Temporal analysis of N-acetylglucosamine extension of N-glycans in the middle silk gland of silkworm Bombyx mori.

Autor: Kajiura H; International Center for Biotechnology, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan; Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan., Eguchi T; International Center for Biotechnology, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan., Uchino K; Division of Silk-Producing Insect Biotechnology, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan., Tatematsu KI; Division of Silk-Producing Insect Biotechnology, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan., Tamura T; Division of Silk-Producing Insect Biotechnology, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan., Sezutsu H; Division of Silk-Producing Insect Biotechnology, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan., Fujiyama K; International Center for Biotechnology, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan; Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan; Osaka University Cooperative Research Station in Southeast Asia (OU:CRS), Faculty of Science, Mahidol University, Bangkok 10400, Thailand. Electronic address: fujiyama@icb.osaka-u.ac.jp.
Jazyk: angličtina
Zdroj: Journal of bioscience and bioengineering [J Biosci Bioeng] 2022 Jun; Vol. 133 (6), pp. 533-540. Date of Electronic Publication: 2022 Apr 06.
DOI: 10.1016/j.jbiosc.2022.03.001
Abstrakt: N-glycosylation of proteins is an important post-translational modification in eukaryotic cells. One of the key modifications in protein N-glycosylation is N-acetylglucosamine (GlcNAc) extension mediated by N-acetylglucosaminyltransferase I (GNTI), which triggers N-glycan maturation from high-mannose-type to hybrid- and complex-type structures in Golgi. However, the temporal contributions of GNTI to GlcNAc extension and the resultant N-glycan structures in insects have not been analyzed. Here, focusing on GlcNAc extension of N-glycan in the silkworm Bombyx mori, we analyzed the temporal N-glycan alterations in the middle silk gland (MSG) and characterized the property of key enzyme for complex-type N-glycan biosynthesis, B. mori GNTI (BmGNTI). N-glycan analysis of N-glycoproteins in the MSG demonstrated that BmGNTI identified and characterized in this study consistently contributed to GlcNAc extension of N-glycans, which led to the accumulation of GlcNAc-extended N-glycans as predominant structures throughout the MSG development. The expression profile of GlcNAc extension-related genes revealed that the enzymes contributing to the hydrolysis of GlcNAc showed stage-specific expressions, thereby resulting in accumulations of the end product N-glycans of the enzyme. These results lead to the speculation that not BmGNTI but rather glycosylhydrolases critically influenced the structural formations and the changes in the ratio of N-glycans with GlcNAc residue(s) in MSG.
(Copyright © 2022 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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