Home LiteratureArticle Details
PMID: 3801566 Published · ppublish English Journal Article

Intensity increases of actin layer-lines on activation of the Limulus muscle.

Biophysical journal ·Vol. 50 ·No. 6 ·1986-12-00 ·Pages 1035-42

Maéda Y, Boulin C, Gabriel A, Sumner I, Koch MH

Abstract

Small angle x-ray diffraction patterns were recorded from isometrically contracting Limulus (horseshoe crab) telson levator muscle using a multiwire proportional-area detector on the storage ring DORIS. In the pattern a substantial increase in intensity is observed on the thin-filament-associated layer-line at 1/38 nm-1 (the first actin layer-line) with a maximum increase at a radial spacing of R = 0.07 nm-1 but there is a much smaller change in the intensity of the 5.9-nm layer-line, which also arises from the thin filament structure. The results suggest that during contraction the myosin heads, presumably being attached to the thin filaments, are arranged along the long-stranded helical tracks of the thin filaments but that the spatial relationship between the heads and the actin monomers varies. Intensity increases have also been observed (Maéda et al., manuscript in preparation) in the part of the patterns from frog muscle and barnacle muscle, which are attributable to the first actin layer-line. It is thus likely that the intensity increase of the first actin layer-line on the Limulus pattern is associated not with structural features which are special to Limulus muscle, but with the tension generating processes that are shared by muscles in general.

MeSH Terms
Actin Cytoskeleton/ultrastructure Actins/physiology Animals Horseshoe Crabs Muscle Contraction Muscles/physiology,ultrastructure X-Ray Diffraction
Chemicals
Actins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Maéda Y
Boulin C
Gabriel A
Sumner I
Koch M H
References (9)
9 references, click to expand
  1. Actomyosin structure in contracting muscle detected by rapid freezing.
    Nature. 1985 Sep 12-18;317(6033):182-4 PMID: 4033798
  2. Time-resolved X-ray diffraction studies of the myosin layer-line reflections during muscle contraction.
    J Mol Biol. 1982 Jul 15;158(4):637-84 PMID: 6981706
  3. F-actin is a helix with a random variable twist.
    Nature. 1982 Jul 8;298(5870):131-5 PMID: 7201078
  4. Changes of thick filament structure during contraction of frog striated muscle.
    Biophys J. 1981 Jan;33(1):121-37 PMID: 6974013
  5. The use of synchrotron radiation in time-resolved X-ray diffraction studies of myosin layer-line reflections during muscle contraction.
    Nature. 1980 Mar 13;284(5752):140-3 PMID: 7189013
  6. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.
    J Mol Biol. 1967 Dec 14;30(2):383-434 PMID: 5586931
  7. Cross-bridge arrangements in Limulus muscle.
    J Mol Biol. 1974 Sep 15;88(2):343-8 PMID: 4452999
  8. Actin filaments in muscle: pattern of myosin and tropomyosin/troponin attachments.
    J Mol Biol. 1978 Sep 25;124(3):501-21 PMID: 712845
  9. X-ray structure analysis of the thin filament of crab striated muscle in the rigor state.
    J Mol Biol. 1980 Mar 25;138(1):1-26 PMID: 7411602
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1986-12-00
Pages
1035-42
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1329777
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com