Enzyme Studies in Muscular Dystrophy. III. In Hereditary Muscular Dystrophy in Mice.

Weinstock, I.M.; Epstein, Sandra; Milhorat, A. T.

doi:10.3181/00379727-99-24320

Cited by 72 publications

(15 citation statements)

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“…This occurs in denervation atrophy in various species [15,21], in nutritional muscular dystrophy in the rabbit [22] and in inherited muscular dystrophy in the mouse [20], and chicken [18]. Furthermore, an increase in alkaline cathepsin activity also occurs in mouse dystrophic muscle [13].…”

Section: Sliwinski Doty and Landmannmentioning

confidence: 99%

Cathepsin Activity in Normal and Dystrophic Human Muscle

Je²

1968

Enzymol Biol Clin

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Section: Sliwinski Doty and Landmannmentioning

confidence: 99%

Cathepsin Activity in Normal and Dystrophic Human Muscle

Je²

1968

Enzymol Biol Clin

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“…An increased acid cathepsin activity has been found in muscular dystrophies of both nutritional [4,8,17,19] and genetic origin [4,16,18], and in denervation atrophy in various species [3,5]. Human muscle was found to have cathepsin activity against myoglobin substrate over a wide pH range, with peaks at 3.9 and 6.6.…”

Section: Introductionmentioning

confidence: 99%

Acid, Neutral and Alkaline Cathepsins in Normal and Diseased Human Muscle

Nc¹,

Cm²

1972

Enzyme

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Homogenates of human skeletal muscle showed autolytic and cathepsin activity over a wide pH range with peaks at 3.6, 6.6 and 8.6. Some evidence was presented for the enzymatic and proteolytic nature of the autolytic process. Both myoglobin and hemoglobin were equally active as substrates at all pH peaks. In mildly abnormal muscle of patients with Duchenne muscular dystrophy, other dystrophies, dermatomyositis and neurogenic atrophies, both autolytic and cathepsin activity in the acid, neutral and alkaline range were either normal or slightly above normal. On the other hand, in severely degenerated muscles of patients with the same disease conditions, large increases in autolytic and cathepsin activity at all pH peaks were found. The increased activity of cathepsins was found to correlate with the degree of muscle degeneration. These results suggest that the cathepsins are involved in the muscle wasting process in human muscle diseases.

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“…The activity of certain of these enzymes, as measured by the ability of tissue pre parations to hydrolyze hemoglobin or synthetic peptides, has been shown to be greatly elevated in muscular dystrophies of both nutri tional and genetic origin [5,6,11,13,14,15]. Although the cathepsins and other lysosomal acid hydrolases have been implicated as a major factor in tissue catabolism [1], the present state of our knowledge does not yet permit a rational explanation of the enzymatic mechanisms responsible for the loss of muscle protein in dystrophic muscle or for protein catabolism in general.…”

mentioning

confidence: 99%

Proteolytic Activity of Skeletal Muscle of Normal and Dystrophic Chickens and Rabbits

Aa¹,

Leong²,

Im³

1966

Enzymol Biol Clin

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Summary. Autolysis of skeletal muscle of rabbits and chickens was demonstrated by a colorimetric ninhydrin procedure. Evidence is presented for the enzymatic and proteolytic nature of the reaction. In skeletal muscle of chickens with a hereditary form of muscular dystrophy or of rabbits with muscular dystrophy resulting from a vitamin E-deficiency, large increases in autolytic activity were found. Autolytic activity was also increased several fold by the addition of purified muscle cathepsin D which indicates that this enzyme is probably involved in autolysis of muscle. These studies suggest that the elevation in the activity of the proteolytic enzymes may be a major factor in the muscle-wasting process characteristic of muscular dystrophy.

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Enzyme Studies in Muscular Dystrophy. III. In Hereditary Muscular Dystrophy in Mice.

Cited by 72 publications

References 0 publications

Cathepsin Activity in Normal and Dystrophic Human Muscle

Cathepsin Activity in Normal and Dystrophic Human Muscle

Acid, Neutral and Alkaline Cathepsins in Normal and Diseased Human Muscle

Proteolytic Activity of Skeletal Muscle of Normal and Dystrophic Chickens and Rabbits

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