Dystrophin is a protein found in membranes surrounding individual muscle fibers, and its deficiency is one of the root causes of muscular dystrophy. It was first identified in 1987 by Louis M. Kunkel, after the 1986 discovery of the mutated gene that causes Duchenne muscular dystrophy (DMD). A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... A muscle fiber (American usage) or muscle fibre (British usage) is a single cell of a muscle. ... The muscular dystrophies are a group of genetic and hereditary muscle diseases; characterized by progressive skeletal muscle weakness, defects in muscle proteins, and the death of muscle cells and tissue. ... 1987 is a common year starting on Thursday of the Gregorian calendar. ... 1986 is a common year starting on Wednesday of the Gregorian calendar. ... Duchenne muscular dystrophy (also known as pseudohypertrophic muscular dystrophy or muscular dystrophy - Duchenne type) is an inherited disorder characterized by rapidly progressive muscle weakness which starts in the legs and pelvis and later affects the whole body. ...
Normal tissue contains small amounts of dystrophin (about 0.002% of total muscle protein), but its absence leads to both DMD and fibrosis, a condition of muscle hardening. A different mutation of the same gene causes defective dystrophin, leading to Becker's muscular dystrophy (BMD). Dystrophin is the longest gene known to date. Fibrosis is the formation or development of excess fibrous connective tissue in an organ or tissue as a reparative or reactive process, as opposed to formation of fibrous tissue as a normal constituent of an organ or tissue. ... Beckers muscular dystrophy (also known as Benign pseudohypertrophic muscular dystrophy) is an X-linked recessive inherited disorder characterized by slowly progressive muscle weakness of the legs and pelvis. ...
Duchenne (DMD) and Becker muscular dystrophy are caused by mutations in the dystrophin (dys) gene.
The requirement for dystrophin is haplo-insufficient, indicating that the Drosophila NMJ is highly sensitive to the levels of Dystrophin, possibly reflecting its interaction with rate-limiting signaling factors (van der Plas, 2006).
Dystrophin and CaMKII are unlikely, however, to signal through the PMad-dependent BMP signaling pathway, because the expression levels and domains of PMad are unchanged when Dystrophin or CaMKII levels are either decreased or increased.
Dystrophin, identified nearly 20 years ago as the protein deficient in Duchenne muscular dystrophy (DMD)[1], is now recognised as the founder member of a protein superfamily with representatives throughout the animal kingdom[2].
Dystrophin, utrophin and DRP2 together constitute the vertebrate members of the dystrophin branch of the superfamily; although their function is not well understood, they each (via their signature C-terminal domains) form the core of a membrane-bound complex comprising dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) [5].
Dp260 is an isoform encoded by exons 30–79 of the mammalian dystrophin gene.
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