First Evidence for Occurrence of Galβ1-3GlcNAcβ1-4Man Unit in<i>N</i>-Glycans of Insect Glycoprotein: β1-3Gal and β1-4GlcNAc Transferases Are Involved in<i>N</i>…

Kimura, Yoshinobu; Tsumura, Kazunori; Kimura, M.; Okihara, Kiyoshi; Sugimoto, H.; Yamada, Hideo

doi:10.1271/bbb.67.1852

Cited by 8 publications

(10 citation statements)

References 11 publications

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“…During structural analysis of minor components of N-glycans linked to this royal jelly glycoprotein, we found an N-glycan bearing a galactose residue. Since the occurrence of a galactosyl residue in N-glycans of naturally occurring insect glycoproteins has hardly been reported so far, 1,4) we describe in this report the structural analysis of the galactosylated N-glycan and a glycopeptide bearing the N-glycans from the 350-kDa RJGP.…”

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confidence: 98%

“…Recently, we have found some hybrid and complex-type N-glycans bearing the Gal b1-3GlcNAc b1-4Man unit among total N-glycans prepared from the royal jelly glycoproteins mixtures, 1) although the identiˆcation of glycoprotein(s) bearing the b1-3 galactosylated N-glycan(s) has not been done. In our previous paper, 2) we showed that 350-kDa royal jelly glycoprotein (350-kDa RJGP or apisin 3) ), which stimulates the proliferation of human monocytes, 2) bears a typical high-mannose type oligosaccharide (Man9-5GlcNAc2) as major components of N-glycans.…”

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confidence: 99%

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350-kDa Royal Jelly Glycoprotein (Apisin), Which Stimulates Proliferation of Human Monocytes, Bears the β1-3GalactosylatedN-Glycan: Analysis of theN-Glycosylation Site

Kimura

Kimura²,

Tsumura³

et al. 2003

Bioscience, Biotechnology, and Biochemistry

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While doing a structural analysis of minor component N-glycans linked to 350-kDa royal jelly glycoprotein (RJGP), which stimulates the proliferation of human monocytes, we found that a Galbeta1-3GlcNAcbeta1-4Man unit occurs on the insect glycoprotein. The structure of the fluorescence-labeled N-glycan was analyzed by sugar component analysis, IS-MS, and (1)H-NMR. The structural analysis showed that the 350-kDa RJGP bears Galbeta1-3GlcNAcbeta1-4(GlcNAcbeta1-2)Manalpha1-3 (Manalpha1-3Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc, suggesting this insect glycoprotein is one of the substrates for both beta1-3 galactosyl and beta1-4 N-acetylglucosamininyl transferases. To our knowledge, this is the first report that succeeded in identifying an insect glycoprotein bearing the beta1-3 galactosylated N-glycan.

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confidence: 98%

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350-kDa Royal Jelly Glycoprotein (Apisin), Which Stimulates Proliferation of Human Monocytes, Bears the β1-3GalactosylatedN-Glycan: Analysis of theN-Glycosylation Site

Kimura

Kimura²,

Tsumura³

et al. 2003

Bioscience, Biotechnology, and Biochemistry

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“…The MALDI-TOF MS confirmed a high homology between the predominant RJ protein apalbumin2 and its minor homolog apalbumin2a. It revealed that apalbumin2a contains a truncated N-and C-termini as well as two fully occupied N-glycosylation sites, one of which carries complex type antennary structures that rarely occur in RJ proteins [31]. These differences might cause different biological activities of major apalbumin2 and its minor homolog apalbumin2a.…”

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confidence: 99%

Towards functional proteomics of minority component of honeybee royal jelly: The effect of post‐translational modifications on the antimicrobial activity of apalbumin2

et al. 2009

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This study illustrates multifunctionality of proteins of honeybee royal jelly (RJ) and how their neofunctionalization result from various PTMs of maternal proteins. Major proteins of RJ, designated as apalbumins belong to a protein family consisting of nine members with M(r) of 49-87 kDa and they are accompanied by high number of minority homologs derived from maternal apalbumins. In spite of many data on diversity of apalbumins, the molecular study of their individual minority homologous is still missing. This work is a contribution to functional proteomics of second most abundant protein of RJ apalbumin2 (M(r) 52.7 kDa). We have purified a minority protein from RJ; named as apalbumin2a, differ from apalbumin2 in M(r) (48.6 kDa), in N-terminal amino acids sequences - ENSPRN and in N-linked glycans. Characterization of apalbumin2a by LC-MALDI TOF/TOF MS revealed that it is a minority homolog of the major basic royal jelly protein, apalbumin2, carrying two fully occupied N-glycosylation sites, one with high-mannose structure, HexNAc2Hex9, and another carrying complex type antennary structures, HexNAc4Hex3 and HexNAc5Hex4. We have found that apalbumin2a inhibit growth of Paenibacillus larvae. The obtained data call attention to functional plasticity of RJ proteins with potential impact on functional proteomics in medicine.

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“…Royal jelly, one of the most famous health foods, contains many bioactive glycoproteins that can stimulate the proliferation of a human monocytic cell line or hepatocytes. 1,2) During structural and functional analysis of N-glycans linked to royal jelly glycoproteins, we found a 1-3 Gal-containing N-glycan, 3,4) suggesting that honeybee cells biosynthesize complex type N-glycans in addition to high-mannose type, hybrid type, and GalNAc-containing complex type N-glycans, [5][6][7][8] but recently we found complex type N-glycans bearing both galactose and GalNAc residues, suggesting the possibility of the presence of a tumor marker T-antigen unit. In this study, therefore, we analyzed the primary structure of -Gal/-GalNAc containing N-glycan.…”

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confidence: 91%

“…Liberated oligosaccharides were N-acetylated, desalted, and labeled with 2-aminopyridine, as described in our previous report. 3) The resulting PA-sugar chains were separated by reverse-phase (RP) HPLC using a Shiseido Capcell pak C18 MG column (10 Â 250 mm, Shiseido, Tokyo, Japan) ( Fig. 1-I).…”

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Tumor Antigen Occurs inN-Glycan of Royal Jelly Glycoproteins: Honeybee Cells Synthesize T-Antigen Unit inN-Glycan Moiety

Kimura

Ushijima

Maeda

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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In our previous paper (Kimura, Y., et al., Biosci. Biotechnol. Biochem., 67, 1852-1856, 2003), we found that a complex type N-glycans containing beta1-3 galactose residue occurs on royal jelly glycoproteins. During structural analysis of minor components of royal jelly N-glycans, we found complex type N-glycans bearing both galactose and N-acetylgalactosamine residues. Detailed structural analysis of pyridylaminated oligosaccharide revealed that the newly found N-glycan had a complex type structure harboring a tumor marker (T-antigen) unit: Galbeta1-3GalNAcbeta1-4GlcNAcbeta1-2Manalpha1-6 (Galbeta1-3GalNAcbeta1-4GlcNAcbeta1-2Manalpha1-3) Manbeta1-4GlcNAcbeta1-4GlcNAc. To our knowledge, this may be the first report of the presence of the T-antigen unit in the N-glycan moiety of eucaryotic glycoproteins.

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First Evidence for Occurrence of Galβ1-3GlcNAcβ1-4Man Unit inN-Glycans of Insect Glycoprotein: β1-3Gal and β1-4GlcNAc Transferases Are Involved inN…

Cited by 8 publications

References 11 publications

350-kDa Royal Jelly Glycoprotein (Apisin), Which Stimulates Proliferation of Human Monocytes, Bears the β1-3GalactosylatedN-Glycan: Analysis of theN-Glycosylation Site

350-kDa Royal Jelly Glycoprotein (Apisin), Which Stimulates Proliferation of Human Monocytes, Bears the β1-3GalactosylatedN-Glycan: Analysis of theN-Glycosylation Site

Towards functional proteomics of minority component of honeybee royal jelly: The effect of post‐translational modifications on the antimicrobial activity of apalbumin2

Tumor Antigen Occurs inN-Glycan of Royal Jelly Glycoproteins: Honeybee Cells Synthesize T-Antigen Unit inN-Glycan Moiety

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