Spatial distribution of “tissue-specific” antigens in the developing human heart and skeletal muscle. I. An immunohistochemical analysis of creatine kinase isoenzyme expression patterns

1990 ◽  
Vol 228 (2) ◽  
pp. 163-176 ◽  
Author(s):  
A. Wessels ◽  
J. L. M. Vermeulen ◽  
S. Z. Virágh ◽  
F. Kálmán ◽  
G. E. Morris ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Spatial Distribution ◽  
Human Heart ◽  
Expression Patterns ◽  
Immunohistochemical Analysis ◽  
Tissue Specific ◽  
Creatine Kinase Isoenzyme ◽  
Specific Antigens

Creatine kinase:aspartate aminotransferase activity ratio as an indicator of the source of an increased creatine kinase activity.

1988 ◽  
Vol 34 (12) ◽  
pp. 2506-2510 ◽  
Author(s):  
D R Dufour
Keyword(s):  
Myocardial Infarction ◽  
Skeletal Muscle ◽  
Acute Myocardial Infarction ◽  
Creatine Kinase ◽  
Retrospective Study ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Creatine Kinase Activity ◽  
Aminotransferase Activity ◽  
Creatine Kinase Isoenzyme

Abstract Although measurements of creatine kinase isoenzyme 2 (CK-MB) are often used to diagnose acute myocardial infarction, their sensitivity and specificity are less than 100%. Because skeletal muscle contains more CK and less aspartate aminotransferase (AST) than cardiac muscle, the CK/AST ratio might provide a useful adjunct in evaluating the source of a supranormal value for CK. I established the following decision levels in a retrospective study of 342 patients: ratios less than 14 (if total CK was 300-1200 U/L), less than 20 (CK 1201-2000 U/L), or less than 25 (CK greater than 2000 U/L) suggested myocardial infarction, with a sensitivity of 95% and a specificity of 65%. In a validation study with 277 additional patients, liver disease and alcohol abuse caused erroneous results, leading to exclusion of 22% of these patients. In the remaining cases, sensitivity was 94%, specificity 90%. The CK/AST ratios changed little with time, suggesting that a single value would be adequate for evaluating patients with increased CK.

scholarly journals Electroacupuncture suppresses myostatin gene expression: cell proliferative reaction in mouse skeletal muscle

2007 ◽  
Vol 30 (2) ◽  
pp. 102-110 ◽  
Author(s):  
Yutaka Takaoka ◽  
Mika Ohta ◽  
Akihiko Ito ◽  
Kunihiko Takamatsu ◽  
Aki Sugano ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Proliferation ◽  
Satellite Cells ◽  
Expression Patterns ◽  
Low Frequency ◽  
Immunohistochemical Analysis ◽  
Long Term Effects ◽  
Transcription Control ◽  
Myostatin Gene ◽  
Mouse Skeletal Muscle

Complementary and alternative medicine (CAM) may provide patients with an alternative to traditional medicine, but an assessment of its efficacy is required. One CAM method, electroacupuncture (EA) treatment, is a maneuver that utilizes stimulation of acupuncture needles with a low-frequency microcurrent. To study the effect of short-term EA, we evaluated the differential expression of genes induced by EA in mouse skeletal muscle for up to 24 h. We then used RT-PCR to confirm the expression patterns of six differentially expressed genes. Bioinformatics analysis of their transcription control regions showed that EA-inducible genes have numerous common binding motifs that are related to cell differentiation, cell proliferation, muscle repair, and hyperplasia. These results suggested that EA treatment may induce cell proliferation in skeletal muscle. To verify this possibility, we used EA to stimulate mouse skeletal muscle daily for up to 1 mo and examined the long-term effects. Immunohistochemical analysis showed that nuclei of muscle cells treated with EA for 1 mo, especially nuclei of satellite cells, reacted with anti-human PCNA. Also, expression of the gene encoding myostatin, which is a growth repressor in muscle satellite cells, was suppressed by daily EA treatment for 1 wk; EA treatment for 1 mo resulted in more marked suppression of the gene. These molecular findings constitute strong evidence that EA treatment suppresses myostatin expression, which leads to a satellite cell-related proliferative reaction and repair in skeletal muscle.

scholarly journals Expression of SERPINA3s in cattle: focus on bovSERPINA3-7 reveals specific involvement in skeletal muscle

Open Biology ◽  
2015 ◽  
Vol 5 (9) ◽  
pp. 150071 ◽  
Author(s):  
Antoine Péré-Brissaud ◽  
Xavier Blanchet ◽  
Didier Delourme ◽  
Patrick Pélissier ◽  
Lionel Forestier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Expression Patterns ◽  
Physiological Role ◽  
Reactive Centre Loop ◽  
Slow Twitch ◽  
High Degree ◽  
Degree Of Similarity ◽  
Different Tissues ◽  
Antiprotease Activity

α 1 -Antichymotrypsin is encoded by the unique SERPINA3 gene in humans, while it is encoded by a cluster of eight closely related genes in cattle. BovSERPINA3 proteins present a high degree of similarity and significant divergences in the reactive centre loop (RCL) domains which are responsible for the antiprotease activity. In this study, we analysed their expression patterns in a range of cattle tissues. Even if their expression is ubiquitous, we showed that the expression levels of each serpin vary in different tissues of 15-month-old Charolais bulls. Our results led us to focus on bovSERPINA3-7, one of the two most divergent members of the bovSERPINA3 family. Expression analyses showed that bovSERPINA3-7 protein presents different tissue-specific patterns with diverse degrees of N -glycosylation. Using a specific antibody raised against bovSERPINA3-7, Western blot analysis revealed a specific 96 kDa band in skeletal muscle. BovSERPINA3-7 immunoprecipitation and mass spectrometry revealed that this 96 kDa band corresponds to a complex of bovSERPINA3-7 and creatine kinase M-type. Finally, we reported that the bovSERPINA3-7 protein is present in slow-twitch skeletal myofibres. Precisely, bovSERPINA3-7 specifically colocalized with myomesin at the M-band region of sarcomeres where it could interact with other components such as creatine kinase M-type. This study opens new prospects on the bovSERPINA3-7 function in skeletal muscle and promotes opportunities for further understanding of the physiological role(s) of serpins.

Creatine kinase isoenzyme MM variants in skeletal muscle and plasma from marathon runners.

1986 ◽  
Vol 32 (1) ◽  
pp. 41-44 ◽  
Author(s):  
F S Apple ◽  
M A Rogers ◽  
J L Ivy
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Strenuous Exercise ◽  
Variant Form ◽  
Distance Runners ◽  
Long Distance ◽  
Marathon Runners ◽  
Creatine Kinase Isoenzyme ◽  
Before And After

Abstract We investigated the patterns of variants of creatine kinase isoenzyme MM (CK-MM) in gastrocnemius muscle and plasma sampled from male and female long-distance runners before and after a marathon race. The proportions of CK-MM variants MM1 (pI 6.90) and MM2 (pI 6.62), identified in the skeletal muscle from both sexes, did not differ significantly from those in skeletal muscle from nonrunning controls or from heart muscle. CK-MM1 was the major (84-85% of total CK-MM) variant form. Patterns of CK-MM in plasma collected from male runners 24, 48, 72, and 96 h after the race were similar to those for female runners, but we detected two new additional variants, which we designate MM1B (pI 6.76) and MM2B (pI 6.49). For both sexes the total CK-MM activities in plasma were significantly (p less than 0.05) greater after the race, but the women's total CK-MM activities were significantly (p less than 0.05) less than the men's. The rates of disappearance of MM1, MM2, and MM3 from plasma after the race differed significantly (p less than 0.05) between men and women, MM1 clearing the fastest. Determination of the CK-MM variants in plasma after strenuous exercise may be of help in assessing CK release from injured skeletal muscle.

scholarly journals Single-Blind Study of Dystrophin Staining in Carriers of Duchenne Muscular Dystrophy

1993 ◽  
Vol 20 (1) ◽  
pp. 44-47 ◽  
Author(s):  
Francois P. Bernier ◽  
Cheryl R. Greenberg ◽  
William C. Halliday ◽  
Klaus Wrogemann
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Duchenne Muscular Dystrophy ◽  
Muscular Dystrophy ◽  
Diagnostic Test ◽  
Family Members ◽  
Immunohistochemical Analysis ◽  
Blind Study ◽  
Single Blind

ABSTRACT:A single-blind study of dystrophin staining in skeletal muscle was performed in 13 biopsies from carriers of Duchenne Muscular Dystrophy (DMD) and controls. The results indicate that immunohistochemical analysis of dystrophin staining is a valuable diagnostic test for DMD carriers when DNA for testing is unavailable from critical family members or is uninformative, when creatine kinase (CK) values are conflicting or when CK values must be used in isolation.

scholarly journals Temporal and spatial distribution of murine placental and brain GLUT3-luciferase transgene as a readout of in vivo transcription

2013 ◽  
Vol 304 (3) ◽  
pp. E254-E266 ◽  
Author(s):  
Shanthie Thamotharan ◽  
David Stout ◽  
Bo-Chul Shin ◽  
Sherin U. Devaskar
Keyword(s):  
Skeletal Muscle ◽  
Spatial Distribution ◽  
Protein Expression ◽  
Luciferase Activity ◽  
Ex Vivo ◽  
Embryonic Brain ◽  
Temporal And Spatial Distribution ◽  
Tissue Specific ◽  
Temporal And Spatial

To investigate in vivo transcription of the facilitative glucose transporter isoform-GLUT3 gene, we created GLUT3-firefly luciferase transgenic mouse lines that demonstrate tissue-specific [adult: brain > testis ≥ skeletal muscle > placenta; postnatal (PN): skeletal muscle > brain = skin], temporal, and spatial distribution of the reporter gene/enzyme activity that is unique from endogenous GLUT3 mRNA/protein. In this mouse model, luciferase expression/activity serving as a readout of in vivo transcription peaked at 12 days gestation along with proliferating cell nuclear antigen (cell replication) in placenta and embryonic brain preceding peak GLUT3 protein expression at 18–19 days gestation. In contrast, a postnatal increase in brain luciferase mRNA peaked with endogenous GLUT3 mRNA, but after that of NeuroD6 protein (neurogenesis) at PN7. Luciferase activity paralleled GLUT3 protein expression with Na+-K+-ATPase (membrane expansion) and synaptophysin (synaptogenesis) proteins, peaking at PN14 and lasting until 60 days in the adult. Thus GLUT3 transcription in placenta and embryonic brain coincided with cell proliferation and in postnatal brain with synaptogenesis. Longitudinal noninvasive bioluminescence (BLI) monitoring of in vivo brain GLUT3 transcription reflected cross-sectional ex vivo brain luciferase activity only between PN7 and PN21. Hypoxia/reoxygenation at PN7 revealed transcriptional increase in brain GLUT3 expression reflected by in vivo BLI and ex vivo luciferase activity. These observations collectively support a temporal contribution by transcription toward ensuring adequate tissue-specific, developmental (placenta and embryonic brain), and postnatal hypoxic brain GLUT3 expression.

Sign in / Sign up

Export Citation Format

Share Document