Differential half‐life of major titin isoforms in normal and remodeling mouse hearts
Alternative splicing is an important regulatory layer in gene expression, but knowledge on the isoform protein molecules continue to lag their canonical counterparts. An open question is whether alternative protein isoforms feature different half-life than the canonical counterpart, which could indicate differential usage and functional diversification. Here we combined a proteogenomics approach with heavy water-based protein turnover analysis to survey 24 pairs of canonical-alternative protein isoforms in the mouse heart. The results provide a reference on their numerical half-life and also reveal widespread differences in isoform stability.
Authors
- Maggie P. Y. Lam (ORCID: https://orcid.org/0000-0001-9488-8319)
- Shaonil Binti (ORCID: https://orcid.org/0000-0002-2904-933X)
- Matthew C. Juber (ORCID: https://orcid.org/0000-0002-8757-7763)
- Boomathi Pandi (ORCID: https://orcid.org/0009-0003-5026-9788)
- Thalia Paiz (ORCID: https://orcid.org/0009-0006-2158-4641)
Institutions
- University of Colorado Anschutz Medical Campus (US)
- University of Colorado Denver (US)
Publication Details
- Journal
- Journal of the American Heart Association
- Published
- 2026-11-06
- DOI
- https://doi.org/10.1161/jaha.126.054215
- Primary Topic
- Advanced Proteomics Techniques and Applications
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science Foundation
- Colorado State University
- National Institutes of Health
- University of Colorado Boulder
- National Heart, Lung, and Blood Institute
- National Institute of General Medical Sciences