Structural characterisation of neutrophil glycans by ultra sensitive mass spectrometric glycomics methodology

被引：62

作者：

Babu, Ponnusamy ^{[1
]}

North, Simon J. ^{[1
]}

Jang-Lee, Jihye ^{[1
]}

Chalabi, Sara ^{[1
]}

Mackerness, Kathryn ^{[2
]}

Stowell, Sean R. ^{[3
]}

Cummings, Richard D. ^{[3
]}

Rankin, Sara ^{[2
]}

Dell, Anne ^{[1
]}

Haslam, Stuart M. ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, Fac Nat Sci, London SW7 2AZ, England

[2] Univ London Imperial Coll Sci Technol & Med, Fac Med, Dept Leukocyte Biol, Natl Heart & Lung Inst, London SW7 2AZ, England

[3] Emory Univ, Sch Med, Atlanta, GA 30322 USA

来源：

GLYCOCONJUGATE JOURNAL | 2009年 / 26卷 / 08期

基金：

英国惠康基金; 美国国家卫生研究院;

关键词：

Mass spectrometry; Neutrophil; Glycomics; Protein glycosylation; SELECTIN GLYCOPROTEIN LIGAND-1; LINKED OLIGOSACCHARIDE STRUCTURES; P-SELECTIN; PSGL-1; CELLS; GALECTIN-1; GLYCOSYLATION; INFLAMMATION; RECOGNITION; ANNOTATION;

D O I：

10.1007/s10719-008-9146-4

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：

Neutrophils are the most abundant white blood cells in humans and play a vital role in several aspects of the immune response. Numerous reports have implicated neutrophil glycosylation as an important factor in mediating these interactions. We report here the application of high sensitivity glycomics methodologies, including matrix assisted laser desorption ionisation (MALDI-TOF) and MALDI-TOF/TOF analyses, to the structural analysis of N- and O-linked carbohydrates released from two samples of neutrophils, prepared by two separate and geographically remote laboratories. The data produced demonstrates that the cells display a diverse range of sialylated and fucosylated complex glycans, with a high level of similarity between the two preparations.

引用

页码：975 / 986

页数：12

共 40 条

[11]

FUKUDA M, 1984, J BIOL CHEM, V259, P925

[12] Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra [J].

Goldberg, D ;

Sutton-Smith, M ;

Paulson, J ;

Dell, A .

PROTEOMICS, 2005, 5 (04) :865-875

[13] P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation [J].

Guyer, DA ;

Moore, KL ;

Lynam, EB ;

Schammel, CMG ;

Rogelj, S ;

McEver, RP ;

Sklar, LA .

BLOOD, 1996, 88 (07) :2415-2421

[14] Mass spectrometric analysis of N- and O-glycosylation of tissues and cells [J].

Haslam, Stuart M. ;

North, Simon J. ;

Dell, Anne .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 2006, 16 (05) :584-591

[15]

HASLETT C, 1985, AM J PATHOL, V119, P101

[16] Complete identification of E-selectin ligands on neutrophils reveals distinct functions of PSGL-1, ESL-1, and CD44 [J].

Hidalgo, Andres ;

Peired, Anna J. ;

Wild, Martin K. ;

Vestweber, Dietmar ;

Frenette, Paul S. .

IMMUNITY, 2007, 26 (04) :477-489

[17] Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses [J].

Hsu, DK ;

Yang, RY ;

Pan, ZX ;

Lu, L ;

Salomon, DR ;

Fung-Leung, WP ;

Liu, FT .

AMERICAN JOURNAL OF PATHOLOGY, 2000, 156 (03) :1073-1083

[18] A novel biological activity for galectin-1 - Inhibition of leukocyte-endothelial cell interactions in experimental inflammation [J].

La, M ;

Cao, TV ;

Cerchiaro, G ;

Chilton, K ;

Hirabayashi, J ;

Kasao, K ;

Oliani, SM ;

Chernajovsky, Y ;

Perretti, M .

AMERICAN JOURNAL OF PATHOLOGY, 2003, 163 (04) :1505-1515

[19] Immunodeficiency diseases caused by defects in phagocytes [J].

Lekstrom-Himes, JA ;

Gallin, JI .

NEW ENGLAND JOURNAL OF MEDICINE, 2000, 343 (23) :1703-1714

[20] MONOSPECIFIC AND COMMON GLYCOPROTEIN LIGANDS FOR E-SELECTIN AND P-SELECTIN ON MYELOID CELLS [J].

LENTER, M ;

LEVINOVITZ, A ;

ISENMANN, S ;

VESTWEBER, D .

JOURNAL OF CELL BIOLOGY, 1994, 125 (02) :471-481

← 1 2 3 4 →