Wyniki wyszukiwania

1

Muscular dystrophy in mice caused by two different alterations of dystrophin gene

100%

Rowinski J., Kozlowska H., Sulikowska-Rowinska A., Rejment E.

Folia Histochemica et Cytobiologica

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2001

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tom 39

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nr 2

2

Muscle stem/progenitor cells and mesenchymal stem cells of bone marrow origin for skeletal muscle regeneration in muscular dystrophies

72%

Klimczak A., Kozlowska U., Kurpisz M.

Archivum Immunologiae et Therapiae Experimentalis

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2018

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tom 66

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nr 5

3

Several dystrophin-glycoprotein complex members are present in crude surface membranes but they are sodium dodecyl sulphate invisible in KCI-washed microsomes from mdx mouse muscle

72%

Daval S., Rocher C., Cherel Y., Rumeur E.

Cellular and Molecular Biology Letters

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2010

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tom 15

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nr 1

134-152

The dystrophin-glycoprotein complex (DGC) is a large trans-sarcolemmal complex that provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. In skeletal muscle, it consists of the dystroglycan, sarcoglycan and cytoplasmic complexes, with dystrophin forming the core protein. The DGC has been described as being absent or greatly reduced in dystrophin-deficient muscles, and this lack is considered to be involved in the dystrophic phenotype. Such a decrease in the DGC content was observed in dystrophin-deficient muscle from humans with muscular dystrophy and in mice with X-linked muscular dystrophy (mdx mice). These deficits were observed in total muscle homogenates and in partially membrane-purified muscle fractions, the so-called KCl-washed microsomes. Here, we report that most of the proteins of the DGC are actually present at normal levels in the mdx mouse muscle plasma membrane. The proteins are detected in dystrophic animal muscles when the immunoblot assay is performed with crude surface membrane fractions instead of the usually employed KCl-washed microsomes. We propose that these proteins form SDS-insoluble membrane complexes when dystrophin is absent.

4

The involvement of oxidative stress in determining the severity and progress of pathological processes in dystrophin-deficient muscles

72%

Niebroj-Dobosz I., Hausmanowa-Petrusewicz I.

Acta Biochimica Polonica

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2005

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tom 52

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nr 2

In both forms of muscular dystrophy, the severe Duchenne’s muscular dystrophy (DMD) with lifespan shortened to about 20 years and the milder Becker dystrophy (BDM) with normal lifespan, the gene defect is located at chromosome locus Xp21. The location is the same in the experimental model of DMD in the mdx mice. As the result of the gene defect a protein called dystrophin is either not synthesized, or is produced in traces. Although the structure of this protein is rather well established there are still many controversies about the dystrophin function. The most accepted suggestion supposes that it stabilizes sarcolemma in the course of the contraction-relaxation cycle. Solving the problem of dystrophin function is a prerequisite for introduction of an effective therapy. Among the different factors which might be responsible for the appearance and progress of dystrophic changes in muscles there is an excessive action of oxidative stress. In this review data indicating the influence of oxidative stress on the severity of the pathologic processes in dystrophy are discussed. Several pieces of data indicating the action of oxidative damage to different macromolecules in DMD/BDM are presented. Special attention is devoted to the degree of oxidative damage to muscle proteins, the activity of neuronal nitric oxide synthase (nNOS) and their involvement in defining the severity of the dystrophic processes. It is indicated that the severity of the morbid process is related to the degree of oxidative damage to muscle proteins and the decrease of the nNOS activity in muscles. Estimation of the degree of the destructive action of oxidative stress in muscular dystrophy may be a useful marker facilitating introduction of an effective antioxidant therapy and regulation of nNOS activity.

5

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

58%

Botzenhart U. U., Vaal V., Rentzsch I., Gredes T., Gedrange T., Kunert-Keil

Journal of Physiology and Pharmacology

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2017

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tom 68

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nr 2

6

HIV-1 Tat-derived peptides as allosteric inhibitors of the proteasome activity

58%

Stoj J., Karpowicz P., Gaczynska M., Osmulski P., Jankowska E.

Acta Neurobiologiae Experimentalis

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2013

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tom 73

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nr 1

The proteasome is a main protease of the ubiquitin-proteasome pathway, responsible for degradation of the majority of intracellular proteins in human cells. Since the proteasome regulates so many processes, abnormalities in its functioning play a causal role in a number of diseases, including muscular dystrophy, cardiovascular diseases and various cancers. The ubiquitin-proteasome pathway is involved also in disorders affecting central nervous system – cerebral ischemia/reperfusion injury and stroke. This implication in pathological condition makes the proteasome an important and very promising therapeutic target. The 26S proteasome, which is responsible for ATP-dependent proteolysis of ubiquitin-tagged proteins, consists of a barrel-like core particle – the 20S proteasome, and attached to it two regulatory particles 19S. The core particle is composed of four rings (αββα). The inner β-rings harbour active sites, which display distinct specificities and are responsible for cleavages of polypeptides after hydrophobic, acidic and basic residues (Marques et al. 2009). On the other hand, N-terminal residues of α subunits create a gate leading to the catalytic chamber. Because most of the already known proteasome inhibitors are competitive they are not selective enough and can block all active sites causing cell apoptosis. We believe that allosteric modulators may be an interesting alternative to active site inhibitors. The multi-subunit and multi-active sites structure of the proteasome creates an opportunity to selective allosteric regulation of its activity. We focus our searching on biomolecules which bind to the α-ring of the 20S proteasome and influence the enzyme’s gating mechanism. HIV-1 Tat protein is one of the natural proteasome regulators competing with 11S activator for binding to the α-rings (Huang et al. 2002). We designed two peptides: G48RKKRRQRRRPS59 (Tat1) and R49KKRRQRR56Q66DPI69 (Tat2) based on a sequence of the basic domain of the protein (Jankowska et al. 2010). We found that both of them efficiently inhibit 20S proteasome. We tried to connect the biological activity of Tat peptides to their structure determined by means of CD, FTIR, NMR and molecular dynamics simulation. Additionally, we synthesized alanine scan of Tat2 to determine the importance of individual amino acids. We exchanged not only single residues but also several adjacent amino acids at once and tested the influence of these changes on the proteasome activity. We also investigated the scan peptides’ structure using FTIR. The work was supported by grants: 538-8440-1043-12, DS/8440-4- 0172-2 and NCN 2011/01/B/ST5/06616

7

Caveolin-1, caveolin-3 and VEGF expression in the masticatory muscles of mdx mice

58%

Kunert-Keil C., Gredes T., Lucke S., Morgenstern S., Mielczarek A., Sporniak-Tutak K., Gedrange T., Spassov A.

Folia Histochemica et Cytobiologica

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2011

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tom 49

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nr 2

8

Interrelationship between gene, its product and phenotype in Duchenne and Becker muscular dystrophy

58%

Hausmanowa-Petrusewicz I., Zaremba J., Fidzianska A., Zimowski J., Bisko M., Badurska B., Fidzianska E., Lusakowska A., Borkowska J.

Acta Neurobiologiae Experimentalis

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1993

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tom 53

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nr 1

9

MU firing characteristics in human dystrophic muscle

58%

Piotrkiewicz M., Filipiuk M., Hausmanowa-Petrusewicz I.

Acta Neurobiologiae Experimentalis

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1993

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tom 53

|

nr 1

Ograniczanie wyników

Muscular dystrophy in mice caused by two different alterations of dystrophin gene

Muscle stem/progenitor cells and mesenchymal stem cells of bone marrow origin for skeletal muscle regeneration in muscular dystrophies

Several dystrophin-glycoprotein complex members are present in crude surface membranes but they are sodium dodecyl sulphate invisible in KCI-washed microsomes from mdx mouse muscle

The involvement of oxidative stress in determining the severity and progress of pathological processes in dystrophin-deficient muscles

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

HIV-1 Tat-derived peptides as allosteric inhibitors of the proteasome activity

Caveolin-1, caveolin-3 and VEGF expression in the masticatory muscles of mdx mice

Interrelationship between gene, its product and phenotype in Duchenne and Becker muscular dystrophy

MU firing characteristics in human dystrophic muscle