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Reactivities of Actin as a Contractile Protein

The molecular basis for the mechanism of contraction in striated muscle, with primary emphasis on the interaction between the thick and thin filaments and the role of the thin (actin) filaments, is the theme presented. Recent information relating to actin-myosin interaction points up the fact that d...

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Detalles Bibliográficos
Autor principal: Hayashi, Teru
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1967
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225744/
https://www.ncbi.nlm.nih.gov/pubmed/6050593
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author Hayashi, Teru
author_facet Hayashi, Teru
author_sort Hayashi, Teru
collection PubMed
description The molecular basis for the mechanism of contraction in striated muscle, with primary emphasis on the interaction between the thick and thin filaments and the role of the thin (actin) filaments, is the theme presented. Recent information relating to actin-myosin interaction points up the fact that definitive statements cannot be made regarding the molecular interaction(s) that lead to contraction. Nevertheless, the properties of actin indicate that (a) actin in the monomeric state has properties differing markedly from actin in the polymer (filament) state; (b) these property differences may be significant in the contractile process, for they include changes in the reactivity of the bound nucleotide and actin-myosin complex formation; (c) the bound nucleotide seems to be required in the contraction process. For these, and other, reasons discussed, the tentative hypothesis is advanced that the contraction reaction involves local changes in the actin filament providing local monomer or monomer-like actin units in the reaction with myosin.
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spelling pubmed-22257442008-04-23 Reactivities of Actin as a Contractile Protein Hayashi, Teru J Gen Physiol Contractile Processes in Striated Muscle The molecular basis for the mechanism of contraction in striated muscle, with primary emphasis on the interaction between the thick and thin filaments and the role of the thin (actin) filaments, is the theme presented. Recent information relating to actin-myosin interaction points up the fact that definitive statements cannot be made regarding the molecular interaction(s) that lead to contraction. Nevertheless, the properties of actin indicate that (a) actin in the monomeric state has properties differing markedly from actin in the polymer (filament) state; (b) these property differences may be significant in the contractile process, for they include changes in the reactivity of the bound nucleotide and actin-myosin complex formation; (c) the bound nucleotide seems to be required in the contraction process. For these, and other, reasons discussed, the tentative hypothesis is advanced that the contraction reaction involves local changes in the actin filament providing local monomer or monomer-like actin units in the reaction with myosin. The Rockefeller University Press 1967-07-01 /pmc/articles/PMC2225744/ /pubmed/6050593 Text en Copyright © 1967 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Contractile Processes in Striated Muscle
Hayashi, Teru
Reactivities of Actin as a Contractile Protein
title Reactivities of Actin as a Contractile Protein
title_full Reactivities of Actin as a Contractile Protein
title_fullStr Reactivities of Actin as a Contractile Protein
title_full_unstemmed Reactivities of Actin as a Contractile Protein
title_short Reactivities of Actin as a Contractile Protein
title_sort reactivities of actin as a contractile protein
topic Contractile Processes in Striated Muscle
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225744/
https://www.ncbi.nlm.nih.gov/pubmed/6050593
work_keys_str_mv AT hayashiteru reactivitiesofactinasacontractileprotein