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Journal article
α-Catenin Localization and Sarcomere Self-Organization on N-Cadherin Adhesive Patterns Are Myocyte Contractility Driven
PloS one, v 7(10), pp e47592-e47592
15 Oct 2012
PMID: 23077648
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The N-cadherin (N-cad) complex plays a crucial role in cardiac cell structure and function. Cadherins are adhesion proteins linking adjacent cardiac cells and, like integrin adhesions, are sensitive to force transmission. Forces through these adhesions are capable of eliciting structural and functional changes in myocytes. Compared to integrins, the mechanisms of force transduction through cadherins are less explored. α-catenin is a major component of the cadherin-catenin complex, thought to provide a link to the cell actin cytoskeleton. Using N-cad micropatterned substrates in an adhesion constrainment model, the results from this study show that α-catenin localizes to regions of highest internal stress in myocytes. This localization suggests that α-catenin acts as an adaptor protein associated with the cadherin mechanosensory apparatus, which is distinct from mechanosensing through integrins. Myosin inhibition in cells bound by integrins to fibronectin-coated patterns disrupts myofibiril organization, whereas on N-cad coated patterns, myosin inhibition leads to better organized myofibrils. This result indicates that the two adhesion systems provide independent mechanisms for regulating myocyte structural organization.
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Details
- Title
- α-Catenin Localization and Sarcomere Self-Organization on N-Cadherin Adhesive Patterns Are Myocyte Contractility Driven
- Creators
- Anant Chopra - Drexel UniversityAkash Patel - Drexel UniversityAdrian C. Shieh - Drexel UniversityPaul A. JanmeyJ. Yasha Kresh - Drexel University
- Publication Details
- PloS one, v 7(10), pp e47592-e47592
- Publisher
- Public Library of Science
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems; [Retired Faculty]
- Web of Science ID
- WOS:000309995100143
- Scopus ID
- 2-s2.0-84867542181
- Other Identifier
- 991019169669604721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Cell Biology