Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens

B. L. Smith, G. M. Preston, F. A. Spring, D. J. Anstee, P. Agre

Research output: Contribution to journalArticlepeer-review

Abstract

Blood group antigens are structural variants in surface carbohydrate or amino acid polymorphisms on extracellular domains of membrane proteins. The red cell water channel-forming integral protein (Aquaporin CHIP) is a homotetramer with only one N-glycosylated subunit, however no CHIP-associated blood group antigens have yet been identified. Immunoblotting, monosaccharide composition analysis, and selective glycosidase digestions revealed that the CHIP-associated oligosaccharide contains ABH determinants and resembles a band 3-type glycan that cannot be cleaved from intact membranes by Peptide:N- glycosidase F. The molecular structure of the Colton antigens was previously unknown, but CHIP was selectively immunoprecipitated with anti-Coa or anti- Cob. The DNA sequence from Colton-typed individuals predicted that residue 45 is alanine in the Co(a+b-) phenotype and valine in the Co(a-b+) phenotype. The nucleotide polymorphism corresponds to a PIIMI endonuclease digestion site in the DNA from Co(a-b+) individuals. These studies have defined antigens within two blood group systems on CHIP: (a) an ABH-bearing polylactosaminoglycan attached to a poorly accessible site in the native membrane; and (b) the Colton antigen polymorphism which may permit the identification of rare individuals with defective water channel expression.

Original languageEnglish (US)
Pages (from-to)1043-1049
Number of pages7
JournalJournal of Clinical Investigation
Volume94
Issue number3
DOIs
StatePublished - 1994

Keywords

  • blood group antigens
  • erythrocyte membrane
  • membrane protein glycosylation
  • water channels

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint

Dive into the research topics of 'Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens'. Together they form a unique fingerprint.

Cite this