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 Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis

2018 ◽  
Vol 6 (2) ◽  
pp. 421-428 ◽  
Author(s):  
Radoslav Grujić ◽  
Radoslav Grujić ◽  
Danica Savanović ◽  
Danica Savanović
Keyword(s):  
Light Chain ◽  
Gel Electrophoresis ◽  
Myosin Light Chain ◽  
Troponin I ◽  
Relative Concentration ◽  
Troponin C ◽  
Myofibrillar Proteins ◽  
Pork Meat ◽  
Capillary Gel Electrophoresis ◽  
Sarcoplasmic Proteins

Myofibrillar and sarcoplasmic proteins were extracted from pork meat (M. Longissimus dorsi) and then separated by capillary gel electrophoresis (CGE). Migration time and peak areas of individual protein molecules in the electropherogram were analysed. The electropherograms obtained after the separation of myofibrillar proteins contained 53 well-separated peaks, of which the following were identified: thymosin, myosin light chain-3 (MLC-3), myosin light chain-2 (MLC-2), troponin C, troponin I, myosin light chain-1 (MLC-1), tropomyosin 1, tropomyosin 2, troponin T, actin, desmin, troponin, C protein, and myosin heavy chain (MHC). The relative concentration of the identified myofibrillar proteins was 74.5%. Of the 56 separated sarcoplasmic proteins the following were identified: myoglobin, myokinase, triosephosphate isomerase, phosphoglycerate mutase, lactate dehydrogenase, glyceraldehyde phosphate dehydrogenase, aldolase, creatine kinase, enolase, phosphoglucose isomerase, pyruvate kinase, phosphoglucomutase, and phosphorylase b. The relative concentration of the identified sarcoplasmic proteins was 83.6% of all sarcoplasmic proteins extracted from the pork meat.

scholarly journals Protein kinase C enhances myosin light-chain kinase effects on force development and ATPase activity in rat single skinned cardiac cells

1992 ◽  
Vol 285 (1) ◽  
pp. 311-317 ◽  
Author(s):  
O Clement ◽  
M Puceat ◽  
M P Walsh ◽  
G Vassort
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Troponin I ◽  
Troponin T ◽  
Cardiac Contraction ◽  
Kinase C

Many neurohormones alter the force of cardiac contraction by variations in the intracellular Ca2+ concentration. alpha 1-Adrenergic and muscarinic stimulations, rather, modify the sensitivity of contractile proteins to Ca(2+)-calmodulin-myosin light-chain kinase (MLCK) complex induces a large increase in Ca2+ sensitivity (0.14 pCa unit) of these easily accessible myofilaments. This increase is further enhanced by up to 0.19 pCa unit when protein kinase C (PKC) is added together with MLCK. Similarly, the Ca2+ ATPase activity of skinned cells in suspension is increased in the presence of MLCK and further in the presence of both kinases. 32P-labelling and SDS/PAGE show that these changes are associated with light-chain 2 (LC2) phosphorylation together with phosphorylation of troponin I and troponin T when PKC is added. Although to a smaller extent than in smooth muscle, phosphorylation of cardiac myosin LC2 may be involved in the modulation of heart contractility.

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.

Morphometry and muscle gene expression in hypertrophied hearts from polyomavirus large T antigen transgenic mice

1995 ◽  
Vol 269 (1) ◽  
pp. H86-H95 ◽  
Author(s):  
E. Holder ◽  
B. Mitmaker ◽  
L. Alpert ◽  
L. Chalifour
Keyword(s):  
Transgenic Mice ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Troponin I ◽  
T Antigen ◽  
Large T Antigen ◽  
Cross Sectional

Transgenic mice expressing polyomavirus large T antigen (PVLT) in cardiomyocytes develop a cardiac hypertrophy in adulthood. Morphometric analysis identified cardiomyocytes enlarged up to ninefold in cross-sectional area in the adult transgenic hearts compared with normal age-matched nontransgenic hearts. Most enlarged cardiomyocytes were found in the subendocardium, whereas normal-sized cardiomyocytes were localized to the midmyocardium. Transgenic hearts did not express detectable skeletal muscle actin mRNA or protein, or skeletal troponin I isoform mRNA. Some, but not all, transgenic hearts expressed an increase in the beta-myosin heavy chain mRNA. All five transgenic mice tested had increased expression of atrial natriuretic factor (ANF) mRNA. Whereas normal hearts expressed three myosin light chain proteins of 19, 16, and 15 kDa, we found that the 19-kDa myosin light chain was not observed in the transgenic hearts. We conclude that adult, PVLT-expressing, transgenic mice developed enlarged cardiomyocytes with an increase in beta-myosin heavy chain and ANF mRNA expression, but a widespread skeletal isoform usage was not present in these transgenic mice. The adult transgenic hearts thus display histological and molecular changes similar to those found in hypertrophy induced by a pressure overload in vivo.

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 Angiotensin Receptor II type 1 and the activation of Myosin Light-Chain Kinase and Protein Kinase C-βII. Mini Review.

2019 ◽  
Author(s):  
Gerry A. Smith
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Troponin I ◽  
Kinase C ◽  
Skeletal Muscle Contraction ◽  
Agonist Property

The involvement of the angiotensin II type 1 receptor in the Frank-Starling Law of the Heart, where the various activations are very limited, allows simple analysis of the kinase systems involved and thence extrapolation of the mechanism to that of angiotensin control of activation of cardiac and skeletal muscle contraction. The involvement of phosphorylation of the myosin light chain in the control of contraction is accepted but not fully understood. The involvement of troponin-I phosphorylation is also indicated but of unknown mechanism. There is no known signal for activation of myosin light chain kinase or Protein Kinase C-&beta;II other than Ca2+/calmodulin but the former is constitutively active and thus has to be under control of a regulated inhibitor the latter kinase may also be the same. Ca2+/calmodulin is not activated in Frank-Starling, i.e. there are no diastolic or systolic [Ca2+] changes. I suggest here that that the regulated inhibition is by myosin light chain phosphatase and/or &beta;-arrestin. Angiotensin activation is by translocation of the &beta;-arrestin from the sarcoplasm to the PM thus reducing its inhibition in the sarcoplasm, this reduced inhibition has been wrongly attributed to a mythical downstream agonist property of &beta;-arrestin.

Autologous Stem Cell Transplantation Improves Survival For High Risk Cardiac Amyloidosis

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 3341-3341
Author(s):  
Piyanuch Kongtim ◽  
Muzaffar H. Qazilbash ◽  
Jatin J. Shah ◽  
Robert Z. Orlowski ◽  
Amir Hamdi ◽  
...  
Keyword(s):  
Induction Chemotherapy ◽  
Light Chain ◽  
Cardiac Involvement ◽  
Troponin I ◽  
Troponin T ◽  
Cardiac Complications ◽  
Cardiac Responses ◽  
History Of ◽  
Related Mortality

Abstract Cardiac involvement in light chain amyloidosis (AL) predicts poor prognosis and is associated with higher treatment related mortality and morbidity during autologous stem cell transplantation (ASCT). We studied the outcomes of AL patients with cardiac involvement undergoing ASCT at our center between January 2002 and December 2012. Out of a total of 264 AL patients, 53 patients had cardiac involvement according to the International Consensus Criteria (Gertz M et al. AJH 2005) and 27 underwent ASCT. Cardiac staging was assessed using the Revised Prognostic Staging System for Light Chain Amyloidosis (Kumar S et al, JCO 2012). Hematologic and cardiac responses were evaluated before and at 1 year after ASCT using the guidelines established by the 10th International Symposium on Amyloid and Amyloidosis (Gertz M et al. AJH 2005). The median age of the patients was 53 years (range 36-74) with a median duration from diagnosis to ASCT of 6 months (range 3-95). The estimated median follow up for the entire cohort was 41 months (range 6-173). Twenty-four patients (89%) had an additional organ involvement, besides heart. Cardiac stage ≥3 was seen in 14 patients. The median troponin-T, Troponin-I, BNP and NT-proBNP levels and free light chain difference (FCL-diff) were 0.054 ng/ml, 0.05 ng/ml, 376 pg/ml, 1888 pg/ml, and 116.4 mg/l respectively (table1). Twenty-four patients (89%) received induction chemotherapy and 22 of those (81%) received novel chemotherapy agents. Eighteen patients (66.6%) achieved at least PR prior to ASCT. Four patients (14.8%) received reduced doses melphalan conditioning (140-180 mg/m2). One-year transplant related mortality (TRM) was 3.7% (1 patient died at day 11 post-transplant due to cardiac event). At 1-year post ASCT, overall HR was seen in 24 patients (89%) (CR=26% and PR=63%) while 3 patients (11%) had cardiac responses. At the time of last follow up, 17 patients (63%) were alive. The median overall survival (OS) from diagnosis and from ASCT was 58 months (95% CI; 46-69) and 46 months (95% CI; 36-55) respectively (figure1). The median progression free survival (PFS) was 25 months (95% CI; 6-44). Cumulative incidence of hematologic relapse at 3 year was 38.5% (95%CI 23.7-62.5). Cardiac progression at last follow up was seen in 1 patient (3.7%). Negative factors affecting OS included lack of induction therapy prior to ASCT and NT-proBNP more than 5000 pg/ml. We conclude that ASCT is well tolerated in patients with high-risk cardiac amyloidosis and the incorporation of induction therapy can improve overall outcomes of these patients.Figure1.Overall SurvivalFigure1. Overall SurvivalTable1Patient CharacteristicsBaseline characteristicsTotal (N=27)Interquartile rangeMedian age (year)5336-71Gender: male (%)20 (74.1)Median time from diagnosis to transplant, (month)63-95Receive induction chemotherapy (%)24 (88.9)Receive novel induction chemotherapy (%)22 (81.5)Light chain type (%)-Kappa-Lambda.6 (22.2) 21 (77.8)Other organ involvement (%)24 (88.9)History of cardiac complications prior ASCT (%)17 (63)History of cardiac complications after ASCT (%)20 (74.1)ICU admission prior ASCT (%)3 (11.1)Cardiac event prior ASCT (%)17 (62.9%)Median FLC-diff (mg/l) (N=15)116.415-1168Median EF (%) (N=19)6030-82Median IVS (mm.) (N=14)1.350.7-2.1Median Troponin-T (ng/ml) (N=20)0.0190.01-0.22Median Troponin-I (ng/ml) (N=19)0.060.03-9.09Median BNP (pg/ml) (N=23)37615.2-1782Median NT-proBNP (pg/ml) (N=12)1888.519-9911Median serum calcium (mg/dl)9.27-11Median serum albumin (g/dl)3.92.4Median Creatinine (mg/dl)1.01-9Median B2 microglobulin (mg/l)3.151-15Median 24-hr urine protein (mg)574120-36006Median serum M protein (g/dl)0.50-4Median LDH (IU/l)377146-770Median BM plasma cell (%)110-58Cardiac stage at diagnosis.Stage 11Stage 25Stage 36Stage 48Cardiac stage at transplant.Stage 13Stage 25Stage 34Stage 46 Disclosures: No relevant conflicts of interest to declare.

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