Cardiac troponin-I content of skeletal muscle in patients with renal failure

2002 ◽  
Vol 35 (5) ◽  
pp. 421-423 ◽  
Author(s):  
Salim Fredericks ◽  
Kate Bainbridge ◽  
Christiane D Fenske ◽  
David Gaze ◽  
Paul O Collinson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Renal Failure ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I

scholarly journals The phosphorylation of troponin I from cardiac muscle

1975 ◽  
Vol 149 (3) ◽  
pp. 525-533 ◽  
Author(s):  
H A Cole ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Cardiac Muscle ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Phosphorylase Kinase ◽  
Dependent Protein Kinase ◽  
Dependent Protein

1. Troponin I isolated from fresh cardiac muscle by affinity chromatography contains about 1.9 mol of covalently bound phosphate/mol. Similar preparations of white-skeletal-muscle troponin I contain about 0.5 mol of phosphate/mol. 2. A 3':5'-cyclic AMP-dependent protein kinase and a protein phosphatase are associated with troponin isolated from cardiac muscle. 3. Bovine cardiac 3':5'-cyclic AMP-dependent protein kinase catalyses the phosphorylation of cardiac troponin I 30 times faster than white-skeletal-muscle troponin I. 4. Troponin I is the only component of cardiac troponin phosphorylated at a significant rate by the endogenous or a bovine cardiac 3':5'-cyclic AMP-dependent protein kinase. 5. Phosphorylase kinase catalyses the phosphorylation of cardiac troponin I at similar or slightly faster rates than white-skeletal-muscle troponin I. 6. Troponin C inhibits the phosphorylation of cardiac and skeletal troponin I catalysed by phosphorylase kinase and the phosphorylation of white skeletal troponin I catalysed by 3':5'-cyclic AMP-dependent protein kinase; the phosphorylation of cardiac troponin I catalysed by the latter enzyme is not inhibited.

scholarly journals GATA elements control repression of cardiac troponin I promoter activity in skeletal muscle cells

2007 ◽  
Vol 8 (1) ◽  
pp. 78 ◽  
Author(s):  
Raffaella Di Lisi ◽  
Anne Picard ◽  
Simonetta Ausoni ◽  
Stefano Schiaffino
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Troponin ◽  
Promoter Activity ◽  
Troponin I ◽  
Muscle Cells ◽  
Cardiac Troponin I ◽  
Skeletal Muscle Cells

Cardiac Troponin I and T Concentrations in Patients with Cocaine-Associated Chest Pain

1996 ◽  
Vol 33 (3) ◽  
pp. 183-186 ◽  
Author(s):  
Mary McLaurin ◽  
Fred S Apple ◽  
Timothy D Henry ◽  
Scott W Sharkey
Keyword(s):  
Skeletal Muscle ◽  
Chest Pain ◽  
Cardiac Troponin ◽  
Muscle Injury ◽  
Troponin I ◽  
Troponin T ◽  
Acute Chest Pain ◽  
Cardiac Troponin I ◽  
Skeletal Muscle Injury ◽  
Rule Out

Patients with cocaine-related chest pain with electrocardiographic (ECG) abnormalities are often admitted to rule out acute myocardial infarction (AMI). Cardiac troponin I and T should be superior to measurement of creatine kinase (CK)—MB for detecting cardiac injury in patients with coexisting skeletal muscle injury. We prospectively evaluated 19 consecutive patients with acute chest pain related to cocaine use who were hospitalized to rule out AMI. The admission ECG was abnormal in 16 of 19 patients. Total CK and CK—MB were elevated during the hospital course in 14 and 3 patients, respectively. Cardiac troponin I and cardiac troponin T levels were within normal limits in all patients demonstrating that recent myocardial injury did not occur. Clinically, no patient had an AMI. Cocaine-induced thoracic skeletal muscle injury or transient cocaine-induced coronary vasospasm should be considered as alternative sources of chest pain in these patients.

Effect of denervation on the content of cardiac troponin-T and cardiac troponin-I in rat skeletal muscle

2007 ◽  
Vol 40 (5-6) ◽  
pp. 423-426 ◽  
Author(s):  
Salim Fredericks ◽  
Hans Degens ◽  
Godfrina McKoy ◽  
Katie Bainbridge ◽  
Paul O. Collinson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Troponin T ◽  
Cardiac Troponin I ◽  
Cardiac Troponin T ◽  
Rat Skeletal Muscle

Cardiac troponin-I is not expressed in fetal and healthy or diseased adult human skeletal muscle tissue

1995 ◽  
Vol 41 (12) ◽  
pp. 1710-1715 ◽  
Author(s):  
G S Bodor ◽  
D Porterfield ◽  
E M Voss ◽  
S Smith ◽  
F S Apple
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Troponin ◽  
Human Skeletal Muscle ◽  
Troponin I ◽  
Tissue Bank ◽  
Cardiac Troponin I ◽  
Muscle Disease ◽  
Adult Skeletal Muscle ◽  
Muscle Sample ◽  
Creatine Kinase Mb

Abstract Cardiac troponin-I (cTnI) is not found in sera of patients with skeletal muscle disease in the absence of myocardial injury. It is not known, however, whether trace amounts of cTnI are expressed in regenerating human skeletal muscle, as has been observed with creatine kinase MB. Using immunohistochemical and biochemical techniques, we investigated cTnI expression in various human muscle tissues: human heart tissue (n = 5), normal adult skeletal muscle (n = 3), and fetal heart (n = 3) and skeletal muscle (n = 3) obtained, respectively, during heart transplant, from autopsy, or from a tissue bank. Specimens from diagnostic tissue biopsies were used as diseased skeletal muscle: polymyositis (PM), n = 13; Duchenne muscular dystrophy (DMD), n = 6. Frozen sections 8 microns thick were stained immunohistochemically for either cTnI or TnI (cardiac or skeletal) by using monoclonal antibodies (MAb) 2B1.9 (cTnI specific) or 3C5.10 (reactive with all TnI isoforms), respectively. cTnI was measured in tissue homogenates by an immunofluorometric assay. Cardiac muscle was stained by both MAbs. Normal fetal and adult skeletal muscle, and samples from all of the PM and DMD patients, stained only with the nonspecific MAb (3C5.10), confirming the sole presence of skeletal TnI. No cTnI was detectable by immunoassay in any skeletal muscle sample. We conclude that cTnI is not expressed in human skeletal muscle during development or during regenerative muscle disease processes such as PM or DMD.

scholarly journals Developing Cardiac and Skeletal Muscle Share Fast-Skeletal Myosin Heavy Chain and Cardiac Troponin-I Expression

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e40725 ◽  
Author(s):  
Kelly C. Clause ◽  
Jason Tchao ◽  
Mary C. Powell ◽  
Li J. Liu ◽  
Johnny Huard ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Skeletal Myosin

scholarly journals The amino acid sequence of rabbit cardiac troponin I

1976 ◽  
Vol 159 (3) ◽  
pp. 633-641 ◽  
Author(s):  
R J A. Grand ◽  
J M Wilkinson ◽  
L E More
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Inhibitory Activity ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Muscle Protein ◽  
Cardiac Troponin I ◽  
Skeletal Muscle Protein ◽  
Fast Skeletal Muscle

The complete amino acid sequence of troponin I from rabbit cardiac muscle was determined by the isolation of four unique CNBr fragments, together with overlapping tryptic peptides containing radioactive methionine residues. Overlap data for residues 35-36, 93-94 and 140-145 are incomplete, the sequence at these positions being based on homology with the sequence of the fast-skeletal-muscle protein. Cardiac troponin I is a single polypeptide chain of 206 residues with mol.wt. 23550 and an extinction coefficient, E 1%,1cm/280, of 4.37. The protein has a net positive charge of 14 and is thus somewhat more basic than troponin I from fast-skeletal muscle. Comparison of the sequences of troponin I from cardiac and fast skeletal muscle show that the cardiac protein has 26 extra residues at the N-terminus which account for the larger size of the protein. In the remainder of sequence there is a considerable degree of homology, this being greater in the C-terminal two-thirds of the molecule. The region in the cardiac protein corresponding to the peptide with inhibitory activity from the fast-skeletal-muscle protein is very similar and it seems unlikely that this is the cause of the difference in inhibitory activity between the two proteins. The region responsible for binding troponin C, however, possesses a lower degree of homology. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50072 (20 pages), at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1976) 153, 5.

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