Journal article
Myofibrillar protein structure and assembly during idiopathic dilated cardiomyopathy
Molecular and cellular biochemistry, v 195(1-2), pp 1-10
01 May 1999
PMID: 10395063
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
A neutral protease, mekratin, active in human hearts at end stage idiopathic dilated cardiomyopathy (IDC), mediates the breakdown of cardiac myosin LC2. Myosin purified from IDC heart tissue forms unusually short synthetic thick filaments. Therefore, determination of filament length and mekratin distribution in IDC heart muscle were initiated. Native thick filaments were prepared directly from control and IDC tissues and analyzed. Also, paraffin-embedded tissue sections were stained with a fluorescently-labeled anti-protease antibody to establish its distribution in myocardial tissues. Control sections had only very weak, background levels of fluorescence whereas IDC sections stained intensely throughout, indicating a wide ranging distribution of the protease within the myocyte cytoplasm. SDS-PAGE revealed LC2 to be present in stoichiometric amounts in control but greatly reduced in IDC heart muscle. Native thick filaments from control myocardium were structurally stable. They had a median length of 1.65 mu m with well-defined bare zones and displayed the 43 nm helical periodicity typical of the relaxed arrangement of myosin heads close to the filaments' shafts. In contrast, native IDC filaments were less stable, and had a median length of 0.9 mu m. These filaments were highly disordered: they had no surface periodicity and myosin heads were positioned away from the filaments' shafts. The shorter, less stable, aperiodic thick filaments from IDC hearts appear to result from depletion of LC2 caused by increased activity of mekratin in the IDC myocardium.
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Details
- Title
- Myofibrillar protein structure and assembly during idiopathic dilated cardiomyopathy
- Creators
- RJC LevineJ B Caulfield - University of Alabama at BirminghamP Norton - University of Alabama at BirminghamP D Chantler - Royal Veterinary CollegeM R Deziel - Albany Medical Center HospitalH S Slayter - Dana-Farber Cancer InstituteS S Margossian - Albany Medical Center Hospital
- Publication Details
- Molecular and cellular biochemistry, v 195(1-2), pp 1-10
- Publisher
- Springer Nature
- Number of pages
- 10
- Grant note
- HL49597 / NHLBI NIH HHS; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI) Wellcome Trust; European Commission R01HL049597 / NATIONAL HEART, LUNG, AND BLOOD INSTITUTE; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000080709900001
- Scopus ID
- 2-s2.0-0033016061
- Other Identifier
- 991019167794804721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Cell Biology