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You searched for subject:(actin myosin interaction). Showing records 1 – 3 of 3 total matches.

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1. 三橋, 里子. Blebbistatinによる気管平滑筋スキンド標本弛緩促進作用のメカニズム : Mechanisms of accelerating effect of blebbistatin on relaxation process of skinned tracheal smooth muscle.

Degree: 修士(健康科学), 2017, Tokyo Metropolitan University / 首都大学東京

[緒言] ミオシンII阻害薬であるblebbiststinは、平滑筋アクトミオシンATPase活性を10μM程度で抑制する。blebbistatinは平滑筋標本においては収縮のCa^<2+>感受性やミオシン軽鎖リン酸化レベルには影響は与えず、アクチン・ミオシン相互作用を直接抑制することにより、その収縮を抑制するといわれている。blebbistatinはミオシンATPase加水分解サイクルに伴うミオシンのアクチンへの結合・解離に影響を及ぼすことが考えられることから、弛緩過程におけるクロスブリッジの解離にも影響を与えることが推察される。そこで本研究では、細胞膜を化学的に破壊して気管平滑筋スキンド標本のCa^<2+>収縮後の弛緩過程とミオシンATPaseサイクルの影響を受けないrigor形成・解離に対するblebbistatinの効果を動力学的に検討した。[方法] モルモット気管平滑筋に100μMのβ-escinで処理をしてスキンド標本を作製し、圧トランスデューサーに取り付けて等尺性張力を測定した。Ca^<2+>による最大収縮の後、EGTAによりCa^<2+>を素早く除去して弛緩させ、同時にblebbistatinを添加し15分間計測した。また、Ca^<2+>収縮後のrigor状態におけるblebbistatinについても同様の方法で検討した。統計処理はt-testを使用しP<0.05を有意水準とした。[結果] Ca^<2+>収縮後の弛緩過程において、気管平滑筋スキンド標本は30μM程度で弛緩過程を促進し、回帰分析の結果からラッチの解離を速めていた。一方、Ca^<2+>収縮後のrigor状態では相対張力において有意な弛緩はみられなかったが、回帰分析の結果、30μMでrigorの解離の抑制と収縮後一度外れたクロスブリッジがrigorに移行する割合がコントロール群と比較して少ない値を示した。[考察] Blebbistatinは、ATPやアクチンのミオシンへの結合を直接阻害するのではなく、ミオシン頭部構造変化に影響してアクチン・ミオシン結合を弱めることが知られている。ATPの有無によって、Ca^<2+>収縮で発生した収縮張力のCa^<2+>除去後の減衰過程に対するblebbistatinの影響が異なるのは、blebbistatinがミオシン頭部構造変化に与える効果はミオシン頭部へのATPの結合の有無によって変化することを強く示唆する。平滑筋細胞において無酸素状態における力学反応の実態は不明であるが、blebbistatinはその解明に向けて研究において有用なツールになると考えられる。

Blebbistatin, an inhibitor of myosin II , has an inhibitory effect on smooth muscle actomyosin ATPase activity at around 10μM. Blebbistatin is also known to suppress the smooth contraction by direct inhibition of myosin-actin interaction without any effects on Ca^<2+> sensitivity to the force or phosphorylation level of myosin light chain. In the present study, to assess the blebbistatin effects on actin-myosin interaction in detail, we investigated effect of blebbistatin in the relaxation process and the reducing rigor tension after the Ca^<2+>-induced contraction using with skinned tracheal smooth muscle kinetically. A tracheal muscle preparation skinned (cell membrane permeabilized) with 100μM β-escin was attached to a force transducer to measure tension mechanical force. After contractile force induced with 10μM Ca^<2+> reached a steady level, Ca^<2+> was quickly removed in the absence or presence of ATP, resulting in relaxation process or reducing rigor tension respectively, with or without blebbistatin for 15 min. The relaxation process after the Ca^<2+>-removal was accelerated in the presence of 30μM blebbistatin and this effect of blebbistatin seemed to result from acceleration of detach from so called “latch” state. On the other hand, blebbistatin at 301M accelerated detachment of rigor bridge and reduced the forming rigor bridges in the absence of ATP, although the agent did not significantly changes in the tension level during decrease in the rigor tension after Ca^<2+> removal. The difference of the blebbistatin effects on the force between relaxation process and reducing rigor tension seems to be due to distinct effects of the agent on conformational changes of myosin in the absence and presence of ATP, because blebbistatin is known not to directly inhibit ATP binding to myosin, but to actin binding affinity of myosin.

首都大学東京, 2017-03-25, 修士(健康科学)

Subjects/Keywords: 気道平滑筋; ラッチ; ブレビスタチン; アクチン・ミオシン相互作用; airway smooth muscle; latch; blebbistatin; actin-myosin interaction

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

三橋, . (2017). Blebbistatinによる気管平滑筋スキンド標本弛緩促進作用のメカニズム : Mechanisms of accelerating effect of blebbistatin on relaxation process of skinned tracheal smooth muscle. (Thesis). Tokyo Metropolitan University / 首都大学東京. Retrieved from http://hdl.handle.net/10748/00009633

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

三橋, 里子. “Blebbistatinによる気管平滑筋スキンド標本弛緩促進作用のメカニズム : Mechanisms of accelerating effect of blebbistatin on relaxation process of skinned tracheal smooth muscle.” 2017. Thesis, Tokyo Metropolitan University / 首都大学東京. Accessed March 01, 2021. http://hdl.handle.net/10748/00009633.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

三橋, 里子. “Blebbistatinによる気管平滑筋スキンド標本弛緩促進作用のメカニズム : Mechanisms of accelerating effect of blebbistatin on relaxation process of skinned tracheal smooth muscle.” 2017. Web. 01 Mar 2021.

Vancouver:

三橋 . Blebbistatinによる気管平滑筋スキンド標本弛緩促進作用のメカニズム : Mechanisms of accelerating effect of blebbistatin on relaxation process of skinned tracheal smooth muscle. [Internet] [Thesis]. Tokyo Metropolitan University / 首都大学東京; 2017. [cited 2021 Mar 01]. Available from: http://hdl.handle.net/10748/00009633.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

三橋 . Blebbistatinによる気管平滑筋スキンド標本弛緩促進作用のメカニズム : Mechanisms of accelerating effect of blebbistatin on relaxation process of skinned tracheal smooth muscle. [Thesis]. Tokyo Metropolitan University / 首都大学東京; 2017. Available from: http://hdl.handle.net/10748/00009633

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

2. 王, 志丹. Caffeine inhibits smooth muscle actin-myosin interaction : カフェインは平滑筋ミオシンアクチン相互作用を抑制する.

Degree: 修士(健康科学), 2017, Tokyo Metropolitan University / 首都大学東京

Caffeine is known to have inhibitory effects on Ca^<2+>-induced contraction in smooth muscle, and possible mechanisms may contribute the inhibitory effects. Recently, it was found a caffeine effect on direct inhibition of myosin-actin interaction in smooth muscle. To clarify whether direct inhibition of myosin-actin interaction of caffeine to be dependent on the regulation of myosin light chain phosphorylation, in the present study, the author examined caffeine effects on skinned (cell membrane permeabilized) smooth muscle contraction. At 10 mM, caffeine significantly suppressed Ca^<2+> induced contraction, which was dependent on myosin light chain phosphorylation. On the other hand, caffeine did not affect 15.5 mM Mg^<2+> induced contraction, which was independent of myosin light chain phosphorylation. The present results suggest that caffeine inhibits actin-myosin interaction of smooth muscle through either inhibition of myosin light chain kinase activity or acceleration of myosin phosphatase activity.

カフェインには平滑筋にCaイオンの抑制があることが知られている。様々な機構がこの抑制に関与している。最近、カフェインは平滑筋のミオシンアクチン相互作用を直接的に抑制することが明らかになった。本研究では、細胞膜を破壊したスキンド盲腸紐標本を用いて、カフェインの平滑筋アクチン・ミオシン相互作用の抑制が、ミオシン軽鎖リン酸化の抑制によるものなのかを検討した。10mMのカェインはミオシン軽鎖リン酸化に依存するCaイオン活性化収縮張力を抑制した。一方、カフェインはミオシン軽鎖リン酸化に依存しない15.5mM Mgイオンによる収縮張力を抑制しない。以上から、カフェインはミオシン軽鎖リン酸化酵素の活性阻害、もしくはミオシンボスファターゼの活性を促進することでミオシン軽鎖リン酸化レベルを低下させることで、平滑筋ミオシンアクチン相互作用を抑制し、平滑筋収縮を抑制することが示唆された。

首都大学東京, 2017-03-25, 修士(健康科学)

Subjects/Keywords: caffeine; Ca^<; 2+>; -induced contraction; myosin-actin interaction; myosin light chain phosphorylation; カフェイン; Ca^<; 2+>; 活性化収縮; ミオシン-アクチン相互作用; ミオシン軽鎖リン酸化

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

王, . (2017). Caffeine inhibits smooth muscle actin-myosin interaction : カフェインは平滑筋ミオシンアクチン相互作用を抑制する. (Thesis). Tokyo Metropolitan University / 首都大学東京. Retrieved from http://hdl.handle.net/10748/00009635

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

王, 志丹. “Caffeine inhibits smooth muscle actin-myosin interaction : カフェインは平滑筋ミオシンアクチン相互作用を抑制する.” 2017. Thesis, Tokyo Metropolitan University / 首都大学東京. Accessed March 01, 2021. http://hdl.handle.net/10748/00009635.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

王, 志丹. “Caffeine inhibits smooth muscle actin-myosin interaction : カフェインは平滑筋ミオシンアクチン相互作用を抑制する.” 2017. Web. 01 Mar 2021.

Vancouver:

王 . Caffeine inhibits smooth muscle actin-myosin interaction : カフェインは平滑筋ミオシンアクチン相互作用を抑制する. [Internet] [Thesis]. Tokyo Metropolitan University / 首都大学東京; 2017. [cited 2021 Mar 01]. Available from: http://hdl.handle.net/10748/00009635.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

王 . Caffeine inhibits smooth muscle actin-myosin interaction : カフェインは平滑筋ミオシンアクチン相互作用を抑制する. [Thesis]. Tokyo Metropolitan University / 首都大学東京; 2017. Available from: http://hdl.handle.net/10748/00009635

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Guelph

3. Mishra, Vadika. Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure.

Degree: MS, Department of Molecular and Cellular Biology, 2015, University of Guelph

Researchers have been trying to determine the mechanism of the crossbridge cycle, containing actomyosin complex, formed by the interaction of F-actin and myosin. But, because actin forms polymers of varying lengths, it has been difficult to crystallize this complex. My research is aimed at developing a homogeneous actomyosin complex with a short actin oligomer that possesses one myosin-binding site. ADPr-oligomers are produced by chemical crosslinking of F-actin and inhibiting polymerization by ADP-ribosylation. Specifically, I determined the behavior of an ADPr-trimer and dimer with myosin and its effect on actomyosin activity. Individual myosin ATPase activities of ADPr-trimer/dimer were similar to basal myosin activity. However, in the presence of long ADPr-oligomers (tetramer, pentamer, etc.) or F-actin, ADPr-dimer/trimer show binding and activity with myosin thick filaments. Thus, I was unable to produce a short actomyosin complex through these efforts and present a model for interaction of short actin oligomers with each other in the presence of long actin filaments and myosin. Advisors/Committee Members: Dawson, John (advisor).

Subjects/Keywords: actin; myosin; interaction; actomyosin; F-actin

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Mishra, V. (2015). Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8714

Chicago Manual of Style (16th Edition):

Mishra, Vadika. “Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure.” 2015. Masters Thesis, University of Guelph. Accessed March 01, 2021. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8714.

MLA Handbook (7th Edition):

Mishra, Vadika. “Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure.” 2015. Web. 01 Mar 2021.

Vancouver:

Mishra V. Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure. [Internet] [Masters thesis]. University of Guelph; 2015. [cited 2021 Mar 01]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8714.

Council of Science Editors:

Mishra V. Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure. [Masters Thesis]. University of Guelph; 2015. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8714

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