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1

The transcriptional cascade associated with creatine kinase down-regulation and mitochondrial biogenesis in mice sarcoma

100%
Bera S., Ray M.
Cellular and Molecular Biology Letters
|
2009
|
tom 14
|
nr 3
481-496
The tissue-specific expressions of creatine kinase (CK) isoforms are regulated by the coordinated action of various transcription factors. The myogenic differentiation factor D (MyoD) family of proteins and the myocyte-specific enhancer binding factor 2 family of transcription factors are important in regulating the muscle-specific expression of cytosolic muscle-type CK (MCK) and mitochondrial CKs. As reported in some related studies, TNF-α mediated degradation of MyoD and myogenin mRNA may lead to severe muscle wasting and cachexia, which is characterized by a low transcript level of MCK and myosin heavy chain proteins. In our previous study, we reported on a complete loss of total CK activity and expression when sarcoma was induced in mouse skeletal muscle (Patra et al. FEBS J. 275 (2008) 3236–3247). This study aimed at investigating the transcriptional cascade of CK down-regulation in carcinogen-induced sarcoma in mouse muscle. Both CK deficiency and enhanced nitric oxide synthase (NOS) were known to augment mitochondrial biogenesis, so we also explored the activation of the transcriptional cascade of mitochondrial biogenesis in this cancer. We observed the activation of the TNF-α-mediated nitric oxide production pathway with NFκB activation and concomitant degradation of MyoD and myogenin mRNA. Exploration of mitochondrial biogenesis revealed high cytochrome c oxidase activity and mitochondrial DNA content in sarcoma. The PGC-related co-activator seems to have a major role in regulating mitochondrial biogenesis by upregulating nuclear respiratory factors and mitochondrial transcription factor A. From the above findings, it can be concluded that severe muscle degeneration leads to CK down-regulation in sarcoma, and that the stimulation of mitochondrial biogenesis indicated a scenario representing both CK deficiency and NOS overexpression on the one hand, and altered bioenergetic profiling on the other.
2

Adenosine deaminase in the diagnosis of white muscle diseases in lambs

84%
Altug N., Agaoglu Z. T., Yuksek N., Kaya A., Keles I.
Medycyna Weterynaryjna
|
2006
|
tom 62
|
nr 09
1007-1010
The aim of the study was to investigate the importance of ADA serum and its isoenzyme activity in diagnosing white muscle disease in lambs. The animal material used in the study was forty seven Akkaraman lambs - twenty seven of which had clinical signs of white muscle disease (white muscle disease group) and twenty healthy lambs (control group). Blood samples were taken and Se levels, CK, LDH, AST, ADA and ADA izoenzyme activity were determined. Following this, the animals in the white muscle disease group received 1 mg sodium selenit + 60 mg vitamin E intramuscularly as a single dose. Fourteen days following sodyum selenit + vitamin E application blood samples were again taken and the same analysis repeated. Apart from ADA2 activity, other enzyme activities were significantly high (p<0.001), and serum Se concentrations were significantly low (p<0.001) in animals of the white muscle disease group compared to the control group. When the parameters obtained from the white muscle disease group were compared before and after treatment it was indicated that all enzyme parameters decreased significantly (p<0.001) after treatment. On the other hand, serum Se concentration increased (p<0.01) after treatment in the diseased group. The results confirm that determining ADA serum and its isoenzymes, together with CK, LDH and AST values seems to be useful in diagnosing white muscle disease.
3
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Changes in caveolin-1, caveolin-3 and vascular endothelial growth factor expression and protein content after botulinum toxin A injection in the right masseter muscle of dystrophin deficient (mdx-) mice

67%
Botzenhart U. U., Vaal V., Rentzsch I., Gredes T., Gedrange T., Kunert-Keil
Journal of Physiology and Pharmacology
|
2017
|
tom 68
|
nr 2
4

Mouse gastrocnemius muscle regeneration after mechanical or cardiotoxin injury

67%
Czerwinska A. M., Streminska W., Ciemerych M. A., Grabowska I.
Folia Histochemica et Cytobiologica
|
2012
|
tom 50
|
nr 1
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