Expression of Long-form N-Acetylglucosamine-6-O-Sulfotransferase 1 in Human High Endothelial Venules

Maiko Fujiwara, Motohiro Kobayashi, Hitomi Hoshino, Kenji Uchimura, Tsutomu Nakada, Junya Masumoto, Yasuhiro Sakai, Minoru Fukuda, Jun Nakayama

研究成果: Article査読

8 被引用数 (Scopus)

抄録

Two members of the N-acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) family, GlcNAc6ST-1 and GlcNAc6ST-2, function in the biosynthesis of 6-sulfo sialyl Lewis X-capped glycoproteins expressed on high endothelial venules (HEVs) in secondary lymphoid organs. Thus, both enzymes play a critical role in L-selectin-expressing lymphocyte homing. Human GlcNAc6ST-1 is encoded by a 1593-bp open reading frame exhibiting two 5′ in-frame methionine codons spaced 141 bp apart. Both resemble the consensus sequence for translation initiation. Thus, it has been hypothesized that both long and short forms of GlcNAc6ST-1 may be present, although endogenous expression of either form has not been confirmed in humans. Here, the authors developed an antibody recognizing amino acid residues between the first two human GlcNAc6ST-1 methionines. This antibody specifically recognizes the long form of the enzyme, a finding validated by Western blot analysis and immunofluorescence cytochemistry of HeLa cells misexpressing long and/or short forms of human GlcNAc6ST-1. Using this antibody, the authors carried out immunofluorescence histochemistry of human lymph node tissue sections and found endogenous expression of the long form of the enzyme in human tissue, predominantly in the trans-Golgi network of endothelial cells that form HEVs.

本文言語English
ページ(範囲)397-407
ページ数11
ジャーナルJournal of Histochemistry and Cytochemistry
60
5
DOI
出版ステータスPublished - 05-2012
外部発表はい

All Science Journal Classification (ASJC) codes

  • 解剖学
  • 組織学

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