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J. Biol. Chem., Vol. 278, Issue 8, 5613-5621, February 21, 2003

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Initiation of O-Glycan Synthesis in IgA1 Hinge Region Is Determined by a Single Enzyme, UDP-N-Acetyl--D-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase 2^*

Hiroko Iwasaki^§, Yan Zhang, Kahori Tachibana, Masanori Gotoh^§, Norihiro Kikuchi^¶, Yeon-Dae Kwon^¶, Akira Togayachi, Takashi Kudo, Tomomi Kubota, and Hisashi Narimatsu^**

From the  Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Open Space Laboratory C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, ^§ Amersham Biosciences KK, 3-25-1, Hyakunincho, Shinjuku-ku, Tokyo 169-0073, ^¶ Mitsui Knowledge Industry Co., Ltd., Honcho 1-32-2, Nakano-ku, Tokyo 164-8721, and  New Energy and Industrial Technology Development Organization, Sunshine 60 Building, 3-1-1, Higashi Ikebukuro, Toshima-ku, Tokyo 170-6028, Japan

The hinge region of human immunoglobulin A1 (*IgA1) possesses multiple O-glycans, of which synthesis is initiated by the addition of GalNAc to serine or threonine through the activity of UDP-N-acetyl--D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (pp-GalNAc-Ts). We found that six pp-GalNAc-Ts, pp-GalNAc-T1, -T2, -T3, -T4, -T6, and -T9, were expressed in B cells, IgA-bearing B cells, and NCI-H929 IgA myeloma cells. pp-GalNAc-T activities of these six enzymes for a synthetic IgA hinge peptide, which has nine possible O-glycosylation sites, were examined using a reversed phase-high performance liquid chromatography, a matrix-assisted laser desorption ionization time of flight mass spectrometry, and peptide sequencing analysis. pp-GalNAc-T2 showed the strongest activity transferring GalNAc to a maximum of eight positions. Other pp-GalNAc-Ts exhibited different substrate specificities from pp-GalNAc-T2; however, their activities were extremely weak. It was reported that the IgA1 hinge region possesses a maximum of five O-glycans, and their amino acid positions have been determined. We found that pp-GalNAc-T2 selectively transferred GalNAc residues to the same five positions. These results strongly suggested that pp-GalNAc-T2 is an essential enzyme for initiation of O-linked glycosylation of the IgA1 hinge region.

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