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Titolo:
An in vitro assay reveals essential protein components for the "catch" state of invertebrate smooth muscle
Autore:
Yamada, A; Yoshio, M; Kojima, H; Oiwa, K;
Indirizzi:
Kansai Adv Res Ctr, Commun Res Lab, Nishi Ku, Kobe, Hyogo 6512492, Japan Kansai Adv Res Ctr Kobe Hyogo Japan 6512492 u, Kobe, Hyogo 6512492, Japan
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 12, volume: 98, anno: 2001,
pagine: 6635 - 6640
SICI:
0027-8424(20010605)98:12<6635:AIVARE>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
REGULATORY LIGHT-CHAINS; ROD PHOSPHORYLATION; MOLLUSCAN MUSCLES; SINGLE-MOLECULE; MINI-TITINS; MYOSIN; FILAMENTS; TWITCHIN; CALCIUM; KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Yamada, A Kansai Adv Res Ctr, Commun Res Lab, Nishi Ku, Iwaoka 588-2, Kobe, Hyogo 6512492, Japan Kansai Adv Res Ctr Iwaoka 588-2 Kobe Hyogo Japan 6512492 , Japan
Citazione:
A. Yamada et al., "An in vitro assay reveals essential protein components for the "catch" state of invertebrate smooth muscle", P NAS US, 98(12), 2001, pp. 6635-6640

Abstract

"Catch," a state where some invertebrate muscles sustain high tension overlong periods of time with little energy expenditure (low ATP hydrolysis rate) is similar to the "latch" state of vertebrate smooth muscles. Its induction and release involve Ca2+-dependent phosphatase and cAMP-dependent protein kinase, respectively. Molecular mechanisms for catch remain obscure. Here, we describe a quantitative microscopic in vitro assay reconstituting the catch state with proteins isolated from catch muscles. Thick filaments attached to glass coverslips and pretreated with approximate to 10(-4) M freeCa2+ and soluble muscle proteins bound fluorescently labeled native thin filaments tightly in catch at approximate to 10(-8) M free Ca2+ in the presence of MgATP. At approximate to 10(-4) M free Ca2+, the thin filaments moved at approximate to4 mum/s. Addition of cAMP and cAMP-dependent protein kinase at approximate to 10(-8) M free Ca2+ caused their release. Rabbit skeletal muscle F-actin filaments completely reproduced the results obtained with native thin filaments, Binding forces > 500 pN/mum between thick and F-actin filaments were measured by glass microneedles, and were sufficient to explain catch tension in vivo. Synthetic filaments of purified myosin and twitchin bound F-actin in catch, showing that other components of native thick filaments such as paramyosin and catchin are not essential, The binding between synthetic thick filaments and F-actin filaments depended on phosphorylation of twitchin but not of myosin, Cosedimentation experiments showed that twitchin did not bind directly to F-actin in catch. These results show that catch is a direct actomyosin interaction regulated by twitchin phosphorylation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 18:04:41