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.


Sialic Acid House Mouse Electrophoretic Variant Backcross Mouse Carbohydrate Side Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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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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