Measurement of myosin light chain I and troponin T as markers on myocardial damage after cardiac surgery

1995 ◽  
Vol 3 ◽  
pp. 86-86
Author(s):  
T UCHINO ◽  
A BELBOUL ◽  
D ROBERTS ◽  
S ISHIMARU
Keyword(s):  
Cardiac Surgery ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Troponin T ◽  
Myocardial Damage

Abstract P219: Differences in Phosphoproteins in Rodent versus Human Hearts: Implications for Translational Studies of Hypertensive Heart Disease

Hypertension ◽  
2015 ◽  
Vol 66 (suppl_1) ◽  
Author(s):  
Robert S Danziger ◽  
Kumar Kotlo ◽  
Allen Samarel ◽  
Hua Chen ◽  
Jared Aldstadt
Keyword(s):  
Heart Disease ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Troponin T ◽  
Hypertensive Heart Disease ◽  
Left Ventricular ◽  
Current Evidence ◽  
Tissue Samples ◽  
Pixel Intensity ◽  
Translational Studies

Background: Rodent models are commonly used to study hypertensive heart disease. Several recent studies have probed the level of correlation between specific signaling pathways and proteins in human and rodents. Current evidence is overwhelming that protein phosphorylations play a key role in cardiac remodeling. Methods: Left ventricular tissue samples were obtained from human systolic failing (n=5) and control (n=5) hearts and 3 rat models of hypertensive heart failure (aortic banding, Dahl salt-sensitive, and spontaneously hypertensive rats (SHR)) and corresponding controls. Total proteins were extracted and and phosphoenrichment performed. Phosphoproteins were separated by 2D-DIGE with Cydye staining. Gel images were registered and rectified for composite analysis and statistical comparisons using pixel intensity. Phosphoproteins were identified by MALDI-TOF/TOF Mass Spectrometry. Results: The patterns of overall protein abundance from normal and failing hearts were not statistically different. However, when the composite of human hearts were compared with composite patterns of phosphoproteins in normal and failing rodent hearts, there were profound differences in the phosphoprotein patterns in 26% of pixels in registered images (P < 0.05). Targeted pair wise analyses showed differences (P < 0.05) between human and rodent hearts for troponin T, myosin light chain, peroxiredoxin, and haptoglobin phosphorylations. Conclusions: Together, the present results indicate significant differences in cardiac phosphoproteins in human versus rodent heart and the importance of confirming findings from rodent studies in humans for translational studies of kinases, phosphatases, and phosphoproteins. This may specifically relate to studies of phosphorylation of myosin light chain and troponin.

scholarly journals Myocardial Infarct Size by Serum Troponin T and Myosin Light Chain 1 Concentration.

1995 ◽  
Vol 59 (3) ◽  
pp. 154-159 ◽  
Author(s):  
Takashi Omura ◽  
Masakazu Teragaki ◽  
Masahiko Takagi ◽  
Tomoko Tani ◽  
Yukio Nishida ◽  
...  
Keyword(s):  
Infarct Size ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Troponin T ◽  
Myocardial Infarct ◽  
Myocardial Infarct Size

scholarly journals Effects of temperature and method of heat treatment on myofibrillar proteins of pork

2014 ◽  
Vol 20 (3) ◽  
pp. 407-415 ◽  
Author(s):  
Dragan Vujadinovic ◽  
Radoslav Grujic ◽  
Vladimir Tomovic ◽  
Aleksandra Torbica
Keyword(s):  
Heat Treatment ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Troponin I ◽  
Troponin T ◽  
Protein S ◽  
Treatment Temperature ◽  
M Protein ◽  
Meat Sample ◽  
Myofibrillar Proteins

During the tests in this paper, meat processing was carried out at different temperatures between the range of 51?C to 100?C. The meat was processed by dry heat (roasting) and wet heat treatments (cooking) in water at atmospheric pressure. After heat treatment, myofibrillar proteins were extracted from solutions at constant ionic strength. Quantitative and qualitative determinations of protein?s fractions were performed by capillary electrophoresis. Myofibrillar proteins were also analized for fresh pork meat sample. Results obtained in fresh meat were compared with those recorded after roasting and cooking. In the fresh and thermally processed pork the following proteins were identified: myosin, light chain 3; myosin, light chain 2; troponin - C; troponin - I; myosin, light chain 1; tropomyosin; troponin - T; actin; desmin; ? - actinin; C - protein; M - protein (M?); M - protein (M?); heavy meromyosin - HMM. For both methods of thermal processing, with increasing heat treatment temperature, concentration of soluble protein in the extract decreases rapidly after 51?C. Cooking treatment had a more intense effect on the proteins change and denaturation than roasting.

Immunocytochemical investigations of muscle differentiation in the Atlantic herring (Clupea harengus: Teleostei)

1994 ◽  
Vol 74 (1) ◽  
pp. 79-91 ◽  
Author(s):  
I. A. Johnston ◽  
Z. Horne
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Troponin I ◽  
Troponin T ◽  
Small Diameter ◽  
Fibre Volume ◽  
Clupea Harengus ◽  
Muscle Fibres ◽  
Atlantic Herring ◽  
Superficial Muscle

The myotomes in yolk-sac larvae of the Atlantic herring (Clupea harengus: Teleostei) contain a single layer of small-diameter superficial muscle fibres surrounding an inner mass of around 280 larger-diameter muscle fibres. The fraction of muscle fibre volume occupied by mitochondria is dependent on temperature, and in larvae reared at 8°C was 41% for the superficial fibres, and 25% for the inner muscle fibres. The inner muscle fibres of larvae share some myofibrillar proteins with adult white muscle, but contain unique isoforms of myosin heavy chains, troponin T, troponin I and myosin light chain 2. A monoclonal antibody has been produced which is specific to myosin light chain 3 (MLC3). Immunocytochemical studies have shown that the expression of MLC3 is switched off in the superficial muscle fibres at the start of metamorphosis when larvae reach 28–30 mm total length (TL). Metamorphosis to the juvenile stage is complete in fish 35–40 mm TL and is also associated with the development of gill filaments and the production of presumptive slow muscle fibres which form externally to the larval superficial muscle fibres in the region of the lateral line nerve.

scholarly journals Monitoring myocardial damage in cardiac surgery by troponin T detection.

Heart ◽  
1994 ◽  
Vol 71 (1) ◽  
pp. 109-109 ◽  
Author(s):  
M. Triggiani ◽  
A. Dolci ◽  
F. Donatelli ◽  
A. Grossi
Keyword(s):  
Cardiac Surgery ◽  
Troponin T ◽  
Myocardial Damage

scholarly journals TROPONIN T AFTER CARDIAC SURGERY: WHAT IS NORMAL? A REVIEW OF THE LITERATURE

2021 ◽  
Vol 5 (11) ◽  
Author(s):  
Jessy Nellipudi
Keyword(s):  
Cardiac Surgery ◽  
Troponin T ◽  
Postoperative Mortality ◽  
Myocardial Damage ◽  
Point Of View ◽  
Cardiac Biomarkers ◽  
Mortality And Morbidity ◽  
Serial Measurement ◽  
Risk Patients ◽  
Post Cardiac Surgery

It is well established that cardiac biomarkers are universally raised post-cardiac surgery. This is due to various preoperative, intraoperative, and postoperative factors. At present, no reliable tool or model considers intraoperative and postoperative factors to predict morbidity and mortality after cardiac surgery. Troponin T as a single or serial measurement to predict postoperative mortality and morbidity, is an attractive diagnostic tool due to the direct relationship to myocardial damage and the availability of testing. Currently, there is no consensus regarding the expected release of troponin T post-cardiac surgery. From a diagnostic and prognostic point of view, troponin T testing could be beneficial in recognising high-risk patients and any imminent compilations early. Therefore, this review aims to assess the expected release profile and prognostic value of troponin T after cardiac surgery. Keywords: troponin T., CABG, MPM, SAPS

scholarly journals p21-activated kinase improves cardiac contractility during ischemia-reperfusion concomitant with changes in troponin-T and myosin light chain 2 phosphorylation

2012 ◽  
Vol 302 (1) ◽  
pp. H224-H230 ◽  
Author(s):  
Michelle M. Monasky ◽  
Domenico M. Taglieri ◽  
Bindiya G. Patel ◽  
Jonathan Chernoff ◽  
Beata M. Wolska ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Diastolic Pressure ◽  
Troponin T ◽  
Ex Vivo ◽  
Ischemia Reperfusion ◽  
Cardiac Contractility ◽  
Left Ventricular ◽  
Myosin Light Chain 2 ◽  
P21 Activated Kinase

p21-activated kinase 1 (Pak1) is a serine/threonine kinase that activates protein phosphatase 2a, resulting in the dephosphorylation of cardiac proteins and increased myofilament Ca2+ sensitivity. Emerging evidence indirectly indicates a role for Pak1 in ischemia-reperfusion (I/R), but direct evidence is lacking. We hypothesize that activation of the Pak1 signaling pathway is a cardioprotective mechanism that prevents or reverses the detrimental effects of ischemic injury by inducing posttranslational modifications in myofilament proteins that ultimately improve cardiac contractility following ischemic insult. In the present study, we subjected ex vivo hearts from wild-type (WT) and Pak1-knockout (KO) mice to 20 min of global cardiac ischemia followed by 30 min of reperfusion. In the absence of Pak1, there was an exacerbation of the increased end-diastolic pressure and reduced left ventricular developed pressure occurring after I/R injury. ProQ analysis revealed an increase in troponin-T phosphorylation at baseline in Pak1-KO hearts compared with WT. Significantly decreased myosin light chain 2 (MLC2) phosphorylation in Pak1-KO hearts compared with WT after I/R injury was confirmed by Western immunoblotting. These data indicate that Pak1-KO hearts have reduced recovery of myocardial performance after global I/R injury concomitant with changes in troponin-T and MLC2 phosphorylation. Finally, a protein-protein association between Pak1 and MLC2, and Pak1 and troponin-T, was determined by coimmunoprecipitation. Thus, results of our study provide a basis for targeting a novel pathway, including Pak1, in the therapies for patients with ischemic events.

scholarly journals Phorbol esters selectively and reversibly inhibit a subset of myofibrillar genes responsible for the ongoing differentiation program of chick skeletal myotubes.

1991 ◽  
Vol 11 (9) ◽  
pp. 4473-4482 ◽  
Author(s):  
J K Choi ◽  
S Holtzer ◽  
S A Chacko ◽  
Z X Lin ◽  
R K Hoffman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Steady State ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Phorbol Esters ◽  
Troponin T ◽  
Housekeeping Genes ◽  
Common Mechanism ◽  
Mrna Levels ◽  
Alpha Actin

Phorbol esters selectively and reversibly disassemble the contractile apparatus of cultured skeletal muscle as well as inhibit the synthesis of many contractile proteins without inhibiting that of housekeeping proteins. We now demonstrate that phorbol esters reversibly decrease the mRNA levels of at least six myofibrillar genes: myosin heavy chain, myosin light chain 1/3, myosin light chain 2, cardiac and skeletal alpha-actin, and skeletal troponin T. The steady-state message levels decrease 50- to 100-fold after 48 h of exposure to phorbol esters. These decreases can be attributed at least in part to decreases in transcription rates. For at least two genes, cardiac and skeletal alpha-actin, some of the decreases are the result of increased mRNA turnover. In contrast, the cardiac troponin T steady-state message level does not change, and its transcription rate decreases only transiently upon exposure to phorbol esters. Phorbol esters do not decrease the expression of the housekeeping genes, alpha-tubulin, beta-actin, and gamma-actin. Phorbol esters do not decrease the steady-state message levels of MyoD1, a gene known to be important in the activation of many skeletal muscle-specific genes. Cycloheximide blocks the phorbol ester-induced decreases in transcription, message stability, and the resulting steady-state message level but does not block the tetradecanoyl phorbol acetate-induced rapid disassembly of the I-Z-I complexes. These results suggests a common mechanism for the regulation of many myofibrillar genes independent of MyoD1 mRNA levels, independent of housekeeping genes, but dependent on protein synthesis.

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