Localization of a pernicious anaemia autoantibody epitope on the alpha-subunit of human H,K-adenosine triphosphatase

Scandinavian Journal of Gastroenterology
Y H SongA M McGregor

Abstract

Four cDNA fragments encoding different portions of the alpha-subunit of human H,K-adenosine triphosphatase (ATPase) were amplified by means of the polymerase chain reaction technique, ligated into the plasmid pGEX-2T, and expressed as glutathione S-transferase fusion proteins in Escherichia coli. The fragments A (residues 163-313), Ba (residues 360-797), Bb (residues 526-797), and C (residues 822-1031) together encompass 77% of the alpha-subunit and cover most of its cytosolic part. The reactivities of autoantibodies in the sera from patients with pernicious anaemia with the recombinant fusion proteins were analysed by immunoblotting. One autoantigenic epitope was found in the NH2-terminal part of the Ba fragment--that is, between residues 360 and 525. No epitope was detected in the other fragments. The Ba fragment was cleaved off from the glutathione S-transferase fusion protein by the action of thrombin and was then further purified. By means of enzyme-linked immunosorbent assay, 28 of 42 sera (67%) from patients with pernicious anaemia were positive against the purified Ba fragment. The present results provide a final proof that the human H,K-ATPase alpha-subunit is a major autoantigen in the parietal cell and that the major...Continue Reading

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Citations

May 1, 1996·Immunology Today·Y H SongN K Maclaren
May 2, 2002·Clinica Chimica Acta; International Journal of Clinical Chemistry·Erik MårdhKurt Borch
Feb 20, 2002·Journal of Gastroenterology and Hepatology·K Dohmen
May 1, 2002·European Journal of Gastroenterology & Hepatology·Masanori ItoKazuaki Chayama
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Jul 11, 2020·Nature Reviews. Disease Primers·Marco Vincenzo LentiAntonio Di Sabatino

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