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 language | English (US) |
|---|---|
| Pages (from-to) | 486-491 |
| Number of pages | 6 |
| Journal | Neurology |
| Volume | 32 |
| Issue number | 5 |
| State | Published - 1982 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Decreased structure-linked latency of lysosomal dipeptidyl aminopeptidase-I activity in Duchenne muscular dystrophy fibroblasts
AU - Davis, M. H.
AU - Gelman, Benjamin
AU - Gruenstein, E.
PY - 1982
Y1 - 1982
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020073381&partnerID=8YFLogxK
M3 - Article
C2 - 7200205
AN - SCOPUS:0020073381
VL - 32
SP - 486
EP - 491
JO - Neurology
JF - Neurology
SN - 0028-3878
IS - 5
ER -