Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027121 (myositis)
4,538 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lectins were used to characterize bone forming cells in posttraumatic myositis ossificans. The lectins applied were as follows: Arachis hypogaea (PNA): specific for beta-D-galactose (1,3)N-acetyl-D-galactosamine (Gal-1,3 GalNac), Canavalia ensiformis (Con A): specific for alpha-D-glucose (D-Glc) and alpha-D-mannose (D-Man) and Wheat germ (WGA): specific for N-acetyl(1,4)D-glucosamine (Glc-NaC) and neuraminic acid. The development of myositis ossificans was characterized by the appearance of a WGA binding cell population. The lectin-binding sites appeared as a cluster in the supranuclear cytoplasm, corresponding to the Golgi-complex. However, the WGA lectin-binding sites disappeared in the mature form of myositis ossificans. We assume that these lectin binding cells may be the bone marrow derived precursors of myofibroblast-like cells which are responsible for bone formation within the damaged muscle.
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PMID:Characterization of bone forming cells in posttraumatic myositis ossificans by lectins. 159 88

Thirty-six biopsy specimens of human biceps and vastus lateralis muscles were examined by histometric analysis and determination of enzyme activities (phosphorylase, triosephosphate dehydrogenase, 3-hydroxacyl-CoA-dehydrogenase, lactate dehydrogenase, hexose isomerase, citrate synthetase, 6-phosphogluconate dehydrogenase). The series included 13 specimens from patients suffering from a benign form of muscular dystrophy (limb girdle and Becker type of muscular dystrophy) and 12 specimens from patients with an acute (n = 5) or chronic (n = 7) form of myositis. Muscle fibres were atrophic in myositis and hypertrophic (with an increased variation of fibre diameters) in muscular dystrophies, as has been shown previously. When myositis samples were compared with either normal or dystrophic muscles, a highly significant lowering of glycolytic enzyme activity was found in chronic myositis, while the activity of 6-phosphogluconate dehydrogenase was elevated to highly significant levels. Measurements of the latter enzyme's activity might be of additional value in differentiating chronic forms of myositis from benign muscular dystrophies.
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PMID:Additional biochemical criteria in the differential diagnosis of myositis. 343 Jan 87