Different Obscurin Isoforms Localize to Distinct Sites at Sarcomeres.
From: Department of Physiology, University of Maryland School of Medicine, 655 W. Baltimore St, MD 21201, USA.
FEBS letters
- Publish Date: Apr 2007
- ISSN: 0014-5793
- Volume: 581
- Issue: 8
- Pages: 1549-54
- Medium: Print
- Language: English
- Citation (JAMA): Bowman Amber L, Kontrogianni-Konstantopoulos Aikaterini, Hirsch Sara S, et al. Different Obscurin Isoforms Localize to Distinct Sites at Sarcomeres.. FEBS Lett. Apr 2007;581:1549-54
Abstract
We used four antibodies to regions of obscurin isoforms A and B, encoded by the obscurin gene, to investigate the location of these proteins in skeletal myofibers at resting and stretched lengths. Obscurin A ( approximately 800 kDa) which was recognized by antibodies generated to the N-terminal, Rho-GEF, and the non-modular C-terminal domain that lacks the kinase-like domains, localizes at the level of the M-band. Obscurin B ( approximately 900 kDa) which has the N-terminal, Rho-GEF, and the C-terminal kinase-like domains, localizes at the level of the A/I junction. Additional isoforms, which lack one or more of these epitopes, are present at the Z-disk and Z/I junction.
Mesh Headings (Keywords): Animals, Muscle Proteins, Muscle, Skeletal, Protein Isoforms, Sarcomeres
Check for Full Text / PubMed Unique Identifier (PMID): 17382936
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.
