The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms
Copyright © 2016 the American Physiological Society..
Skeletal muscles present a non-cross-bridge increase in sarcomere stiffness and tension on Ca(2+) activation, referred to as static stiffness and static tension, respectively. It has been hypothesized that this increase in tension is caused by Ca(2+)-dependent changes in the properties of titin molecules. To verify this hypothesis, we investigated the static tension in muscles containing different titin isoforms. Permeabilized myofibrils were isolated from the psoas, soleus, and heart ventricle from the rabbit, and tested in pCa 9.0 and pCa 4.5, before and after extraction of troponin C, thin filaments, and treatment with the actomyosin inhibitor blebbistatin. The myofibrils were tested with stretches of different amplitudes in sarcomere lengths varying between 1.93 and 3.37 μm for the psoas, 2.68 and 4.21 μm for the soleus, and 1.51 and 2.86 μm for the ventricle. Using gel electrophoresis, we confirmed that the three muscles tested have different titin isoforms. The static tension was present in psoas and soleus myofibrils, but not in ventricle myofibrils, and higher in psoas myofibrils than in soleus myofibrils. These results suggest that the increase in the static tension is directly associated with Ca(2+)-dependent change in titin properties and not associated with changes in titin-actin interactions.
Errataetall: |
CommentIn: Am J Physiol Cell Physiol. 2016 Jan 1;310(1):C17-8. - PMID 26538091 |
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Medienart: |
E-Artikel |
Erscheinungsjahr: |
2016 |
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Erschienen: |
2016 |
Enthalten in: |
Zur Gesamtaufnahme - volume:310 |
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Enthalten in: |
American journal of physiology. Cell physiology - 310(2016), 1 vom: 01. Jan., Seite C19-26 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Cornachione, Anabelle S [VerfasserIn] |
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Links: |
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Themen: |
Calcium |
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Anmerkungen: |
Date Completed 02.05.2016 Date Revised 30.09.2020 published: Print-Electronic CommentIn: Am J Physiol Cell Physiol. 2016 Jan 1;310(1):C17-8. - PMID 26538091 Citation Status MEDLINE |
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doi: |
10.1152/ajpcell.00156.2015 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM253086108 |
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500 | |a Citation Status MEDLINE | ||
520 | |a Copyright © 2016 the American Physiological Society. | ||
520 | |a Skeletal muscles present a non-cross-bridge increase in sarcomere stiffness and tension on Ca(2+) activation, referred to as static stiffness and static tension, respectively. It has been hypothesized that this increase in tension is caused by Ca(2+)-dependent changes in the properties of titin molecules. To verify this hypothesis, we investigated the static tension in muscles containing different titin isoforms. Permeabilized myofibrils were isolated from the psoas, soleus, and heart ventricle from the rabbit, and tested in pCa 9.0 and pCa 4.5, before and after extraction of troponin C, thin filaments, and treatment with the actomyosin inhibitor blebbistatin. The myofibrils were tested with stretches of different amplitudes in sarcomere lengths varying between 1.93 and 3.37 μm for the psoas, 2.68 and 4.21 μm for the soleus, and 1.51 and 2.86 μm for the ventricle. Using gel electrophoresis, we confirmed that the three muscles tested have different titin isoforms. The static tension was present in psoas and soleus myofibrils, but not in ventricle myofibrils, and higher in psoas myofibrils than in soleus myofibrils. These results suggest that the increase in the static tension is directly associated with Ca(2+)-dependent change in titin properties and not associated with changes in titin-actin interactions | ||
650 | 4 | |a Comparative Study | |
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
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700 | 1 | |a Rassier, Dilson E |e verfasserin |4 aut | |
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