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Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality

Academic Article
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Overview

authors

  • Fritz-Six, K. L.
  • Cox, P. R.
  • Fischer, R. S.
  • Xu, B. S.
  • Gregorio, C. C.
  • Zoghbi, H. Y.
  • Fowler, Velia

publication date

  • December 2003

journal

  • Journal of Cell Biology  Journal

abstract

  • Tropomodulin1 (Tmod1) caps thin filament pointed ends in striated muscle, where it controls filament lengths by regulating actin dynamics. Here, we investigated myofibril assembly and heart development in a Tmod1 knockout mouse. In the absence of Tmod1, embryonic development appeared normal up to embryonic day (E) 8.5. By E9.5, heart defects were evident, including aborted development of the myocardium and inability to pump, leading to embryonic lethality by E10.5. Confocal microscopy of hearts of E8-8.5 Tmod1 null embryos revealed structures resembling nascent myofibrils with continuous F-actin staining and periodic dots of alpha-actinin, indicating that I-Z-I complexes assembled in the absence of Tmod1. Myomesin, a thick filament component, was also assembled normally along these structures, indicating that thick filament assembly is independent of Tmod1. However, myofibrils did not become striated, and gaps in F-actin staining (H zones) were never observed. We conclude that Tmod1 is required for regulation of actin filament lengths and myofibril maturation; this is critical for heart morphogenesis during embryonic development.

subject areas

  • Actinin
  • Animals
  • Carrier Proteins
  • Connectin
  • Embryo Loss
  • Embryonic and Fetal Development
  • Gene Targeting
  • Genotype
  • Gestational Age
  • Heart
  • Humans
  • Mice
  • Mice, Knockout
  • Microfilament Proteins
  • Muscle Proteins
  • Myocardial Contraction
  • Myocardium
  • Myofibrils
  • Peptides, Cyclic
  • Tropomodulin
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Research

keywords

  • actin
  • cardiac muscle
  • sarcomere
  • tropomodulin
  • tropomyosin
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Identity

PubMed Central ID

  • PMC2173615

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200308164

PubMed ID

  • 14657235
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Additional Document Info

start page

  • 1033

end page

  • 1044

volume

  • 163

issue

  • 5

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