Post-translational modifications of immunoglobulin G:: a mouse IgG variant that lacks the entire CH1 domain

被引：6

作者：

Masuda, K ^{[1
]}

Yamaguchi, Y

Kato, K

Kim, H

Takahashi, N

Shimada, I

Arata, Y

机构：

[1] Suntory Inst Bioorgan Res, Shimamoto, Osaka 6188503, Japan

[2] Meijo Univ, Fac Pharm, Tempaku Ku, Nagoya, Aichi 4688503, Japan

[3] Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyo Ku, Tokyo 1130033, Japan

[4] Nakano Vinegar Co Ltd, Glyco Lab, Aichi 4758586, Japan

[5] Water Res Inst, Tsukuba, Ibaraki 3050047, Japan

来源：

MOLECULAR IMMUNOLOGY | 1999年 / 36卷 / 15-16期

关键词：

IgG; hinge region; post-translational modification; O-glycosylation; mass spectrometry;

D O I：

10.1016/S0161-5890(99)00131-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In the present study, we characterized the post-translational modifications of a short-chain variant of mouse IgG2a that lacks the entire C(H)1 domain. The short-chain IgG2a and its proteolytic fragments were subjected to electrosplay ionization- and fast atom bombardment-mass spectrometric analyses. It has been demonstrated that approximately 14% of the heavy chain of the short-chain IgG2a is O-glycosylated with a disaccharide of Gal-GalNAc- at Thr220A in the hinge region, while the O-glycosylation does not occur in its parent IgG2a molecule. Two additional modifications have been detected at the C-termini of both the heavy and light chains of the short-chain IgG2a. Biological significance of the post-translational modifications of the short-chain IgG2a variant is briefly discussed. (C) 2000 Elsevier Science Ltd. AU rights reserved.

引用

页码：993 / 1003

页数：11

共 24 条

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IGARASHI, T
SATO, M
KATSUBE, Y
TAKIO, K
TANAKA, T
NAKANISHI, M
ARATA, Y
BIOCHEMISTRY, 1990, 29 (24) : 5727 - 5733
[2] Post-translational structural modifications of immunoglobulin G and their effect on biological activity
Laura K. Hmiel
Kurt A. Brorson
Michael T. Boyne
Analytical and Bioanalytical Chemistry, 2015, 407 : 79 - 94
[3] Post-translational structural modifications of immunoglobulin G and their effect on biological activity
Hmiel, Laura K.
Brorson, Kurt A.
Boyne, Michael T., II
ANALYTICAL AND BIOANALYTICAL CHEMISTRY, 2015, 407 (01) : 79 - 94
[4] Post-translational Modifications Differentially Affect IgG1 Conformation and Receptor Binding
Houde, Damian
Peng, Yucai
Berkowitz, Steven A.
Engen, John R.
MOLECULAR & CELLULAR PROTEOMICS, 2010, 9 (08) : 1716 - 1728
[5] The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
Starkova, T. Yu.
Artamonova, T. O.
Ermakova, V. V.
Chikhirzhina, E. V.
Khodorkovskii, M. A.
Tomilin, A. N.
ACTA NATURAE, 2019, 11 (02): : 82 - 91
[6] Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CH1 Domain Deletion
Yanaka, Saeko
Nishiguchi, Shigetaka
Yogo, Rina
Watanabe, Hiroki
Shen, Jiana
Yagi, Hirokazu
Uchihashi, Takayuki
Kato, Koichi
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2022, 23 (04)
[7] Mapping post-translational modifications of the histone variant macroH2A1 using tandem mass spectrometry
Chu, FX
Nusinow, DA
Chalkely, RJ
Plath, K
Panning, B
Burlingame, AL
MOLECULAR & CELLULAR PROTEOMICS, 2006, 5 (01) : 194 - 203
[8] Mapping post-translational modifications of the histone variant macroH2A1 using tandem mass spectrometry
Chu, F
Nusinow, DA
Chalkley, RJ
Plath, K
Panning, B
Burlingame, AL
FASEB JOURNAL, 2006, 20 (04): : A529 - A529
[9] Post-translational modifications of HTLV-1 Tax carboxy-terminal domain: role in cellular transformation
Julie Lodewick
Anne Sophie Rinaldi
Françoise Bex
Retrovirology, 11 (Suppl 1)
[10] Loss of splice consensus signal is responsible for the removal of the entire CH1 domain of the functional camel IGG2A heavy-chain antibodies
Nguyen, VK
Hamers, R
Wyns, L
Muyldermans, S
MOLECULAR IMMUNOLOGY, 1999, 36 (08) : 515 - 524

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