Decreased structure-linked latency of lysosomal dipeptidyl aminopeptidase-I activity in Duchenne muscular dystrophy fibroblasts

M. H. Davis, Benjamin Gelman, E. Gruenstein

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Crude lyosomal pellets were prepared from skin fibroblasts grown from patients having Duchenne muscular dystrophy, and from normal controls. Disruption of the lysosomes by nonionic detergents resulted in the expression of latent activity of the enzyme dipeptidyl aminopeptidase-I(DAP-I). Duchenne lysosomes showed less structure-linked latency than those from normal controls, and sedimentation studies demonstrated that the difference was not caused by increased leakage of the enzyme from lyosomes. Permeability properties of the lysosomes for an artificial substrate revealed no difference of the apparent K(m). However, in intact lysosomes the apparent K(a) for Cl- of this chloride-requiring enzyme was found to be lower in DMD lysosomes. The apparent increase in entry of Cl- was closely related with the decreased amount of the DAP-I latency. High concentrations of extra-lysosomal Cl- correlated the abnormality.

Original languageEnglish (US)
Pages (from-to)486-491
Number of pages6
JournalNeurology
Volume32
Issue number5
StatePublished - 1982
Externally publishedYes

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Cathepsin C
Duchenne Muscular Dystrophy
Lysosomes
Fibroblasts
Enzymes
Detergents
Chlorides
Permeability
Skin

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Decreased structure-linked latency of lysosomal dipeptidyl aminopeptidase-I activity in Duchenne muscular dystrophy fibroblasts. / Davis, M. H.; Gelman, Benjamin; Gruenstein, E.

In: Neurology, Vol. 32, No. 5, 1982, p. 486-491.

Research output: Contribution to journalArticle

Davis, M. H. ; Gelman, Benjamin ; Gruenstein, E. / Decreased structure-linked latency of lysosomal dipeptidyl aminopeptidase-I activity in Duchenne muscular dystrophy fibroblasts. In: Neurology. 1982 ; Vol. 32, No. 5. pp. 486-491.
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