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• W1974932783 abstract "It has been reported that besides defects in the phosphorylation such as in the I-cell disease, a failure in the uncovering of mannose 6-phosphate residues may result in an increase of lysosomal enzyme activities in serum [Alexander et al., Hum. Genet. 73, 53-59 (1986)]. We examined fibroblasts that were derived from the original biopsy, observed an enhanced secretion of lysosomal enzymes including cathepsin D, but found that both the phosphorylation and uncovering of mannose 6-phosphate residues were normal. The enhanced secretion of cathepsin D was characterized by an increase in the secretion of phosphorylated molecules that were sensitive to a treatment with alkaline phosphatase. The enhanced secretion of the phosphatase-sensitive form of procathepsin D was further increased in the presence of antibodies directed to cation-independent mannose 6-phosphate receptors. In contrast, antibodies specific to cation-dependent mannose 6-phosphate receptors selectively inhibited the secretion of the phosphatase-sensitive procathepsin D molecules. A chromatographic analysis of oligosaccharides from the secreted procathepsin D confirmed that the cells secrete proenzyme molecules rich in oligosaccharides with two uncovered phosphate residues. It is suggested that the enhanced secretion of procathepsin D in the variant fibroblasts results from an abnormal sorting rather than processing of phosphorylated lysosomal enzymes." @default.
• W1974932783 created "2016-06-24" @default.
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• W1974932783 creator A5032867939 @default.
• W1974932783 creator A5091738586 @default.
• W1974932783 date "1998-10-01" @default.
• W1974932783 modified "2023-10-14" @default.
• W1974932783 title "Abnormal lysosomal sorting with an enhanced secretion of cathepsin D precursor molecules bearing monoester phosphate groups" @default.
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• W1974932783 doi "https://doi.org/10.1016/s0171-9335(98)80081-2" @default.
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• W1974932783 hasPublicationYear "1998" @default.
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