Mannose receptor-mediated regulation of serum glycoprotein homeostasis

被引：382

作者：

Lee, SJ

Evers, S

Roeder, D

Parlow, AF

Risteli, J

Risteli, L

Lee, YC

Feizi, T

Langen, H

Nussenzweig, MC

机构：

[1] Rockefeller Univ, Lab Mol Immunol, New York, NY 10021 USA

[2] F Hoffmann La Roche & Co Ltd, Infect Dis, CH-4070 Basel, Switzerland

[3] F Hoffmann La Roche & Co Ltd, Genet, CH-4070 Basel, Switzerland

[4] Univ Calif Los Angeles, Harbor Med Ctr, Natl Hormone & Pituitary Program, Torrance, CA 90509 USA

[5] Univ Oulu, Dept Clin Chem, FIN-90014 Oulu, Finland

[6] Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA

[7] Univ London Imperial Coll Sci Technol & Med, Fac Med, Northwick Pk Inst Med Res, Glycosci Lab, Harrow HA1 3UJ, Middx, England

[8] Howard Hughes Med Inst, New York, NY 10021 USA

来源：

SCIENCE | 2002年 / 295卷 / 5561期

关键词：

D O I：

10.1126/science.1069540

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Carbohydrates are thought to function as tags that mark circulatory glycoproteins for rapid clearance. To examine the role of the mannose receptor (MR) in glycoprotein clearance, we generated mice genetically deficient in MR. MR-/- mice were defective in clearing proteins bearing accessible mannose and N-acetylglucosamine residues and had elevated levels of eight different lysosomal hydrolases. Proteomic analysis of MR-/- and control mouse sera showed that an additional 4 out of 52 proteins identified were elevated in MR-/- serum. Each of these is up-regulated during inflammation and wound heating. Thus, MR appears to operate as an essential regulator of serum glycoprotein homeostasis.

引用

页码：1898 / 1901

页数：4

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