acid-phosphatase and Dermatomyositis

To determine the presence of small integrin-binding ligand N-linked glycoprotein (SIBLING) and bone components in juvenile dermatomyositis (DM) pathologic calcifications.. Calcifications were removed from 4 girls with juvenile DM symptoms for mean +/- SD 36.9 +/- 48.3 months and were stained for SIBLING proteins: full-length osteopontin (OPN), bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin phosphoprotein (DPP), and matrix extracellular phosphoglycoprotein (MEPE); bone markers: osteocalcin (OC), core-binding factor alpha 1 (CBFalpha1), and alkaline phosphatase (AP) for osteoblasts; tartrate-resistant acid phosphatase (TRAP) for osteoclasts; and the mineral regulators osteonectin (ON) and matrix Gla protein (MGP). The deposit center, periphery, adjacent connective tissue, and vascular endothelial cells were examined.. Alizarin red stained calcified deposits that did not localize with collagen, like bone, under polarized light. Hematoxylin and eosin stain revealed a paucity of connective tissue and absence of bone-like structures. The deposits, connective tissue, and vascular endothelial cells were positive for BSP, DPP, DMP1, and AP; MEPE was not detected. OC, ON, and MGP were present in the deposits and vascular endothelial cells; OPN and CBFalpha1 were present in deposits and connective tissue. TRAP-positive osteoclasts were localized to the calcification periphery.. The disorganized juvenile DM calcifications differ in structure, composition, and protein content from bone, suggesting that they may not form through an osteogenic pathway. Osteoclasts at the deposit surface represent an attempt to initiate its resolution.

Topics: Acid Phosphatase; Adolescent; Alkaline Phosphatase; Biomarkers; Calcinosis; Calcium-Binding Proteins; Child; Core Binding Factor Alpha 1 Subunit; Dermatomyositis; Extracellular Matrix Proteins; Female; Glycoproteins; Humans; Integrin-Binding Sialoprotein; Isoenzymes; Matrix Gla Protein; Osteoblasts; Osteocalcin; Osteoclasts; Osteogenesis; Osteonectin; Osteopontin; Phosphoproteins; Sialoglycoproteins; Tartrate-Resistant Acid Phosphatase

On the basis of previous (n = 23) and current muscle biopsies (n = 25) as well as five animal-experimental investigations, the paper deals with the cause and the manifestation of perifascicular muscle-fiber atrophy. A deteriorated trophic situation of the subfascial or marginal muscle fibers in patients suffering from immunocomplex vasculopathies in connection with a reduced supply of blood to the muscles is seen as the cause of the areactive weight loss (atrophy). This is accompanied by a considerably reduced capillary supply of blood to the muscle fibers. Even in normal conditions, the portion of collateral vessels and capillaries is lower in the subfascial region than in the center of the fascicle. When the blood supply is disturbed, the marginal fibers are in a trophic situation worse than that of the central muscle fibers. They become atrophied. In responsive patients, the muscle fibers regenerate and recapillarize during the convalescence period. This can be shown histochemically by means of the alkaline phosphatase reaction. The extent of perifascicular musclefiber atrophy can be fixed in quantitative terms by the method of Baumli and Mumenthaler. Where a second biopsy is indicated, results can be obtained regarding the changes in the perifascicular atrophy as a consequence of the therapy provided.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Animals; Basement Membrane; Biopsy; Capillaries; Child; Dermatomyositis; Female; Fluorescent Antibody Technique; Humans; Immune Complex Diseases; Immunoglobulins; Ischemia; Male; Middle Aged; Muscle, Smooth, Vascular; Muscles; Muscular Atrophy; Muscular Dystrophies; Myositis; Rats; Rats, Inbred Strains

Regenerating fibres from tibialis anterior muscles of mice and hamsters transplanted as minced fragments for 7 and 9 days respectively were compared for basophilia, ribonucleic acid (RNA) and acid phosphatase activity with fibres in muscles of patients with Duchenne muscular dystrophy, limb--girdle dystrophy and dermatomyositis. Normal muscles of mice, hamsters and humans were used as controls. In normal muscle fibres basophilia and RNA activity were restricted to the nuclei and acid phosphatase activity was occasionally observed in the nuclei, endomysial connective tissue and around muscle spindles. Diseased human muscle fibres were rich in acid phosphatase activity, the enzyme being most prominent in degenerating and basophilic fibres. When examined in serial sections, all basophilic fibres showed RNA and acid phosphatase activity. Similarly, all regenerating fibres in minced transplants which were basophilic to haematoxylin contained high RNA and acid phosphatase activity. It is suggested that basophilia in diseased human muscle fibres represents regeneration and that the lysosomes, as defined by acid phosphatase activity in these fibres, may be promoting their growth and differentiation by facilitating greater nucleocytoplasmic communication which ultimately could lead to protein synthesis.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Animals; Child; Child, Preschool; Cricetinae; Dermatomyositis; Female; Histocytochemistry; Humans; Infant; Lysosomes; Male; Mice; Middle Aged; Muscles; Muscular Dystrophies; Regeneration; RNA

Topics: Acetates; Acid Phosphatase; Adolescent; Adult; Child; Child, Preschool; Dermatomyositis; Glycoside Hydrolases; Hexosaminidases; Humans; Middle Aged; Muscles; Muscular Diseases; Muscular Dystrophies; Myositis; Myotonic Dystrophy; Surface-Active Agents

Topics: Acid Phosphatase; Alkaline Phosphatase; Arthritis, Rheumatoid; Collagen Diseases; Dermatomyositis; Humans; Lupus Erythematosus, Systemic; Nephritis; Neutrophils; Peroxidases; Prednisolone