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rdf:type |
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lifeskim:mentions |
umls-concept:C0007600,
umls-concept:C0017262,
umls-concept:C0017982,
umls-concept:C0033684,
umls-concept:C0171484,
umls-concept:C0330390,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C1880022,
umls-concept:C1883525,
umls-concept:C1979963,
umls-concept:C2003903,
umls-concept:C2346866
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pubmed:issue |
20
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pubmed:dateCreated |
2001-5-23
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid Precursor Protein Secretases,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/BACE1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BACE2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:CamilleriPP,
pubmed-author:CharlwoodJJ,
pubmed-author:ClarkeBB,
pubmed-author:DingwallCC,
pubmed-author:HussainII,
pubmed-author:JohansonKK,
pubmed-author:MaticoRR,
pubmed-author:MooreSS,
pubmed-author:PowellD JDJ,
pubmed-author:RatcliffeSS,
pubmed-author:SkehelJ MJM,
pubmed-author:SweitzerSS,
pubmed-author:TrillJJ
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16739-48
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11278492-Alzheimer Disease,
pubmed-meshheading:11278492-Amyloid Precursor Protein Secretases,
pubmed-meshheading:11278492-Animals,
pubmed-meshheading:11278492-Aspartic Acid Endopeptidases,
pubmed-meshheading:11278492-Brain,
pubmed-meshheading:11278492-CHO Cells,
pubmed-meshheading:11278492-Carbohydrate Conformation,
pubmed-meshheading:11278492-Carbohydrate Sequence,
pubmed-meshheading:11278492-Cell Line,
pubmed-meshheading:11278492-Cricetinae,
pubmed-meshheading:11278492-Endopeptidases,
pubmed-meshheading:11278492-Glycoproteins,
pubmed-meshheading:11278492-Glycosylation,
pubmed-meshheading:11278492-Humans,
pubmed-meshheading:11278492-Molecular Sequence Data,
pubmed-meshheading:11278492-Oligosaccharides,
pubmed-meshheading:11278492-Polysaccharides,
pubmed-meshheading:11278492-Recombinant Proteins,
pubmed-meshheading:11278492-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:11278492-Spodoptera,
pubmed-meshheading:11278492-Transfection
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pubmed:year |
2001
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pubmed:articleTitle |
Characterization of the glycosylation profiles of Alzheimer's beta -secretase protein Asp-2 expressed in a variety of cell lines.
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pubmed:affiliation |
Department of Analytical Sciences, SmithKline Beecham Pharmaceuticals, Harlow, Essex CM19 5AW, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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