Investigating The Regulation And Role Of P38 Mapk In Collagen-Related Limb Girdle Muscular Dystrophy

2020 ◽  
Author(s):  
Briseida Oceguera-Perez
Keyword(s):  
Muscular Dystrophy ◽  
P38 Mapk ◽  
Limb Girdle Muscular Dystrophy

scholarly journals The role of magnetic resonance imaging of muscles in the differential diagnosis of certain forms and subtypes of limb-girdle muscular dystrophy: case analysis

2021 ◽  
Vol 16 (8) ◽  
pp. 43-47
Author(s):  
H.V. Palahuta ◽  
O.Ye. Fartushna
Keyword(s):  
Magnetic Resonance Imaging ◽  
Magnetic Resonance ◽  
Muscular Dystrophy ◽  
Correct Diagnosis ◽  
Integrated Approach ◽  
Limb Girdle Muscular Dystrophy ◽  
Resonance Imaging ◽  
Laboratory Methods ◽  
Progressive Muscular Dystrophy

Limb-girdle muscular dystrophy is a genetically heterogeneous group of disorders that are characterized by slowly progressing muscle weakness and presents a diagnostic problem in the neurological practice. The combination of clinical, radiological, and laboratory methods of examination plays an important role in referring the patient to genetic counseling and making the correct diagnosis. Magnetic resonance imaging of muscles is increasingly used to give clues in the primary muscle damage diagnosis, based on specific patterns of muscle lesion. The article provides two clinical cases as an example of an integrated approach to the diagnosis of progressive muscular dystrophy using genetic analysis and magnetic resonance imaging of muscles

scholarly journals Costameric Integrin and Sarcoglycan protein levels are altered in a Drosophila model for Limb Girdle Muscular Dystrophy type 2H

2020 ◽  
pp. mbc.E20-07-0453
Author(s):  
Simranjot Bawa ◽  
Samantha Gameros ◽  
Kenny Baumann ◽  
David S. Brooks ◽  
Joseph A. Kollhoff ◽  
...  
Keyword(s):  
Muscular Dystrophy ◽  
Limb Girdle Muscular Dystrophy ◽  
Nuclear Morphology ◽  
Muscle Degeneration ◽  
Transgenic Expression ◽  
Protein Levels ◽  
Drosophila Model ◽  
Core Components ◽  
First Time

Mutations in two different domains of the ubiquitously expressed TRIM32 protein give rise to two clinically separate diseases, one of which is Limb-girdle muscular dystrophy type 2H (LGMD2H). Uncovering the muscle-specific role of TRIM32 in LGMD2H pathogenesis has proven difficult as neurogenic phenotypes, independent of LGMD2H pathology, are present in TRIM32 KO mice. We previously established a platform to study LGMD2H pathogenesis using Drosophila melanogaster as a model. Here we show that LGMD2H disease-causing mutations in the NHL domain are molecularly and structurally conserved between fly and human TRIM32. Furthermore, transgenic expression of a subset of myopathic alleles (R394H, D487N and 520fs) induce myofibril abnormalities, altered nuclear morphology and reduced TRIM32 protein levels, mimicking phenotypes in patients afflicted with LGMD2H. Intriguingly, we also report for the first time that the protein levels of βPS integrin and Sarcoglycan δ, both core components of costameres, are elevated in TRIM32 disease-causing alleles. Similarly, murine myoblasts overexpressing a catalytically inactive TRIM32 mutant, aberrantly accumulate α- and β-Dystroglycan and α-Sarcoglycan. We speculate that the stoichiometric loss of costamere components disrupts costamere complexes to promote muscle degeneration.

scholarly journals The role of cell transplantation in modifying the course of limb girdle muscular dystrophy: a longitudinal 5-year study

2015 ◽  
pp. 93 ◽  
Author(s):  
Amruta Paranjape ◽  
Alok Sharma ◽  
Hemangi Sane ◽  
Nandini Gokulchandran ◽  
Sushant Gandhi ◽  
...  
Keyword(s):  
Muscular Dystrophy ◽  
Cell Transplantation ◽  
Limb Girdle Muscular Dystrophy

scholarly journals ANO5 ensures trafficking of annexins in wounded myofibers

2021 ◽  
Vol 220 (3) ◽  
Author(s):  
Steven J. Foltz ◽  
Yuan Yuan Cui ◽  
Hyojung J. Choo ◽  
H. Criss Hartzell
Keyword(s):  
Plasma Membrane ◽  
Fine Structure ◽  
Muscular Dystrophy ◽  
Knockout Mice ◽  
Annexin A2 ◽  
Limb Girdle Muscular Dystrophy ◽  
Membrane Repair ◽  
Phospholipid Scramblase ◽  
Plasma Membrane Repair

Mutations in ANO5 (TMEM16E) cause limb-girdle muscular dystrophy R12. Defective plasma membrane repair is a likely mechanism. Using myofibers from Ano5 knockout mice, we show that trafficking of several annexin proteins, which together form a cap at the site of injury, is altered upon loss of ANO5. Annexin A2 accumulates at the wound to nearly twice the level observed in WT fibers, while annexin A6 accumulation is substantially inhibited in the absence of ANO5. Appearance of annexins A1 and A5 at the cap is likewise diminished in the Ano5 knockout. These changes are correlated with an alteration in annexin repair cap fine structure and shedding of annexin-positive vesicles. We conclude that loss of annexin coordination during repair is disrupted in Ano5 knockout mice and underlies the defective repair phenotype. Although ANO5 is a phospholipid scramblase, abnormal repair is rescued by overexpression of a scramblase-defective ANO5 mutant, suggesting a novel, scramblase-independent role of ANO5 in repair.

scholarly journals Filamin 2 (FLN2): A Muscle-specific Sarcoglycan Interacting Protein

2000 ◽  
Vol 148 (1) ◽  
pp. 115-126 ◽  
Author(s):  
Terri G. Thompson ◽  
Yiu-Mo Chan ◽  
Andrew A. Hack ◽  
Melissa Brosius ◽  
Michael Rajala ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Protein Localization ◽  
Membrane Integrity ◽  
Limb Girdle Muscular Dystrophy ◽  
Interacting Protein ◽  
Glycoprotein Complex ◽  
Dystrophin Glycoprotein Complex ◽  
Dystrophin Glycoprotein

Mutations in genes encoding for the sarcoglycans, a subset of proteins within the dystrophin–glycoprotein complex, produce a limb-girdle muscular dystrophy phenotype; however, the precise role of this group of proteins in the skeletal muscle is not known. To understand the role of the sarcoglycan complex, we looked for sarcoglycan interacting proteins with the hope of finding novel members of the dystrophin–glycoprotein complex. Using the yeast two-hybrid method, we have identified a skeletal muscle-specific form of filamin, which we term filamin 2 (FLN2), as a γ- and δ-sarcoglycan interacting protein. In addition, we demonstrate that FLN2 protein localization in limb-girdle muscular dystrophy and Duchenne muscular dystrophy patients and mice is altered when compared with unaffected individuals. Previous studies of filamin family members have determined that these proteins are involved in actin reorganization and signal transduction cascades associated with cell migration, adhesion, differentiation, force transduction, and survival. Specifically, filamin proteins have been found essential in maintaining membrane integrity during force application. The finding that FLN2 interacts with the sarcoglycans introduces new implications for the pathogenesis of muscular dystrophy.

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