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Related Experiment Videos

Titin isoform changes in rat myocardium during development.

Chad M Warren1, Paul R Krzesinski, Kenneth S Campbell

  • 1Muscle Biology Laboratory, 1805 Linden Drive West, University of Wisconsin-Madison, Madison, WI 53706, USA.

Mechanisms of Development
|September 30, 2004
PubMed
Summary

Titin protein isoforms change significantly during rat heart development, with fetal forms replaced by adult versions. This developmental switch in titin splicing correlates with changes in cardiac muscle passive tension.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiovascular Physiology

Background:

  • Titin is a large protein crucial for muscle elasticity and cardiac function.
  • Alternative splicing of titin generates diverse isoforms with distinct mechanical properties.
  • Understanding titin's developmental regulation is key to comprehending cardiac maturation.

Purpose of the Study:

  • To investigate developmental changes in titin alternative splicing in rat cardiac muscle.
  • To correlate titin isoform switching with functional changes in cardiac passive tension.
  • To characterize the molecular basis of titin isoform diversity during development.

Main Methods:

  • SDS-agarose gel electrophoresis to analyze titin protein isoforms.
  • cDNA sequencing to examine titin gene expression and alternative splicing.

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  • Passive tension measurements on isolated cardiac myocyte-sized fragments.

    • Main Results:

    • Fetal titin (3710 kDa) was replaced by adult N2B isoform (2990 kDa) after birth.
    • The N2B isoform constituted ~85% of ventricular titin in adults.
    • Alternative splicing in PEVK and Ig domains contributed to fetal titin's larger size and heterogeneity.
    • Neonatal ventricles exhibited lower passive tension than adult ventricles.

    Conclusions:

    • Significant developmental shifts in titin splicing occur in rat cardiac muscle.
    • These splicing changes result in distinct titin isoforms with altered mechanical properties.
    • The observed titin isoform switching parallels developmental changes in other cardiac proteins and impacts cardiac function.