因此，钙调蛋白可能通过提高获得完全激活所需的肌球蛋白磷酸化水平来发挥作用。我们的结果还表明，钙调蛋白不会通过将肌球蛋白与肌动蛋白交联来维持平滑肌中的力，因为钙调蛋白与肌球蛋白结合的竞争不会导致张力降低。
相似文献
1
Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles.钙调蛋白和钙调蛋白的一个20 kDa肌动蛋白结合片段可抑制去皮砂囊肌纤维束中的张力发展。
Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):5904-8. doi: 10.1073/pnas.90.13.5904.
2
Stimulation of the ATP-dependent interaction between actin and myosin by a myosin-binding fragment of smooth muscle caldesmon.平滑肌钙调蛋白的肌球蛋白结合片段对肌动蛋白和肌球蛋白之间ATP依赖性相互作用的刺激作用。
Cell Motil Cytoskeleton. 1994;29(3):250-8. doi: 10.1002/cm.970290308.
3
Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.在去表皮骨骼肌纤维中，钙调蛋白片段对肌动蛋白横桥结合的抑制作用。
Biophys J. 1997 Mar;72(3):1287-94. doi: 10.1016/S0006-3495(97)78775-7.
4
In vitro motility analysis of smooth muscle caldesmon control of actin-tropomyosin filament movement.平滑肌钙调蛋白对肌动蛋白-原肌球蛋白丝运动的体外运动分析。
J Biol Chem. 1995 Aug 25;270(34):19688-93. doi: 10.1074/jbc.270.34.19688.
5
Comparison of the effects of calponin and a 38-kDa caldesmon fragment on formation of the "strong-binding" state in ghost muscle fibers.钙调蛋白与38 kDa钙调素片段对鬼肌纤维中“强结合”状态形成的影响比较
Biochem Biophys Res Commun. 1996 Jun 14;223(2):240-4. doi: 10.1006/bbrc.1996.0878.
6
Phosphorylation of high-Mr caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction between actin and myosin.蛋白激酶C对高分子量钙调蛋白的磷酸化作用可调节该蛋白对肌动蛋白和肌球蛋白之间相互作用的调节功能。
Eur J Biochem. 1990 Mar 30;188(3):495-500. doi: 10.1111/j.1432-1033.1990.tb15427.x.
7
Mechanism for the inhibition of acto-heavy meromyosin ATPase by the actin/calmodulin binding domain of caldesmon.钙调蛋白结合肌动蛋白结构域抑制肌动蛋白-重酶解肌球蛋白ATP酶的机制。
Biochemistry. 1991 Jan 22;30(3):712-7. doi: 10.1021/bi00217a019.
8
Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin.钙调蛋白对ATP酶活性以及平滑肌和骨骼肌肌球蛋白亚片段与肌动蛋白结合的影响。
J Biol Chem. 1988 Feb 5;263(4):1878-85.
9
Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned fibres of chicken gizzard smooth muscle.钙调蛋白对鸡砂囊平滑肌肌动球蛋白ATP酶活性及皮肤纤维收缩的抑制作用。
FEBS Lett. 1985 Nov 11;192(1):9-12. doi: 10.1016/0014-5793(85)80032-6.
10
Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin.钙调蛋白抑制骨骼肌肌动球蛋白亚片段-1的ATP酶活性以及肌球蛋白亚片段-1与肌动蛋白的结合。
J Biol Chem. 1987 Apr 25;262(12):5711-6.
引用本文的文献
1
Dual thick and thin filament linked regulation of stretch- and L-NAME-induced tone in young and senescent murine basilar artery.年轻和衰老小鼠基底动脉中粗细肌丝双重连接调节拉伸和L-精氨酸甲酯诱导的张力
Front Physiol. 2023 Mar 28;14:1099278. doi: 10.3389/fphys.2023.1099278. eCollection 2023.
2
Caldesmon ablation in mice causes umbilical herniation and alters contractility of fetal urinary bladder smooth muscle.钙调蛋白在小鼠中被消融会导致脐疝，并改变胎儿膀胱平滑肌的收缩性。
J Gen Physiol. 2021 Jul 5;153(7). doi: 10.1085/jgp.202012776. Epub 2021 Jun 11.
3
New insights into myosin phosphorylation during cyclic nucleotide-mediated smooth muscle relaxation.环核苷酸介导的平滑肌松弛过程中肌球蛋白磷酸化的新见解。
J Muscle Res Cell Motil. 2012 Dec;33(6):471-83. doi: 10.1007/s10974-012-9306-9. Epub 2012 Jun 19.
4
Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1.p21激活激酶1对豚鼠平滑肌收缩及肌球蛋白轻链磷酸化的抑制作用
J Physiol. 2003 Jun 1;549(Pt 2):489-500. doi: 10.1113/jphysiol.2002.033167. Epub 2003 Apr 11.
5
Caldesmon exhibits a clustered distribution along individual chicken gizzard native thin filaments.钙调蛋白在单个鸡胗天然细肌丝上呈簇状分布。
J Muscle Res Cell Motil. 2001;22(1):77-90. doi: 10.1023/a:1010392322503.
6
Thiophosphorylation-induced Ca(2+) sensitization of guinea-pig ileum contractility is not mediated by Rho-associated kinase.硫代磷酸化诱导的豚鼠回肠收缩性的钙（2+）敏化并非由Rho相关激酶介导。
J Physiol. 2001 Jun 15;533(Pt 3):651-64. doi: 10.1111/j.1469-7793.2001.t01-2-00651.x.
7
Mutant Caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis.缺乏细胞周期蛋白依赖性激酶2（cdc2）磷酸化位点的突变型钙调蛋白延迟M期进入并抑制胞质分裂。
Mol Biol Cell. 2001 Jan;12(1):239-50. doi: 10.1091/mbc.12.1.239.
8
A role for p21-activated kinase in endothelial cell migration.p21激活激酶在内皮细胞迁移中的作用。
J Cell Biol. 1999 Nov 15;147(4):831-44. doi: 10.1083/jcb.147.4.831.
9
Caldesmon inhibits nonmuscle cell contractility and interferes with the formation of focal adhesions.钙调蛋白抑制非肌细胞的收缩性，并干扰粘着斑的形成。
Mol Biol Cell. 1999 Oct;10(10):3097-112. doi: 10.1091/mbc.10.10.3097.
10
Clostridium difficile toxin B inhibits carbachol-induced force and myosin light chain phosphorylation in guinea-pig smooth muscle: role of Rho proteins.艰难梭菌毒素B抑制豚鼠平滑肌中卡巴胆碱诱导的张力及肌球蛋白轻链磷酸化：Rho蛋白的作用
J Physiol. 1998 Jan 1;506 ( Pt 1)(Pt 1):83-93. doi: 10.1111/j.1469-7793.1998.083bx.x.
本文引用的文献
1
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
2
Calmodulin is essential for smooth muscle contraction.钙调蛋白对平滑肌收缩至关重要。
FEBS Lett. 1981 Mar 23;125(2):141-5. doi: 10.1016/0014-5793(81)80704-1.
3
Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin.从鸡砂囊中纯化一种与F-肌动蛋白相互作用的钙调蛋白结合蛋白。
Proc Natl Acad Sci U S A. 1981 Sep;78(9):5652-5. doi: 10.1073/pnas.78.9.5652.
4
Ca2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography.钙调蛋白上钙离子诱导的疏水位点：用于通过苯基-琼脂糖亲和色谱法纯化钙调蛋白
Biochem Biophys Res Commun. 1982 Jan 29;104(2):830-6. doi: 10.1016/0006-291x(82)90712-4.
5
Isolation of the native form of chicken gizzard myosin light-chain kinase.鸡肌胃肌球蛋白轻链激酶天然形式的分离。
Biochem J. 1984 Mar 15;218(3):863-70. doi: 10.1042/bj2180863.
6
Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.钙调蛋白对平滑肌肌动蛋白激活的肌球蛋白Mg2 + -ATP酶活性的抑制作用。
J Biol Chem. 1984 Nov 25;259(22):13656-9.
7
Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.平滑肌钙调蛋白。快速纯化及F-肌动蛋白交联特性。
J Biol Chem. 1984 Oct 25;259(20):12873-80.
8
Caldesmon150 regulates the tropomyosin-enhanced actin-myosin interaction in gizzard smooth muscle.钙调蛋白150调节肌胃平滑肌中肌动蛋白-肌球蛋白相互作用增强的原肌球蛋白。
Biochem Biophys Res Commun. 1985 Oct 30;132(2):645-51. doi: 10.1016/0006-291x(85)91181-7.
9
Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle.钙调蛋白是一种细长、灵活的分子，定位于平滑肌的肌动球蛋白结构域。
EMBO J. 1986 Feb;5(2):251-7. doi: 10.1002/j.1460-2075.1986.tb04206.x.
10
Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-independent fragments.
J Biol Chem. 1987 Oct 5;262(28):13828-34.
Zotero 插件