Glycosylation of Natural Human Neutrophil Gelatinase B and Neutrophil Gelatinase B-Associated Lipocalin
| Autor: | T Bratt, N Borregaard, S Masure, Taj S. Mattu, David Harvey, Pauline M. Rudd, Raymond A. Dwek, Ghislain Opdenakker, P. E. Van den Steen, J Van Damme, Bernhard Kuster, Mark R. Wormald |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Glycan Glycosylation Neutrophils Molecular Sequence Data Oligosaccharides Context (language use) Lipocalin Biochemistry Fucose Amidohydrolases chemistry.chemical_compound Lipocalin-2 Fibroblast activation protein alpha Polysaccharides Proto-Oncogene Proteins Carbohydrate Conformation Humans Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Gelatinase Computer Simulation Oncogene Proteins biology Molecular biology Lipocalins Sialic acid Carbohydrate Sequence Matrix Metalloproteinase 9 chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Electrophoresis Polyacrylamide Gel Carrier Proteins Acute-Phase Proteins |
| Zdroj: | Rudd, P, Mattu, T, Masure, S, Bratt, T, Van Den Steen, P, Wormald, M, Küster, B, Harvey, D, Borregaard, N, Van Damme, J, Dwek, R & Opdenakker, G 1999, ' Glycosylation of natural human neutrophil Gelatinase B and neutrophil gelatinase B-associated lipocalin ', Biochemistry, vol. 38, pp. 13937-13950 . |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi991162e |
| Popis: | Gelatinase B is a matrix metalloproteinase (MMP-9) involved in tissue remodeling, development, cancer, and inflammation. Neutrophils produce three major forms of (pro)gelatinase B: 92 kDa monomers, homodimers, and complexes of gelatinase B covalently bound to neutrophil gelatinase B-associated lipocalin (NGAL). In contrast to the case for other proteinases, little information about the glycosylation of any natural human MMP is available. Here, both gelatinase B and NGAL were purified from human peripheral blood neutrophils, and the entire contents of the released N- and O-glycan pools were analyzed simultaneously using recently developed high-performance liquid chromatography-based technology. The results are discussed within the context of the domain structure of gelatinase B and a molecular model of NGAL based on data from this study and the three-dimensional nuclear magnetic resonance (NMR) structure of the protein. More than 95% of the N-linked glycans attached to both gelatinase B and NGAL were partially sialylated, core-fucosylated biantennary structures with and without outer arm fucose. The O-linked glycans, which were estimated to comprise approximately 85% of the total sugars on gelatinase B, mainly consisted of type 2 cores with Galbeta1,4GlcNAc (lactosamine) extensions, with or without sialic acid or outer arm fucose. This paper also contains the first report of O-linked glycans attached to NGAL. Although both proteins were isolated from neutrophils and contained O-linked glycans mainly with type 2 cores, the glycans attached to individual serine/threonine residue(s) in NGAL were significantly smaller than those on gelatinase B. In contrast to NGAL, gelatinase B contains a region rich in Ser, Thr, and Pro typical of O-glycosylated mucin-like domains. |
| Databáze: | OpenAIRE |
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