Troponin I: Inhibitor or facilitator

Perry, S. V.

doi:10.1007/978-1-4615-5543-8_2

Cited by 66 publications

(112 citation statements)

References 142 publications

Supporting

Mentioning

107

Contrasting

Unclassified

Order By: Relevance

“…There are pronounced functional differences between fiber types with greater shortening velocity and increased maximal power output in fast-twitch relative to slow-twitch fibers (1,15). Although many functional differences between fiber types have been ascribed to myosin composition (1,15), variation in the composition of thin-filament proteins, such as troponin C, I, and T isoforms (20,22,23), could also contribute. This point is particularly relevant to our results since our laboratory (31) and others (36) have shown alterations in fiber-type distribution in CHF, with a shift toward a more fast-twitch phenotype.…”

Section: Discussionmentioning

confidence: 99%

Skeletal muscle contractile protein function is preserved in human heart failure

Okada

Toth²,

VanBuren³

2008

Journal of Applied Physiology

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Skeletal muscle contractile protein function is preserved in human heart failure

Okada

Toth²,

VanBuren³

2008

Journal of Applied Physiology

View full text Add to dashboard Cite

show abstract

“…The three components of troponin, troponin I, C, and T, work together to regulate actomyosin activity (Farah and Reinach, 1995;Perry, 1999Perry, , 2003. Troponin I binding to the actin/ tropomyosin chains results in the site on the actin with which the myosin heads interact becoming blocked.…”

Section: Regulation Of Cross-bridge Cyclingmentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

128

View full text Add to dashboard Cite

This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

show abstract

“…In the absence of Ca 2+ , TnC interacts weakly with TnI (K app = ∼10 6 M −1 ), which binds to actin through its inhibitory and actinbinding sites (residues 96-116 in fast skeletal TnI (FTnI) or 128-148 in cardiac TnI (CTnI) and 140-148 in FTnI and 172-180 in CTnI (Fig. 3) [reviewed in (38)]. This inhibitory function of TnI, as well as the regions of TnI that are responsible for inhibition, have been extensively studied in many laboratories [reviewed in (3,(39)(40)(41)].…”

Section: Troponin Imentioning

confidence: 99%

The Role of Troponins in Muscle Contraction

2002

View full text Add to dashboard Cite

SummaryTroponin (Tn) is the sarcomeric Ca 2+ regulator for striated (skeletal and cardiac) muscle contraction. On binding Ca 2+ Tn transmits information via structural changes throughout the actintropomyosin filaments, activating myosin ATPase activity and muscle contraction. Although the Tn-mediated regulation of striated muscle contraction is now well understood, the role of different Tn isoforms in these processes is the subject of intensive investigations. This review addresses the physiological significance of the multiple Tn isoforms in skeletal and cardiac muscles as well as their role in the regulation of contraction.

show abstract

Troponin I: Inhibitor or facilitator

Cited by 66 publications

References 142 publications

Skeletal muscle contractile protein function is preserved in human heart failure

Skeletal muscle contractile protein function is preserved in human heart failure

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

The Role of Troponins in Muscle Contraction

Contact Info

Product

Resources

About