Titin/connectin-based modulation of the Frank-Starling mechanism of the heart
Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $])....
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Fukuda, Norio [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2005 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media, Inc. 2006 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of muscle research and cell motility - Kluwer Academic Publishers, 1980, 26(2005), 6-8 vom: Dez., Seite 319-323 |
|---|---|
| Übergeordnetes Werk: |
volume:26 ; year:2005 ; number:6-8 ; month:12 ; pages:319-323 |
| Links: |
|---|
| DOI / URN: |
10.1007/s10974-005-9038-1 |
|---|
| Katalog-ID: |
OLC2067126938 |
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| 520 | |a Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. | ||
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10.1007/s10974-005-9038-1 doi (DE-627)OLC2067126938 (DE-He213)s10974-005-9038-1-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Fukuda, Norio verfasserin aut Titin/connectin-based modulation of the Frank-Starling mechanism of the heart 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, Inc. 2006 Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. Lattice Spacing Muscle Length Sarcomere Length Passive Force Length Dependence Granzier, Henk L. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 26(2005), 6-8 vom: Dez., Seite 319-323 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:26 year:2005 number:6-8 month:12 pages:319-323 https://doi.org/10.1007/s10974-005-9038-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2007 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 26 2005 6-8 12 319-323 |
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10.1007/s10974-005-9038-1 doi (DE-627)OLC2067126938 (DE-He213)s10974-005-9038-1-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Fukuda, Norio verfasserin aut Titin/connectin-based modulation of the Frank-Starling mechanism of the heart 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, Inc. 2006 Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. Lattice Spacing Muscle Length Sarcomere Length Passive Force Length Dependence Granzier, Henk L. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 26(2005), 6-8 vom: Dez., Seite 319-323 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:26 year:2005 number:6-8 month:12 pages:319-323 https://doi.org/10.1007/s10974-005-9038-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2007 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 26 2005 6-8 12 319-323 |
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10.1007/s10974-005-9038-1 doi (DE-627)OLC2067126938 (DE-He213)s10974-005-9038-1-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Fukuda, Norio verfasserin aut Titin/connectin-based modulation of the Frank-Starling mechanism of the heart 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, Inc. 2006 Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. Lattice Spacing Muscle Length Sarcomere Length Passive Force Length Dependence Granzier, Henk L. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 26(2005), 6-8 vom: Dez., Seite 319-323 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:26 year:2005 number:6-8 month:12 pages:319-323 https://doi.org/10.1007/s10974-005-9038-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2007 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 26 2005 6-8 12 319-323 |
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10.1007/s10974-005-9038-1 doi (DE-627)OLC2067126938 (DE-He213)s10974-005-9038-1-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Fukuda, Norio verfasserin aut Titin/connectin-based modulation of the Frank-Starling mechanism of the heart 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, Inc. 2006 Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. Lattice Spacing Muscle Length Sarcomere Length Passive Force Length Dependence Granzier, Henk L. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 26(2005), 6-8 vom: Dez., Seite 319-323 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:26 year:2005 number:6-8 month:12 pages:319-323 https://doi.org/10.1007/s10974-005-9038-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2007 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 26 2005 6-8 12 319-323 |
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Fukuda, Norio Granzier, Henk L. |
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Fukuda, Norio |
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590 570 |
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titin/connectin-based modulation of the frank-starling mechanism of the heart |
| title_auth |
Titin/connectin-based modulation of the Frank-Starling mechanism of the heart |
| abstract |
Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. © Springer Science+Business Media, Inc. 2006 |
| abstractGer |
Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. © Springer Science+Business Media, Inc. 2006 |
| abstract_unstemmed |
Abstract The basis of the Frank-Starling mechanism of the heart is the increase in active force when muscle is stretched. Various findings have shown that muscle length, i.e., sarcomere length (SL), modulates activation of cardiac myofilaments at a given concentration of $ Ca^{2+} $ ([$ Ca^{2+} $]). This augmented $ Ca^{2+} $ activation with SL, commonly known as “length-dependent activation”, is manifested as the leftward shift of the force-pCa (=−log [$ Ca^{2+} $]) relation as well as by the increase in maximal $ Ca^{2+} $-activated force. Despite the numerous studies that have been undertaken, the molecular mechanism(s) of length-dependent activation is (are) still not fully understood. The giant sarcomere protein titin/connectin is the largest protein known to date. Titin/connectin is responsible for most passive force in vertebrate striated muscle and also functions as a molecular scaffold during myofibrillogenesis. Recent studies suggest that titin/connectin plays an important role in length-dependent activation by sensing stretch and promoting actomyosin interaction. Here we review and extend this previous work and focus on the mechanism by which titin/connectin might modulate actomyosin interaction. © Springer Science+Business Media, Inc. 2006 |
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Titin/connectin-based modulation of the Frank-Starling mechanism of the heart |
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