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. 1982 Jan 15;202(1):183–190. doi: 10.1042/bj2020183

Defective catabolism of low-density lipoprotein by fibroblasts from patients with I-cell disease.

J C Williams, D B Weinstein, A L Miller, D Steinberg
PMCID: PMC1158089  PMID: 7082306

Abstract

Skin fibroblast cultures from patients with I-cell disease (mucolipidosis II) are characterized by multiple lysosomal enzyme deficiencies The present studies deal with the consequences of these deficiencies with respect to the metabolism of plasma low-density lipoproteins. Degradation of the protein moiety was defective in I-cells compared with control cells, but the binding and internalization of low density lipoprotein were much less affected. Measurements of low-density lipoprotein degradation in homogenates demonstrated directly for the first time a deficiency of acid proteinase activity in I-cell fibroblasts. Comparison of results in 6-h incubations with those in 24-h incubations showed accumulation of intracellular low-density lipoprotein in I-cell fibroblasts and an accelerating rate of degradation, possibly attributable to intracellular accumulation of low-density lipoprotein substrate. The significance of these findings with respect to low-density lipoprotein metabolism in vivo is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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