Extraction of proteins other than myosin from the isolated rabbit myofibril

Perry, S. V.; Corsi, Annamaria

doi:10.1042/bj0680005

Cited by 136 publications

(23 citation statements)

References 15 publications

(10 reference statements)

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“…Therefore, it can be assumed that actin, myosin and/or tropomyosin must occur in appreciable quantities in the Z bands. However, the obvious correlation that every tropomyosin extraction procedure has been reported to remove or severely disturb the Z bands (5,6,12,29,36) has not been emphasizecl, yet these data are consistent regardless of the other proteins extracted, whether actin, myosin or both.…”

Section: Interpretationssupporting

confidence: 56%

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Urea extraction of Z bands, intercalated disks, and desmosomes

Rash

Shay

Biesele

1968

Journal of Ultrastructure Research

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Section: Interpretationssupporting

confidence: 56%

“…For comparison with published results of others, we have completed additional extractions after brief or prolonged storage in 50% glycerol (6,11,29), noting however, several possible sources of error introduced by this procedure (4,8).…”

Section: Methodsmentioning

confidence: 99%

Urea extraction of Z bands, intercalated disks, and desmosomes

Rash

Shay

Biesele

1968

Journal of Ultrastructure Research

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“…The proteasome inhibitors MG101 (N-acetyl-Leu-Leunorleucinal) and MG132 (Cbz-Leu-Leu-leucinal) were kindly provided by ProScript, Inc. (formerly MyoGenics, Inc., Cambridge, MA). Myofibrils were isolated in bulk from fresh rabbit psoas muscles and purified as described previously (31). Myosin, actin, and troponin were labeled with 125 I using the chloramine-T procedure (32), and myoglobin was labeled with [ 14 C]formaldehyde (33).…”

Section: Methodsmentioning

confidence: 99%

Importance of the ATP-Ubiquitin-Proteasome Pathway in the Degradation of Soluble and Myofibrillar Proteins in Rabbit Muscle Extracts

Solomon

Goldberg

1996

Journal of Biological Chemistry

361

288

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Recent studies have suggested that activation of the ubiquitin-proteasome pathway is primarily responsible for the rapid loss of muscle proteins in various types of atrophy. The present studies were undertaken to test if different classes of muscle proteins are degraded by this pathway. In extracts of rabbit psoas muscle, the complete degradation of soluble proteins to amino acids was stimulated up to 6-fold by ATP. Peptide aldehyde inhibitors of the proteasome or the removal of proteasomes markedly inhibited only the ATP-dependent process. Addition of purified myosin, actin, troponin, or tropomyosin to these extracts showed that these proteins served as substrates for the ubiquitin-proteasome pathway. By contrast, degradation of myoglobin did not require ATP, proteasomes, or any known proteases in muscles.When myosin, actin, and troponin were added as actomyosin complexes or as intact myofibrils to these extracts, they were not hydrolyzed at a significant rate, probably because in these multicomponent complexes, these proteins are protected from degradation. Accordingly, actin (but not albumin or troponin) inhibited the degradation of 125 I-myosin, and actin was found to selectively inhibit ubiquitin conjugation to 125 I-myosin. Also, the presence of tropomyosin inhibited the degradation of 125 I-troponin. However, neither actin nor tropomyosin inhibited the degradation of 125 I-lysozyme or soluble muscle proteins. Thus, specific interactions between the myofibrillar proteins appear to protect them from ubiquitin-dependent degradation, and the ratelimiting step in their degradation is probably their dissociation from the myofibril.

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“…The main constituent of the thin filament is actin (Huxley and Hanson 1954;Perry and Corsi 1958;Ebashi et al 1969). The actomyosin complex was originally budded Bmyosin B^in 1941 by Szent-Györgyi (1942) to distinguish it from the myosin (called myosin A) based on their different solubility and viscosity properties.…”

Section: Actin the Major Component Of Thin Filamentsmentioning

confidence: 99%

Historical perspective on heart function: the Frank–Starling Law

Sequeira

Velden

2015

Biophys Rev

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More than a century of research on the FrankStarling Law has significantly advanced our knowledge about the working heart. The Frank-Starling Law mandates that the heart is able to match cardiac ejection to the dynamic changes occurring in ventricular filling and thereby regulates ventricular contraction and ejection. Significant efforts have been attempted to identify a common fundamental basis for the Frank-Starling heart and, although a unifying idea has still to come forth, there is mounting evidence of a direct relationship between length changes in individual constituents (cardiomyocytes) and their sensitivity to Ca 2+ ions. As the Frank-Starling Law is a vital event for the healthy heart, it is of utmost importance to understand its mechanical basis in order to optimize and organize therapeutic strategies to rescue the failing human heart. The present review is a historic perspective on cardiac muscle function. We Brevive^a century of scientific research on the heart's fundamental protein constituents (contractile proteins), to their assemblies in the muscle (the sarcomeres), culminating in a thorough overview of the several synergistically events that compose the Frank-Starling mechanism. It is the authors' personal beliefs that much can be gained by understanding the Frank-Starling relationship at the cellular and whole organ level, so that we can finally, in this century, tackle the pathophysiologic mechanisms underlying heart failure.

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Extraction of proteins other than myosin from the isolated rabbit myofibril

Cited by 136 publications

References 15 publications

Urea extraction of Z bands, intercalated disks, and desmosomes

Urea extraction of Z bands, intercalated disks, and desmosomes

Importance of the ATP-Ubiquitin-Proteasome Pathway in the Degradation of Soluble and Myofibrillar Proteins in Rabbit Muscle Extracts

Historical perspective on heart function: the Frank–Starling Law

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