A non-cross-bridge, static tension is present in permeabilized skeletal muscle fibers after active force inhibition or actin extraction
When activated muscle fibers are stretched, there is a long-lasting increase in the force. This phenomenon, referred to as "residual force enhancement," has characteristics similar to those of the "static tension," a long-lasting increase in force observed when muscles are stretched in the presence of Ca(2+) but in the absence of myosin-actin interaction. Independent studies have suggested that these two phenomena have a common mechanism and are caused either by 1) a Ca(2+)-induced stiffening of titin or by 2) promoting titin binding to actin. In this study, we performed two sets of experiments in which activated fibers (pCa(2+) 4.5) treated with the myosin inhibitor blebbistatin were stretched from 2.7 to 2.8 μm at a speed of 40 L(o)/s, first, after partial extraction of TnC, which inhibits myosin-actin interactions, or, second, after treatment with gelsolin, which leads to the depletion of thin (actin) filaments. We observed that the static tension, directly related with the residual force enhancement, was not changed after treatments that inhibit myosin-actin interactions or that deplete fibers from troponin C and actin filaments. The results suggest that the residual force enhancement is caused by a stiffening of titin upon muscle activation but not with titin binding to actin. This finding indicates the existence of a Ca(2+)-regulated, titin-based stiffness in skeletal muscles.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2012 |
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| Erschienen: |
2012 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:302 |
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| Enthalten in: |
American journal of physiology. Cell physiology - 302(2012), 3 vom: 01. Feb., Seite C566-74 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Cornachione, Anabelle S [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 25.03.2012 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1152/ajpcell.00355.2011 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM213143542 |
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| 100 | 1 | |a Cornachione, Anabelle S |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A non-cross-bridge, static tension is present in permeabilized skeletal muscle fibers after active force inhibition or actin extraction |
| 264 | 1 | |c 2012 | |
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| 500 | |a Date Revised 30.09.2020 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a When activated muscle fibers are stretched, there is a long-lasting increase in the force. This phenomenon, referred to as "residual force enhancement," has characteristics similar to those of the "static tension," a long-lasting increase in force observed when muscles are stretched in the presence of Ca(2+) but in the absence of myosin-actin interaction. Independent studies have suggested that these two phenomena have a common mechanism and are caused either by 1) a Ca(2+)-induced stiffening of titin or by 2) promoting titin binding to actin. In this study, we performed two sets of experiments in which activated fibers (pCa(2+) 4.5) treated with the myosin inhibitor blebbistatin were stretched from 2.7 to 2.8 μm at a speed of 40 L(o)/s, first, after partial extraction of TnC, which inhibits myosin-actin interactions, or, second, after treatment with gelsolin, which leads to the depletion of thin (actin) filaments. We observed that the static tension, directly related with the residual force enhancement, was not changed after treatments that inhibit myosin-actin interactions or that deplete fibers from troponin C and actin filaments. The results suggest that the residual force enhancement is caused by a stiffening of titin upon muscle activation but not with titin binding to actin. This finding indicates the existence of a Ca(2+)-regulated, titin-based stiffness in skeletal muscles | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Actins |2 NLM | |
| 650 | 7 | |a Connectin |2 NLM | |
| 650 | 7 | |a Gelsolin |2 NLM | |
| 650 | 7 | |a Heterocyclic Compounds, 4 or More Rings |2 NLM | |
| 650 | 7 | |a Muscle Proteins |2 NLM | |
| 650 | 7 | |a Troponin C |2 NLM | |
| 650 | 7 | |a blebbistatin |2 NLM | |
| 650 | 7 | |a 20WC4J7CQ6 |2 NLM | |
| 650 | 7 | |a Protein Kinases |2 NLM | |
| 650 | 7 | |a EC 2.7.- |2 NLM | |
| 650 | 7 | |a Myosins |2 NLM | |
| 650 | 7 | |a EC 3.6.4.1 |2 NLM | |
| 650 | 7 | |a Calcium |2 NLM | |
| 650 | 7 | |a SY7Q814VUP |2 NLM | |
| 700 | 1 | |a Rassier, Dilson E |e verfasserin |4 aut | |
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