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

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.

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.

scholarly journals Troponin I from human skeletal and cardiac muscles

1978 ◽  
Vol 171 (1) ◽  
pp. 251-259 ◽  
Author(s):  
P Cummins ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Troponin ◽  
Skeletal Muscles ◽  
Cardiac Tissue ◽  
Troponin I ◽  
Rank Order ◽  
Cardiac Troponin I ◽  
Rabbit Muscle ◽  
Cardiac Muscles ◽  
Human Skeletal Muscles

1. Myofibrils from human skeletal muscle contained regulatory proteins exhibiting similar electrophoretic behaviour to those present in rabbit skeletal muscle. 2. All human skeletal muscles examined contained two forms of troponin I corresponding to the forms already characterized in fast and slow rabbit muscle. 3. The ratios of the amounts of the two forms of troponin I in different human skeletal muscles were not identical with the ratios for the type 1 to type 2 fibres published in the literature. The ratios could, however, be arranged in the same rank order. 4. Primate heart contained a single form of troponin I different in molecular weight and amino acid composition from the skeletal forms. 5. A monospecific antiserum to human cardiac troponin I was prepared in the sheep and shown not to react with the fast or slow skeletal-muscle forms of troponin I from human and other species. 6. The anti-(human cardiac-muscle troponin I) reacted with the cardiac troponin I from the human, baboon, rabbit and rhesus monkey. Positive reactions were also obtained with urea extracts of whole cardiac tissue.

scholarly journals Muscle-specific expression of the troponin I gene requires interactions between helix-loop-helix muscle regulatory factors and ubiquitous transcription factors.

1991 ◽  
Vol 11 (1) ◽  
pp. 267-280 ◽  
Author(s):  
H Lin ◽  
K E Yutzey ◽  
S F Konieczny
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Troponin I ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Specific Expression ◽  
Enhancer Activity ◽  
Regulatory Factors ◽  
Helix Loop Helix ◽  
Muscle Regulatory Factors

The quail fast skeletal troponin I (TnI) gene is a member of the contractile protein gene set and is expressed exclusively in differentiated skeletal muscle cells. TnI gene transcription is controlled by an internal regulatory element (IRE), located within the first intron, that functions as a muscle-specific enhancer. Recent studies have shown that the TnI IRE may interact directly with the muscle regulatory factors MyoD, myogenin, and Myf-5 to produce a muscle-specific expression pattern, since these factors trans-activate cotransfected TnI gene constructs in C3H10T1/2 fibroblasts. In this study, we have examined the protein-IRE interactions that are responsible for transcriptionally activating the TnI gene during skeletal muscle development. We demonstrate that the helix-loop-helix muscle regulatory factors MyoD, myogenin, Myf-5, and MRF4, when complexed with the immunoglobulin enhancer-binding protein E12, interact with identical nucleotides within a muscle regulatory factor-binding site (MRF site) located in the TnI IRE. The nuclear proteins that bind to the MRF site are restricted to skeletal muscle cells, since protein extracts from HeLa, L, and C3H10T1/2 fibroblasts do not contain similar binding activities. Importantly, the TnI MRF site alone is not sufficient to elicit the full enhancer activity associated with the IRE. Instead, two additional regions (site I and site II) are required. The proteins that interact with site I and site II are expressed in both muscle and nonmuscle cell types and by themselves are ineffective in activating TnI gene expression. However, when the MRF site is positioned upstream or downstream of site I and site II, full enhancer activity is restored. We conclude that helix-loop-helix muscle regulatory factors must interact with ubiquitously expressed proteins to generate the active TnI transcription complex that is present in differentiated muscle fibers.

Muscle-specific expression of the troponin I gene requires interactions between helix-loop-helix muscle regulatory factors and ubiquitous transcription factors

1991 ◽  
Vol 11 (1) ◽  
pp. 267-280 ◽  
Author(s):  
H Lin ◽  
K E Yutzey ◽  
S F Konieczny
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Troponin I ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Specific Expression ◽  
Enhancer Activity ◽  
Regulatory Factors ◽  
Helix Loop Helix ◽  
Muscle Regulatory Factors

The quail fast skeletal troponin I (TnI) gene is a member of the contractile protein gene set and is expressed exclusively in differentiated skeletal muscle cells. TnI gene transcription is controlled by an internal regulatory element (IRE), located within the first intron, that functions as a muscle-specific enhancer. Recent studies have shown that the TnI IRE may interact directly with the muscle regulatory factors MyoD, myogenin, and Myf-5 to produce a muscle-specific expression pattern, since these factors trans-activate cotransfected TnI gene constructs in C3H10T1/2 fibroblasts. In this study, we have examined the protein-IRE interactions that are responsible for transcriptionally activating the TnI gene during skeletal muscle development. We demonstrate that the helix-loop-helix muscle regulatory factors MyoD, myogenin, Myf-5, and MRF4, when complexed with the immunoglobulin enhancer-binding protein E12, interact with identical nucleotides within a muscle regulatory factor-binding site (MRF site) located in the TnI IRE. The nuclear proteins that bind to the MRF site are restricted to skeletal muscle cells, since protein extracts from HeLa, L, and C3H10T1/2 fibroblasts do not contain similar binding activities. Importantly, the TnI MRF site alone is not sufficient to elicit the full enhancer activity associated with the IRE. Instead, two additional regions (site I and site II) are required. The proteins that interact with site I and site II are expressed in both muscle and nonmuscle cell types and by themselves are ineffective in activating TnI gene expression. However, when the MRF site is positioned upstream or downstream of site I and site II, full enhancer activity is restored. We conclude that helix-loop-helix muscle regulatory factors must interact with ubiquitously expressed proteins to generate the active TnI transcription complex that is present in differentiated muscle fibers.

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