Ir Genes pp 135-146 | Cite as

Biosynthesis and Genetics of Ia Antigens and Their Associated Invariant Chain

  • P. P. Jones
  • C. E. Day
  • D. King
  • J. McNicholas
  • E. Sung
Part of the Experimental Biology and Medicine book series (EBAM, volume 4)


Since the discovery of Ia antigens in 1974 a tremendous amount of information has been gathered on the structure, genetics and possible functions of these molecules. However, the finding in 1979 that Ia antigen immunopre- cipitates contain a third polypeptide chain, designated the Ia antigen-associated invariant chain (Ii) (1), raised new questions about the assembly, processing, and expression of Ia antigens. The Ii chain, a protein with a molecular weight of 31,000 and a pI greater than 8, is non- covalently-associated with both I-A and I-E subregioncontrolled Ia antigens (1). Recent studies have suggested that it has a rather unusual subcellular distribution. It appears to be associated with Ia chain complexes in the intracellular membranes but not in the plasma membrane (2,3) . Its carbohydrate side chains also differ from those of the α and β chains, containing mannose but not fucose (4) and lacking sialic acid (3), which suggests that the Li chain possesses only unprocessed high-mannose oligosaccharides.


Starch Hydrate Carbohydrate Citrate Electrophoresis 


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Copyright information

© The Humana Press Inc. 1983

Authors and Affiliations

  • P. P. Jones
    • 1
  • C. E. Day
    • 1
  • D. King
    • 1
  • J. McNicholas
    • 1
  • E. Sung
    • 1
  1. 1.Department of Biological SciencesStanford UniversityStanfordUSA

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