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4 edition of Dystrophin gene regulation in muscle found in the catalog.

Dystrophin gene regulation in muscle

Jennifer Bestard

Dystrophin gene regulation in muscle

by Jennifer Bestard

  • 336 Want to read
  • 19 Currently reading

Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

Thesis (M.Sc.) -- University of Toronto, 2000.

SeriesCanadian theses = -- Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches : negative. --
ID Numbers
Open LibraryOL20846325M
ISBN 100612540863
OCLC/WorldCa50755986

  Record studies in all patients that have XLDC with mutations at the 5′ end of the dystrophin gene have noticed brain and Purkinje isoforms of dystrophin located in the skeletal muscle. However, they have not been noticed in cardiac muscle (Singh, ). This regulation compensates for the lack of the muscle isoform. Nine patients with Duchenne or Becker muscular dystrophy were injected via the radialis muscle with a full-length human dystrophin plasmid, either once with or µg of DNA or twice, 2 weeks apart, with µg of the biopsies taken 3 weeks after the initial injection, the vector was detected at the injection site in all by:

The brain and cerebellar Purkinje promoters were found to be essentially inactive in muscle cell lines and primary cultures. Since dystrophin muscle enhancer-1 (DME1), a muscle-specific enhancer, is preserved in these patients, the authors tested its ability to upregulate the brain and cerebellar Purkinje promoters in muscle cells. • nearly all types of muscular dystrophy arise from single-gene mutations (one target) challenging: • efficient delivery of the new gene to most of the striated muscle in the body (>40% of body mass) • design of viral vectors to carry the large genes to be replaced (dystrophin gene, for example, is Mb in size) • muscle transduction File Size: 2MB.

Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic. Utrophin is a protein that in humans is encoded by the UTRN gene.. The protein encoded by this gene is a component of the in was found during research into Duchenne's muscular name is a contraction for ubiquitous kb gene for utrophin is found on the long arm of human chromosome in was discovered due to its homology with s: UTRN, DMDL, DRP, DRP1, utrophin.


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Dystrophin gene regulation in muscle by Jennifer Bestard Download PDF EPUB FB2

DYSTROPHIN GENE REGULATION IN MUSCLE Master of Science, Jennifer Bestard Department of Medical Biophysics University of Toronto ABSTRACT The identification and charactenzation of the muscle-promoter and a muscle- specific enhancer within intron 1 has led to advances in Our undentanding of dystrophin oene regulation in : Jennifer Bestard.

The Dystrophin Glycoprotein Complex Regulates the Epigenetic Activation of Muscle Stem Cell Commitment Natasha C. Chang,1,2 Marie-Claude Sincennes,1,2 Fabien P. Chevalier,1,2 Caroline E.

Brun,1,2 Melanie Lacaria,1,2 Jessica Segale´s,3 Pura Mun˜oz-Ca´noves,3 Hong. This gene encodes a large, rod-like cytoskeletal protein which is found at the inner surface of muscle fibers in skeletal and cardiac muscles.

The encoded protein, dystrophin, is part of the dystrophin-glycoprotein complex, which bridges the inner cytoskeleton (F-actin) and the extra-cellular matrix. This protein is required for proper development and organization of myofibers as contractile.

Key Terms. dystrophin: A cytoplasmic structural protein that is deficient in some forms of muscular dystrophy.; muscular dystrophy: A group of genetic diseases that cause progressive skeletal muscle weakness, defects in muscle proteins, and the death of muscle cells and tissue.; Muscular dystrophy (MD) is a group of muscle diseases characterized by the creation of non-functional muscle.

DMD, the largest known human gene, provides instructions for making a protein called dystrophin. This protein is located primarily in muscles used for movement (skeletal muscles) and in heart (cardiac) muscle. Small amounts of dystrophin are present in nerve cells in the brain. A number of genes that cause LGMD2s encode proteins that directly associate with dystrophin, forming integral parts of the dystrophin glycoprotein complex (DGC).

In muscle cells, the dystrophin complex localizes at the membrane and connects intercellular cytoskeleton to Cited by:   The dystrophin (DMD) gene, located at Xpp, is one of the largest human genes and consists of 79 DMD gene encodes dystrophin, a large Author: Tetsuhiko Ikeda, Hidehiko Fujinaka, Kiyoe Goto, Takashi Nakajima, Tetsuo Ozawa.

The gene encoding dystrophin is the largest identified in humans, occupying approximately 1% of the X chromosome. It extends over Kb and comprises 79 exons (20).

Approximately % from the patients which were diagnoses with DMD/DMB have a deletions in the dystrophin gene. The remaining 30% are assumed to results from micro deletions. Up-regulation of the dystrophin-related gene utrophin represents a promising therapeutic strategy for the treatment of Duchenne Muscular Dystrophy (DMD).

In order to re-program the utrophin expression level in muscle, we engineered artificial zinc finger transcription factors (ZF-ATFs) that target the utrophin ʻAʼ Cited by: 5. Dystrophin is a rod-shaped protein, measuring about nm, consisting of amino acids with a calculated molecular weight of kDa.

Dystrophin is predominantly hydrophilic throughout its entire length and 31% of the amino-acids are charged (i.e. Arg, Asp, Glu, His and Lys).Missing: muscle book.

Introduction. Duchenne muscular dystrophy (DMD) is a lethal X-linked disorder caused by mutations in the dystrophin gene, which encodes a cytoskeletal protein, absence of dystrophin results in progressive degeneration of skeletal and cardiac muscle with fibrotic tissue replacement, fatty infiltration, and subsequent early death by respiratory or heart failure.Cited by: What is dystrophin.

Dystrophin is a protein found in muscle cells. It is one of a group of proteins that work together to strengthen muscle fibers and protect them from injury as muscles contract and relax. INTRODUCTION. Mutations of the dystrophin DMD gene are the cause of two devastating and to date incurable diseases, Duchenne (DMD) and Becker (BMD) muscular dystrophies [].

DMD gene is the longest human gene with Megabases of DNA representing ~1% of the chromosome X DNA [2, 3].It is localized on the locus p21 of chromosome X and codes for the protein by: Without dystrophin the muscle fibre membranes become damaged and eventually the muscle fibres die.

Gene regulation. Increasing or decreasing the amount of protein produced by a gene. These mice have a mutation in the dystrophin gene – the gene that is mutated in boys with Duchenne.

The X-linked dystrophin gene is by far the largest of genes that encode proteins in the human genome: its 79 exons cover million base pairs (bp).This large size makes the gene.

Although the lack of dystrophin expression in muscle myofibers is the central cause of Duchenne muscular dystrophy (DMD), accumulating evidence suggests that DMD may also be a Cited by: 2. The dystrophin gene is the largest gene identified so far, covering more than megabases (Mb), and contains at least 79 exons; the high spontaneous mutation rate is a reflection of the large gene size.

Dystrophin is primarily expressed in skeletal, cardiac, and smooth muscle cells, with smaller amounts expressed in the brain and retina. Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC).

Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan Aliases: DMD, BMD, CMD3B, DXS. Abnormal calcium handling in muscular dystrophy was confirmed by studies with mdx fibres, demonstrating increases in cytosolic Ca2+ levels in dystrophin-deficient myotubes [6].

However, this finding was not universally confirmed. Several other groups reported no difference in the resting values of intracellular Ca2+ concentrations inFile Size: KB. Of note, down-regulation of dystrophin in mTOR − muscle cannot be attributed to the loss of both mTORC1 and mTORC2 functions because DmKO mice neither display a more severe phenotype than RAmKO nor the characteristic Akt protein up-regulation observed in dystrophin-deficient muscles (Dogra et al., ).Cited by:.

tively adsorb the dystrophin-glycoprotein complex. Further- more, there is a marked reduction of the K glycoprotein in muscle from mdx mice and DMD patients. These results imply that in dystrophic muscle, the absence of dystrophin may lead to the loss of a dystrophin .Mutational analysis of muscle and brain specific promoter regions of dystrophin gene in DMD/BMD Italian patients by denaturing gradient gel electrophoresis (DGGE).

Mol. Cell.The and kD dystrophin-associated proteins were severely reduced in the heart, despite the presence of Dp71, but not in skeletal muscle. The absence of dystrophin and the down-regulation of the dystrophin-associated proteins in the heart accounted for the severe cardiomyopathy in this by: