muscular dystrophies/protease

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The role of proteases in excitation-contraction coupling failure in muscular dystrophy.

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Duchenne muscular dystrophy (DMD) is one of the most frequent types of muscular dystrophy. Alterations in intracellular calcium (Ca(2+)) handling are thought to contribute to the disease severity in DMD, possibly due to the activation of Ca(2+)-activated proteases. The purpose of this study was

Serine protease in mice with hereditary muscular dystrophy.

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The activities of serine protease, cathepsin B1, ornithine aminotransferase, and aldolase in skeletal muscles of mice with hereditary muscular dystrophy and their normal litter mates were studied. In dystrophic muscle, the specific and total activities of serine protease were much higher than in

Successful treatment of murine muscular dystrophy with the protease inhibitor bestatin.

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Continued administration of the dipeptide protease inhibitor Bestatin to 34 mice with genetic muscular dystrophy from the onset of clinical deficit, cured about half of the animals within 3 months. Cessation of treatment in the recovered mice at age 4 months was not followed by relapse. Examinations

Calcium activated neutral proteases (milli- and micro-CANP) and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD).

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Calcium activated neutral protease (milli- and micro-forms) and its endogenous inhibitor have been quantified in muscle from Duchenne muscular dystrophy (DMD) patients. The specific activities of both the enzymes are found to be significantly elevated. Some of the properties studied indicate that

High molecular weight kininogen, the extracellular inhibitor of thiol proteases, is deficient in hamsters with muscular dystrophy.

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High molecular weight kininogen has been shown to be the principal plasma inhibitor of cellular thiol proteases including cathepsins B, H and L and calpains 1 and 2. Since these same enzymes have been reported to be elevated in animals with muscular dystrophy, we studied plasmas from hamsters with

Spectrin extractability from erythrocyte in Duchenne muscular dystrophies and the effect of proteases on erythrocyte ghosts.

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We studied the erythrocyte membrane proteins from patients with Duchenne muscular dystrophy (DMD) using SDS-polyacrylamide gel electrophoresis. Our observations were the following: (1) The electrophoretic densitogram of freshly prepared DMD-ghosts was similar to that of controls. After the

Treatment of mouse muscular dystrophy with the protease inhibitor pepstatin.

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Dystrophic mice were treated for 5 weeks beginning at 3 weeks of age with 20 ugm per day of pepstatin, a potent inhibitor of cathepsin D. Mortality was less and weight gain greater in pepstatin treated mice than in controls. Muscle bulk was greater and hind lamb contractures were reduced in treated

A drug inhibits the mitochondrial protease inducing calmitine deficiency in skeletal muscle of patients with Duchenne's muscular dystrophy and dy/dy dystrophic mice.

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This study demonstrates that the cause of calmitine deficiency in dy/dy dystrophic mice and patients with Duchenne's muscular dystrophy (DMD) is the same; i.e., the absence of an inhibitor of calmitine-specific mitochondrial protease. This inhibitor, which is present in control mice and control

Preclinical increase in activity of muscle microsomal trypsin-like protease in murine muscular dystrophy, C57BL/10-mdx.

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Preclinical alterations of protease activities in skeletal muscles from 10-day-old dystrophic mouse, C57BL/10-mdx, were examined by using 10 fluorogenic peptide substrates. Among the activities tested, only Boc-Val-Pro-Arg-MCA-hydrolyzing enzyme of the muscle microsomes showed an about 6-fold higher

Absence of a calmitine-specific protease inhibitor in skeletal muscle mitochondria of patients with Duchenne's muscular dystrophy.

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We studied the effect of mitochondrial extracts from skeletal muscle of patients with Duchenne's muscular dystrophy (DMD) on calmitine from the skeletal muscle of normal mice and control subjects. Our results clearly show the existence of an abnormal proteolytic activity of mitochondria from

Calcium-activated neutral protease from muscle and platelets of Duchenne muscular dystrophy cases.

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Calcium-activated neutral protease (CANP) has been purified from its endogenous inhibitor and its activity is monitored in the muscle of Duchenne Muscular Dystrophy (DMD) patients. The specific activity of the enzyme is found to be significantly higher as compared to normal. CANP from platelets of

Calcium activated neutral protease in blood cells from patients & carriers of Duchenne muscular dystrophy.

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As blood cells such as platelets, lymphocytes and erythrocytes from patients with Duchenne muscular dystrophy show evidence of membrane alterations and elevation of intra-cellular calcium, one of the calcium related changes i.e., the activity of calcium activated neutral protease (CANP) was

Therapeutic trial with protease inhibitor (leupeptin) in chicken muscular dystrophy. A histologic and histochemical study.

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For the purpose of observing the therapeutic benefit of protease inhibitors for progressive muscular dystrophy, a large quantity of doses of leupeptin of 10 mg/kg/day and 50 mg/kg/day were administered i.p. to male chickens afflicted with hereditary muscular dystrophy (line 413) for 4 months

Muscular dystrophy: inhibition of degeneration in vivo with protease inhibitors.

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The protease inhibitors leupeptin and pepstatin were used in vivo in genetically dystrophic chickens to determine their effects on the histological and biochemical changes observed in this disease. These compounds appear to delay the degeneration of muscle tissue which is characteristic of this

Cloning of cDNA encoding a regeneration-associated muscle protease whose expression is attenuated in cell lines derived from Duchenne muscular dystrophy patients.

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In the dystrophin-mutant mdx mouse, an animal model for Duchenne muscular dystrophy (DMD), damaged skeletal muscles are efficiently regenerated and thus the animals thrive. The phenotypic differences between DMD patients and the mdx mice suggest the existence of factors that modulate the muscle

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