@article {1094,
	title = {Cellular uptake of ribonuclease A relies on anionic glycans.},
	journal = {Biochemistry},
	volume = {49},
	year = {2010},
	month = {2010 Dec 21},
	pages = {10666-73},
	abstract = {<p>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.</p>
},
	keywords = {Affinity, Animals, Anions, Cattle, Cell Line, Cell Proliferation, CHO Cells, Chondroitin Sulfates, Chromatography, Cricetinae, Cricetulus, Flow Cytometry, Fluorescence, Glycoproteins, Glycosaminoglycans, Heparitin Sulfate, Humans, Mass, Matrix-Assisted Laser Desorption-Ionization, Microscopy, Molecular Weight, N-Acetylneuraminic Acid, Pancreatic, Polysaccharides, Protein Binding, Ribonuclease, Spectrometry},
	issn = {1520-4995},
	doi = {10.1021/bi1013485},
	author = {Chao, Tzu-Yuan and Lavis, Luke D and Raines, Ronald T}
}
