Erythrocytes contain cytoplasmic glycoproteins. O-linked GlcNac on band 4.1

G. D. Holt, R. S. Haltiwanger, C. R. Torres, Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review

Abstract

Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex. Here we demonstrate that O-GlcNAc moieties are also added to human erythrocyte cytoplasmic proteins. Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose. The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques. The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on as yet unidentified 65-kDa protein. In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties. One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.

Original languageEnglish (US)
Pages (from-to)14847-14850
Number of pages4
JournalJournal of Biological Chemistry
Volume262
Issue number31
StatePublished - 1987

ASJC Scopus subject areas

  • Biochemistry

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