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Biochemistry. 2010 Dec 21;49(50):10666-73. doi: 10.1021/bi1013485. Epub 2010 Nov 23.

Cellular uptake of ribonuclease A relies on anionic glycans.

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1
Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706, United States.

Abstract

Bovine pancreatic ribonuclease (RNase A) can enter human cells, even though it lacks a cognate cell-surface receptor protein. Here, we report on the biochemical basis for its cellular uptake. Analyses in vitro and in cellulo revealed that RNase A interacts tightly with abundant cell-surface proteoglycans containing glycosaminoglycans, such as heparan sulfate and chondroitin sulfate, as well as with sialic acid-containing glycoproteins. The uptake of RNase A correlates with cell anionicity, as quantified by measuring electrophoretic mobility. The cellular binding and uptake of RNase A contrast with those of Onconase, an amphibian homologue that does not interact tightly with anionic cell-surface glycans. As anionic glycans are especially abundant on human tumor cells, our data predicate utility for mammalian ribonucleases as cancer chemotherapeutic agents.

PMID:
21062061
PMCID:
PMC3032661
DOI:
10.1021/bi1013485
[Indexed for MEDLINE]
Free PMC Article
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