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  • 1
    Electronic Resource
    Electronic Resource
    Calcium regulation in the human myocardium affected by dilated cardiomyopathy: A structural basis for impaired Ca2+-sensitivity (1999)
    Springer
    Molecular and cellular biochemistry 194 (1999), S. 301-313 
    Details
    ISSN: 1573-4919
    Keywords: ATPase activity ; cardiomyopathy ; heart failure ; myosin light chains ; troponin-tropomyosin ; mekratin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Calcium regulation in the human heart is impaired during idiopathic dilated cardiomyopathy (IDC). Here, we analyze the structural basis for impairment in the regulatory mechanism. Regulation of contractility was monitored by MgATPase and Ca2+-binding assays as a function of calcium. Myofibrillar proteolysis and expression of troponin T isoforms were established by gel electrophoresis and by Western blots. Myofibrillar ATPase assays in low salt however, revealed a drastic lowering of calcium sensitivity in IDC myofibrils as indicated by reductions in both activation by high calcium and in EGTA-mediated inhibition of MgATPase. Structural changes in myofilament proteins were found in most IDC hearts, specifically proteolysis of myosin light chain 2 (LC2), troponin T and I (TnT and TnI), and sometimes large isoform shift in TnT. IDC did not induce mutations in LC2 and troponin C (TnC), as established by cDNA sequence data from IDC cases, thus, calcium binding to IDC myofibrils was unaffected. Reassociation of IDC myofibrils with native LC2 raised MgATPase activation at high Ca2+ to control levels, while repletion with intact, canine TnI/TnT restored inhibition at low Ca2+. A model, identifying possible steps in the steric blocking mechanism of regulation, is proposed to explain IDC-induced changes in Ca2+-regulation. Moreover, shifts in TnT isoforms may imply either a genetic or a compensatory factor in the development and pathogenesis of some forms of IDC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006980405359
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  • 2
    Electronic Resource
    Electronic Resource
    Myofibrillar protein structure and assembly during idiopathic dilated cardiomyopathy (1999)
    Springer
    Molecular and cellular biochemistry 195 (1999), S. 1-10 
    Details
    ISSN: 1573-4919
    Keywords: myosin light chains ; native thick filaments ; dilated cardiomyopathy ; heart failure ; immunohistochemistry ; mekratin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: 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 μm 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 μm. 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006940513097
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning of the cDNA and nucleotide sequence of a skeletal muscle protease from myopathic hamsters (1998)
    Springer
    Molecular and cellular biochemistry 181 (1998), S. 125-135 
    Details
    ISSN: 1573-4919
    Keywords: cardiomyopathy ; serine proteases ; myosin light chain 2 ; cDNA cloning ; mast cells ; mekratin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract A neutral protease with an estimated Mr of about 26 kD and responsible for cleavage of myosin LC2 was isolated from hamster skeletal muscle. Complementary DNAs were generated by RT-PCR using total hamster muscle RNA and degenerate oligonucleotide primers based on the sequences of two internal peptides. The nucleotide sequences of the resultant cDNAs were subsequently determined and the complete amino acid sequence of the protease deduced. Although the hamster protein shared 63-85% identity in nucleotide and amino acid sequences with rat and mouse mast cell proteases, it had a higher degree of specificity for myosin LC2 than mast cell proteases which also digested myosin LC1 and myosin heavy chains. As a result, the hamster protease was designated mekratin because of its unique enzymatic specificities to distinguish it from other mast cell proteases. A polyclonal antibody was raised specific to the hamster muscle and human cardiac muscle mekratins without apparent cross-reaction with rat mast cell proteases. We have earlier demonstrated the presence in excess of a neutral protease that specifically cleaves LC2 in human hearts obtained at end stage idiopathic dilated cardiomyopathy (IDC). Western analyses revealed that heart tissue from patients with IDC contained 5-10 fold more mekratin than control samples. Furthermore, the level of the protease in human IDC tissues was similar to that seen in myopathic hamster skeletal muscle. No bands were recognized by the antibody when IDC myofibrils were probed due to the removal of soluble proteins during sample preparation. Thus, these results strongly suggest that the anti-mekratin antibody will provide positive identification of IDC in many cases and diagnosis by exclusion may be replaced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006842332340
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  • 4
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    Mars 2020 Entry, Descent, and Landing Instrumentation 2 (MEDLI2) Sensor Suite (2017)
    In:  CASI
    Details
    Publication Date: 2019-08-13
    Description: The Mars 2020 Entry, Descent, and Landing Instrumentation 2 (MEDLI2) sensor suite seeks to address the aerodynamic, aerothermodynamic, and thermal protection system (TPS) performance issues during atmospheric entry, descent, and landing of the Mars 2020 mission. Based on the highly successful instrumentation suite that flew on Mars Science Laboratory (MEDLI), the new sensor suite expands on the types of measurements and also seeks to answer questions not fully addressed by the previous mission. Sensor Package: MEDLI2 consists of 7 pressure transducers, 17 thermal plugs, 2 heat flux sensors, and one radiometer. The sensors are distributed across both the heatshield and backshell, unlike MEDLI (the first sensor suite), which was located solely on the heat-shield. The sensors will measure supersonic pressure on the forebody, a pressure measurement on the aftbody, near-surface and in-depth temperatures in the heatshield and backshell TPS materials, direct total heat flux on the aftbody, and direct radiative heating on the aftbody. Instrument Development: The supersonic pressure transducers, the direct heat flux sensors, and the radiometer all were tested during the development phase. The status of these sensors, including the piezo-resistive pressure sensors, will be presented. The current plans for qualification and calibration for all of the sensors will also be discussed. Post-Flight Data Analysis: Similar to MEDLI, the estimated flight trajectory will be reconstructed from the data. The aerodynamic parameters that will be reconstructed will be the axial force coefficient, freestream Mach number, base pressure, atmospheric density, and winds. The aerothermal quantities that will be determined are the heatshield and backshell aero-heating, turbulence transition across the heatshield, and TPS in-depth performance of PICA. By directly measuring the radiative and total heat fluxes on the back-shell, the convective portion of the heat flux will be estimated. The status of the current tools to perform the post-flight data analysis will be presented, along with plans for model improvements.
    Keywords: Spacecraft Instrumentation and Astrionics
    Type: ARC-E-DAA-TN40069 , International Planetary Probe Workshop; Jun 12, 2017 - Jun 16, 2017; The Hague; Netherlands
    Format: application/pdf
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  • 5
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    Overview of the MEDLI Project (2008)
    In:  CASI
    Details
    Publication Date: 2019-07-13
    Description: The Mars Science Laboratory Entry, Descent, and Landing Instrumentation (MEDLI) Project s objectives are to measure aerothermal environments, sub-surface heatshield material response, vehicle orientation, and atmospheric density for the atmospheric entry and descent phases of the Mars Science Laboratory (MSL) entry vehicle. The flight science objectives of MEDLI directly address the largest uncertainties in the ability to design and validate a robust Mars entry system, including aerothermal, aerodynamic and atmosphere models, and thermal protection system (TPS) design. The instrumentation suite will be installed in the heatshield of the MSL entry vehicle. The acquired data will support future Mars entry and aerocapture missions by providing measured atmospheric data to validate Mars atmosphere models and clarify the design margins for future Mars missions. MEDLI thermocouple and recession sensor data will significantly improve the understanding of aeroheating and TPS performance uncertainties for future missions. MEDLI pressure data will permit more accurate trajectory reconstruction, as well as separation of aerodynamic and atmospheric uncertainties in the hypersonic and supersonic regimes. This paper provides an overview of the project including the instrumentation design, system architecture, and expected measurement response.
    Keywords: Spacecraft Instrumentation and Astrionics
    Type: 2008 IEEE Aerospace Conference; Mar 01, 2008 - Mar 08, 2008; Big Sky, MT; United States
    Format: application/pdf
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