Bmd Measurement

Presentation: The word comes from Latin and Greek roots dystrophy which means "food faulty. When doctors began describing muscle diseases in the 19th century, they had few other tools of their own eyes. The muscles of many diseases seem to be wasting away, and doctors in some sort of theory that they were not well fed. Today we know that many diseases are caused by muscle atrophy defects in genes coding for muscle proteins. Most of these proteins appear to play a supporting role to the structure of muscle fibers, although some proteins may play a role in biochemical processes that occur within the muscle fibers. The term muscular dystrophy refers to a group of genetic diseases characterized by progressive weakness and degeneration of the skeletal or voluntary muscles, the movement control. The muscles of the heart and some other involuntary muscles are also affected in some forms of muscular dystrophy, and a few forms involve other organs as well. The major forms of muscular dystrophy are myotonic, Duchenne, Becker, member of belts, facioscapulo-joint, congenital oculomotor pharangeal, distal and Emery-Dreifuss. Some of these names are based on the location of the affected muscles. For example, "facioscapulo-humeral" refers to the muscles that move the face, scapula (shoulder blade) and humerus bone of the arm (top). Others are based on the type of muscle problem in question ("myotonic" means difficulty relaxing muscles), age of onset of disease (as in "congenital" or the birth of appearance Dystrophy), or physicians who first described the disease (Duchenne, Becker, Emery Dreifuss and are names of doctors). The forms of muscular dystrophy differ in severity, age of onset, muscle first and most often affected, the speed at which symptoms progress, and how disorders are inherited. Muscular dystrophy is diagnosed by muscle biopsy, DNA tests, electromyography (EMG) and nerve conduction velocity (NCV). Blood enzyme tests are useful because the muscles become degenerate "leaks". These enzymes leak, which can then be detected in the blood. The presence of these enzymes in the blood above normal is a sign of muscular dystrophy. One such enzyme is creatine kinase or CK. The CK level is elevated in many forms of muscular dystrophy, some forms resulting in a higher level than others.



Duchenne muscular dystrophy (DMD) is the most common disorders of sex-linked recessive lethal, affecting 1-3500 live births male (1). DMD children show early symptoms of muscle degeneration, frequently develop contractures, and lose the ability to walk between 6 and 12 years. With progression of the disease, most patients succumb to death by respiratory failure and cardiac dysfunction in their twenties (2). The main cause of this disease is caused by mutations in the gene for dystrophin, which is essential for the structural and functional integrity of the muscles (3). Mutations in dystrophin result in membrane damage, allowing a massive infiltration of immune cells, chronic inflammation, necrosis and severe muscle degeneration (2). Normally, muscle cells have the capacity to regenerate in response to signals of injury. However, this ability is lost in DMD, probably due to a depletion of satellite cells during continuous degeneration and regeneration cycles (1). Although dystrophin mutations are the leading cause of DMD is the secondary process leading to persistent inflammation and regeneration that impaired the progression of the disease may exacerbate. DMD is characterized by (i) The onset of muscle weakness usually before 4 years, (ii) causing muscle selective pelvic and pectoral (iii) the calf muscle hypertrophy, (iv) high rates of coarsely serum CK and (v) progressive muscle weakness tirelessly, leading to inability to work within 10 years of the onset and later contractures and chest deformities. It is not art