Dystrophin: Gene, Protein and Cell Biology PDF

PBB GE Dystrophin: Gene, Protein and Cell Biology PDF 202222 s at fs. Desmin is a protein that in humans is encoded by the DES gene. 5 kD protein composed of 470 amino acids.


This book is concerned with advances in research on dystrophin, and how its absence gives rise to muscular dystrophy. It is the first book to address relationships between the molecular structure and function of dystrophin since the structure of the gene for this protein was elucidated in 1988. The volume covers recent advances in knowledge on the structure of both the dystrophin gene and its associated promoters, and on the protein itself. Functional interactions of dystrophin and its related proteins in the environment of the plasma membrane are a central feature of the book. Other aspects considered are the expression of the dystrophin complex in muscle, in the brain, and at the neuromuscular junction. The book concludes with discussions of muscle regeneration, gene therapy of Duchenne muscular dystrophy, and cellular approaches to the therapy of the disease.

There are three major domains to the desmin protein: a conserved alpha helix rod, a variable non alpha helix head, and a carboxy-terminal tail. Cardiac tissue also exhibited progressive necrosis and calcification of the myocardium. In human heart failure, desmin expression is upregulated, which has been hyopthesized to be a defense mechanism in an attempt to maintain normal sarcomere alignment amidst disease pathogenesis. Desmin has been evaluated for role in assessing the depth of invasion of urothelial carcinoma in TURBT specimens.

A dysfunctional desmin mutation in a patient with severe generalized myopathy ». Proceedings of the National Academy of Sciences of the United States of America. Human desmin-coding gene: complete nucleotide sequence, characterization and regulation of expression during myogenesis and development ». The physiological role of cardiac cytoskeleton and its alterations in heart failure ». Mass spectrometry characterization of human DES at COPaKB ».

Integration of cardiac proteome biology and medicine by a specialized knowledgebase ». The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation? Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle ». Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments ». Association with actin and desmin filaments ». Immunological characterization of the subunit of the 100 A filaments from muscle cells ».

Invariance and heterogeneity in the major structural and regulatory proteins of chick muscle cells revealed by two-dimensional gel electrophoresis ». Desmin: molecular interactions and putative functions of the muscle intermediate filament protein ». Revista Brasileira De Pesquisas Medicas E Biologicas. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin ». The absence of desmin leads to cardiomyocyte hypertrophy and cardiac dilation with compromised systolic function ». Journal of Molecular and Cellular Cardiology.

Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle ». Structural and functional roles of desmin in mouse skeletal muscle during passive deformation ». Increased expression of cytoskeletal, linkage, and extracellular proteins in failing human myocardium ». Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function ». Functional characterization of the novel DES mutation p.

L136P associated with dilated cardiomyopathy reveals a dominant filament assembly defect ». Desmin mutation responsible for idiopathic dilated cardiomyopathy ». Missense mutations in desmin associated with familial cardiac and skeletal myopathy ». De novo desmin-mutation N116S is associated with arrhythmogenic right ventricular cardiomyopathy ». Desmin mutations and arrhythmogenic right ventricular cardiomyopathy ». Dual color photoactivation localization microscopy of cardiomyopathy-associated desmin mutants ».