Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0026850 (
muscular dystrophy
)
5,870
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Myoadenylate deaminase
(
MAD
) is the rate-limiting enzyme in the purine nucleotide cycle which is biochemically linked to glycolysis and the citric cycle and thereby providing energy during intense muscular activity. In muscle fibers, myoadenylate deaminase operates at considerably higher activity levels than in other organs. First detected using enzyme-histochemical methods, it now appears that deficiency of myoadenylate deaminase is one of the most frequent enzyme defects in muscle. The primary defect may occur as an isolated nosological entity or not infrequently it is also associated with a large spectrum of different neuromuscular conditions. It seems to be the primary unassociated
MAD
deficiency that has recently become amenable to successful treatment with D-ribose in high doses. Secondary
MAD
deficiency may occur in muscle fibers and muscles that have undergone structural damage as seen, for instance, in polymyositis,
muscular dystrophy
, and denervation. The wealth of biochemical, morphological, and clinical data that has accumulated since the discovery of
MAD
deficiency during the past decade provides nosological significance of
MAD
deficiency as a real entity.
...
PMID:Myoadenylate deaminase deficiency. 332 44
We studied the histochemical staining and biochemical activity of
AMP deaminase
in biopsied muscle in Becker-type
muscular dystrophy
(BMD), Fukuyama-type congenital muscular dystrophy (FCMD), Duchenne-type
muscular dystrophy
(DMD), Werdnig-Hoffmann disease (WH) in order to elucidate the change of
AMP deaminase
activity in muscle with neuromuscular disorders in childhood. The intensity of
AMP deaminase
staining did not decrease in BMD with mild pathologic change, but in DMD, FCMD and WH it decreased in parallel with the severity of the pathologic change. The biochemical activity of
AMP deaminase
did not decrease in muscle with mild pathologic change in patients with DMD and tended to decrease according to the progress of the disease. The activity of
AMP deaminase
in muscle of patients with FCMD and WH which showed severe pathologic change was remarkably low. It was demonstrated that the decrease in the activity of
AMP deaminase
was related to the intensity of pathologic change rather than diagnosis of a neuromuscular disorder.
...
PMID:AMP deaminase activity of skeletal muscle in neuromuscular disorders in childhood. Histochemical and biochemical studies. 380 28
