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Originally published In Press as doi:10.1074/jbc.M009361200 on January 30, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16739-16748, May 18, 2001
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Characterization of the Glycosylation Profiles of Alzheimer's beta -Secretase Protein Asp-2 Expressed in a Variety of Cell Lines*

Joanne CharlwoodDagger , Colin Dingwall§, Rosalie Matico, Ishrut Hussain§, Kyung Johanson, Stephen Moore§, David J. Powell||, J. Mark SkehelDagger , Steve Ratcliffe**, Brian Clarke**, John TrillDagger Dagger , Sharon SweitzerDagger Dagger §§, and Patrick CamilleriDagger ¶¶

From the Dagger  Department of Analytical Sciences, SmithKline Beecham Pharmaceuticals, Harlow, Essex CM19 5AW, United Kingdom, the § Department of Neurociences, SmithKline Beecham Pharmaceuticals, Harlow, Essex CM19 5AW, United Kingdom, the  Department of Protein Biochemistry, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406, the || Department of Molecular Screening Technologies, SmithKline Beecham Pharmaceuticals, Harlow, Essex CM19 5AW, United Kingdom, the ** Department of Computational and Structural Sciences, SmithKline Beecham Pharmaceuticals, Harlow, Essex CM19 5AW, United Kingdom, and the Dagger Dagger  Department of Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406

Amyloid 39-42 beta  -peptides are the main components of amyloid plaques found in the brain of Alzheimer's disease patients. Amyloid 39-42 beta -peptide is formed from amyloid precursor protein by the sequential action of beta - and gamma -secretases. Asp-2 is a transmembrane aspartic protease expressed in the brain, shown to have beta -secretase activity. Mature Asp-2 has four N-glycosylation sites. In this report we have characterized the carbohydrate structures in this glycoprotein expressed in three different cell lines, namely Chinese hamster ovary, CV-1 origin of SV40, and baculovirus-infected SF9 cells. Biantennary and triantennary oligosaccharides of the "complex" type were released from glycoprotein expressed in the mammalian cells, whereas mannose-rich glycans were identified from glycoprotein synthesized in the baculovirus-infected cells. Site-directed mutagenesis of the asparagine residues at amino acid positions 153, 172, 223, and 354 demonstrate that the protease activity of Asp-2 is dependent on its glycosylation.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§§ To whom correspondence may be addressed: Dept. of Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, 709 Swedeland Rd., King of Prussia, PA 19406. Tel.: 610-270-7208; Fax: 610-270-4091; E-mail: sharon_m_sweitzer@sbphrd.com.

¶¶ To whom correspondence may be addressed: Dept. of Analytical Sciences, SmithKline Beecham Pharmaceuticals, New Frontiers Science Park, Third Avenue, Harlow, Essex CM19 5AW, United Kingdom. Tel.: 44-1279-622026; Fax: 44-1279-627427; E-mail: patrick_camilleri@sbphrd.com.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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