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Åke Lernmark

Principal investigator

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Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding

Author

  • Christiane S Hampe
  • Lisa P Hammerle
  • Alberto Falorni
  • John D. Robertson
  • Åke Lernmark

Summary, in English

The role of K396 in the enzymatic catalysis and the antigenicity of the 65 kDa isoform of glutamate decarboxylase (GAD65) was analyzed using the K396R GAD65 mutant. GAD65 is a major autoantigen in Type 1 diabetes and autoantibodies directed to GAD65 are widely used markers for this disease. We found that (1) recombinant human GAD65 is fully enzymatically active; (2) the K396R mutation abolished GAD65 activity; and (3) the K396R mutant retained full antigenicity to GAD65 autoantibodies in serum from Type 1 diabetes patients, but not to polyclonal antibodies raised to the catalytic domain.

Publishing year

2001-01-19

Language

English

Pages

185-189

Publication/Series

FEBS Letters

Volume

488

Issue

3

Document type

Journal article

Publisher

Wiley-Blackwell

Keywords

  • Autoimmunity
  • Diabetes
  • Glutamate decarboxylase
  • Pyridoxal 5-phosphate

Status

Published

ISBN/ISSN/Other

  • ISSN: 0014-5793