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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1983 Feb;80(3):775–779. doi: 10.1073/pnas.80.3.775

Identification and characterization of cells deficient in the mannose 6-phosphate receptor: evidence for an alternate pathway for lysosomal enzyme targeting.

C A Gabel, D E Goldberg, S Kornfeld
PMCID: PMC393462  PMID: 6298775

Abstract

Newly synthesized lysosomal enzymes acquire phosphomannosyl units, which allow binding of the enzymes to the mannose 6-phosphate receptor and subsequent translocation to lysosomes. In some cell types, this sequence of events is necessary for the delivery of these enzymes to lysosomes. Using a slime mold lysosomal hydrolase as a probe, we have identified three murine cell lines that lack the receptor and one line that contains very low (3%) receptor activity. Each of these lines synthesizes the mannose 6-phosphate recognition marker on its lysosomal enzymes, but, unlike cell lines with high levels of receptor, the cells accumulate oligosaccharides containing phosphomonoesters. The receptor-deficient lines possess high levels of intracellular acid hydrolase activity, which is contained in dense granules characteristic of lysosomes. The data suggest that intracellular mechanisms independent of the mannose 6-phosphate receptor must exist in some cells for the delivery of acid hydrolases to lysosomal organelles.

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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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