Glycosylation of Natural Human Neutrophil Gelatinase B and Neutrophil Gelatinase B-Associated Lipocalin
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- 作者：Pauline M. Rudd ; Taj S. Mattu ; Stefan Masure ; Tomas Bratt ; Philippe E. Van den Steen ; Mark R. Wormald ; Bernard Kü ; ster ; David J. Harvey ; Niels Borregaard ; Jo Van Damme ; Raymond A. Dwek ; and Ghisla
- 刊名：Biochemistry
- 出版年：1999
- 出版时间：October 19, 1999
- 年：1999
- 卷：38
- 期：42
- 页码：13937 - 13950
- 全文大小：216K
- 年卷期：v.38,no.42(October 19, 1999)
- ISSN：1520-4995
文摘
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 anynatural human MMP is available. Here, both gelatinase B and NGAL were purified from human peripheralblood neutrophils, and the entire contents of the released N- and O-glycan pools were analyzedsimultaneously using recently developed high-performance liquid chromatography-based technology. Theresults are discussed within the context of the domain structure of gelatinase B and a molecular model ofNGAL based on data from this study and the three-dimensional nuclear magnetic resonance (NMR) structureof the protein. More than 95% of the N-linked glycans attached to both gelatinase B and NGAL werepartially sialylated, core-fucosylated biantennary structures with and without outer arm fucose. The O-linkedglycans, which were estimated to comprise approximately 85% of the total sugars on gelatinase B, mainlyconsisted of type 2 cores with Gal
hars/beta2.gif" BORDER=0 ALIGN="middle">1,4GlcNAc (lactosamine) extensions, with or without sialic acid orouter arm fucose. This paper also contains the first report of O-linked glycans attached to NGAL. Althoughboth 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 thanthose on gelatinase B. In contrast to NGAL, gelatinase B contains a region rich in Ser, Thr, and Protypical of O-glycosylated mucin-like domains.
hars/beta2.gif" BORDER=0 ALIGN="middle">1,4GlcNAc (lactosamine) extensions, with or without sialic acid orouter arm fucose. This paper also contains the first report of O-linked glycans attached to NGAL. Althoughboth 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 thanthose on gelatinase B. In contrast to NGAL, gelatinase B contains a region rich in Ser, Thr, and Protypical of O-glycosylated mucin-like domains.