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tropinine c

W Frank Peacock, Deborah Diercks, Robert Birkhahn, Adam J Singer, Judd E Hollander, Richard Nowak, Basmah Safdar, Chadwick D Miller, Mary Peberdy, Francis Counselman, Abhinav Chandra, Joshua Kosowsky, James Neuenschwander, Jon Schrock, Elizabeth Lee-Lewandrowski, William Arnold, John Nagurney
BACKGROUND: We aimed to compare the diagnostic accuracy of the Alere Triage Cardio3 Tropinin I (TnI) assay (Alere, Inc., USA) and the PathFast cTnI-II (Mitsubishi Chemical Medience Corporation, Japan) against the central laboratory assay Singulex Erenna TnI assay (Singulex, USA). METHODS: Using the Markers in the Diagnosis of Acute Coronary Syndromes (MIDAS) study population, we evaluated the ability of three different assays to identify patients with acute myocardial infarction (AMI)...
September 2016: Annals of Laboratory Medicine
Vesna V Radović
INTRODUCTION: Biochemical cardiac markers play an important role in diagnosing and treatment of patients with acute coronary syndrome. Markers of myocytes necrosis, troponins, have been recommended for diagnosing and treatment of myocardial infarction with ST segment elevation, myocardial infarction without ST segment elevation and unstable angina pectoris. Two more groups of cardiac markers have been gaining in importance: inflammation markers and cardiac function markers.The objective of this study was the risk stratification and identification of patients with coronary syndrome, who could take advantage from evolutionary, changes of serum cardiac markers...
September 2010: Medicinski Pregled
C I Tsao, R J Chen, N K Chou, W J Ko, N H Chi, H Y Yu, Y S Chen, S C Chen, S S Wang
With improved immunosuppressive regimens, transplantation techniques, and postoperative care, heart transplantation (HTx) has been established as a definite therapy for end-stage heart disease. Because of a donor shortage, we have accepted marginal individuals. In this study, we identified donor-related factors influencing survival after HTx by retrospective analysis of recipient data after primary HTx from February 2002 to December 2006. The Cox regression model was used to examine the effects of the following variables on survival of 112 heart transplant recipients: demographic data of gender, age, body weight, donor-recipient body weight ratio; history of smoking, alcohol drinking, diabetes mellitus, hypertension, hepatitis B surface antigen, anti-hepatitis C virus antibody; donor condication before transplantation including catecholamine doses, hypotension, cardiopulmonary resuscitation, creatine MB isoenzyme of creatine kinase (CK-MB), tropinin I, and cold ischemic time of the allograft...
October 2008: Transplantation Proceedings
Chih-Yung Chiou, I-Ping Chen, Chienhsun Chen, Henry Ju-Lin Wu, Nuwei Vivian Wei, Carden C Wallace, Chaolun Allen Chen
Calmodulin (CaM), belonging to the tropinin C (TnC) superfamily, is one of the calcium-binding proteins that are highly conserved in their protein and gene structure. Based on the structure comparison among published vertebrate and invertebrate CaM, it is proposed that the ancestral form of eumetazoan CaM genes should have five exons and four introns (four-intron hypothesis). In this study, we determined the gene structure of CaM in the coral Acropora muricata, an anthozoan cnidarian representing the basal position in animal evolution...
April 2008: Journal of Molecular Evolution
N Morjana, D Clark, R Tal
Cardiac troponin I (cTnI) is the inhibitory subunit of the troponin complex and is a biochemical marker for myocardial infarction (MI). It is found in human serum within 4-6 h following MI. One of us has shown [Morjana (1998) Biotechnol. Appl. Biochem. 28, 105-111] that MI patient serum TnI is cleaved at the N- and C-terminals and that the TnI fragments exist as a complex with tropinin C (TnC) and troponin T (TnT). In the present study, we have generated C-terminal truncated TnI fragments and studied their immunological and biochemical properties...
April 2001: Biotechnology and Applied Biochemistry
R Hirsch, C L Dent, M K Wood, C B Huddleston, E N Mendeloff, D T Balzer, Y Landt, C A Parvin, M Landt, J H Ladenson, C E Canter
BACKGROUND: Perioperative myocardial injury is a major determinant of postoperative cardiac dysfunction for congenital heart disease, but its assessment during this period is difficult. The objective of this study was to determine the suitability of using postoperative serum concentrations of cardiac troponin I (cTnI) for this purpose. METHODS: Cardiac troponin I levels were measured serially in the serum of patients undergoing uncomplicated repairs of atrial septal defect (n = 23), ventricular septal defect (n = 16) or tetralogy of Fallot (n = 16)...
May 1998: Annals of Thoracic Surgery
B Lauer, C Niederau, U Kühl, M Schannwell, M Pauschinger, B E Strauer, H P Schultheiss
BACKGROUND AND OBJECTIVE: Results of routine laboratory tests for demonstrating myocardial damage in patients suspected of having myocarditis are often negative. This study was undertaken to ascertain (1) whether measuring Tropinin T (cTnT) in these patients can sensitively determine myocardial cell death, (2) to what extent this correlates with the findings of endomyocardial biopsy, and (3) whether measurement of cTnT can provide noninvasive assessment of the course of myocarditis. PATIENTS AND METHODS: 80 consecutive patients (52 men, 28 women) with clinically suspected myocarditis were investigated...
April 3, 1998: Deutsche Medizinische Wochenschrift
A B Akella, H Su, E H Sonnenblick, V G Rao, J Gulati
The Ca2+ sensitivity of tension in cardiac muscle is length dependent, such that the sensitivity is diminished with decreasing sarcomere length below 2.4 microm. This length dependence of Ca2+ sensitivity of tension also forms the basis for the Frank-Starling mechanism in the heart. The fast-twitch skeletal muscle has a much lower length dependence of Ca2+ sensitivity. In a recent study of skinned cardiotrabeculae, we indicated that the exchange of endogenous cardiac troponin C (TnC) for skeletal troponin C also resulted in a major reduction in the length dependence to the level of skeletal muscle...
January 1997: Journal of Molecular and Cellular Cardiology
E Fyrberg, C C Fyrberg, C Beall, D L Saville
In vertebrates troponin complexes interact co-operatively with tropomyosin dimers to modulate skeletal muscle contraction. In order further to investigate troponin assembly and function in vivo, we are developing molecular genetic approaches. Here we report characterization of the gene that encodes Drosophila tropinin-T and analyses of muscle defects engendered by several mutant alleles. We found that the Drosophila troponin-T locus specifies at least three proteins having sequences similar to vertebrate troponin-T...
December 5, 1990: Journal of Molecular Biology
Z Dobrowolski, G Q Xu, W Chen, S E Hitchcock-DeGregori
Five deletion mutants of the D/E linker region of the troponin C central helix were tested for conformational and functional differences from wild-type troponin C. The mutants were in the region 87KEDAKGKSEEE97: dEDA, dKG, dKGK, dKEDAKGK, and dSEEE, designed to change the length of the central helix and the orientation of the Ca(2+)-binding domains relative to each other [Dobrowolski, Z., Xu, G.-Q., & Hitchcock-DeGregori, S.E. (1991) J. Biol. Chem. 266, 5703-5710]. Previous work showed that all mutants except dSEEE are partially defective in one part of the Ca2+ switch or the other...
July 23, 1991: Biochemistry
D Mercola, B Bullard, J Priest
No abstract text is available yet for this article.
April 17, 1975: Nature
F J Wilson, D Camiscoli, M J Irish, T Hirabayashi
The pectoral muscles from normal and dystrophic chickens were reacted with rabbit antisera to troponin-C and to troponin-I, and the distribution of antibodies was determined by fluorescence microscopy of antibody-stained myofibrils and immuno-electron microscopy of separated I band segments. Chickens of dystrophic strain 308 and control New Hampshire hens were used in this work. Myofibrils which were prepared from both normal and dystrophic muscles and reacted with anti-troponin-I were fluorescent in the I band and A band regions...
April 1978: Journal of Histochemistry and Cytochemistry: Official Journal of the Histochemistry Society
C Mahendran, S Berl
A troponin-like complex has been isolated from bovine brain cortex. This tropinin-like complex, with brain tropomyosin, confers Ca2+ sensitivity to the actin-activated myosin adenosinetriphosphatase (ATP phosphohydrolase, EC That is, the Mg2+-stimulated ATPase activity generated by the interaction of purified muscle actin with muscle myosin is inhibited in the absence of Ca2+ but not in the presence of Ca2+ as a result of the addition of both brain tropomyosin and troponin-like complex. The troponin-like complex contains three components, one of which is similar in molecular weight to the troponin-T of skeletal actomyosin...
June 1977: Proceedings of the National Academy of Sciences of the United States of America
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