Source:http://linkedlifedata.com/resource/pubmed/id/11231279
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
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| pubmed:dateCreated |
2001-3-20
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| pubmed:abstractText |
Golgi alpha-mannosidase II is an enzyme that processes the intermediate oligosaccharide Gn(1)M(5)Gn(2) to Gn(1)M(3)Gn(2) during biosynthesis of N-glycans. Previously, we isolated a cDNA encoding a protein homologous to alpha-mannosidase II and designated it alpha-mannosidase IIx. Here, we show by immunocytochemistry that alpha-mannosidase IIx resides in the Golgi in HeLa cells. When coexpressed with alpha-mannosidase II, alpha-mannosidase IIx colocalizes with alpha-mannosidase II in COS cells. A protein A fusion of the catalytic domain of alpha-mannosidase IIx hydrolyzes a synthetic substrate, 4-umbelliferyl-alpha-D-mannoside, and this activity is inhibited by swainsonine. [(3)H]glucosamine-labeled Chinese hamster ovary cells overexpressing alpha-mannosidase IIx show a reduction of M(6)Gn(2) and an accumulation of M(4)Gn(2). Structural analysis identified M(4)Gn(2) to be Man alpha 1-->6(Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc. The results suggest that alpha-mannosidase IIx hydrolyzes two peripheral Man alpha 1-->6 and Man alpha 1-->3 residues from [(Man alpha 1-->6)(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc, during N-glycan processing.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosidases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Staphylococcal Protein A,
http://linkedlifedata.com/resource/pubmed/chemical/Swainsonine,
http://linkedlifedata.com/resource/pubmed/chemical/chitobiose,
http://linkedlifedata.com/resource/pubmed/chemical/mannosyl-oligosaccharide 1,3 -...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0014-2956
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
268
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1280-8
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:11231279-Animals,
pubmed-meshheading:11231279-CHO Cells,
pubmed-meshheading:11231279-COS Cells,
pubmed-meshheading:11231279-Carbohydrate Conformation,
pubmed-meshheading:11231279-Carbohydrate Sequence,
pubmed-meshheading:11231279-Chromatography, High Pressure Liquid,
pubmed-meshheading:11231279-Cricetinae,
pubmed-meshheading:11231279-Disaccharides,
pubmed-meshheading:11231279-Fluorescent Antibody Technique,
pubmed-meshheading:11231279-Golgi Apparatus,
pubmed-meshheading:11231279-HeLa Cells,
pubmed-meshheading:11231279-Humans,
pubmed-meshheading:11231279-Immunohistochemistry,
pubmed-meshheading:11231279-Mannosidases,
pubmed-meshheading:11231279-Mice,
pubmed-meshheading:11231279-Polysaccharides,
pubmed-meshheading:11231279-Recombinant Fusion Proteins,
pubmed-meshheading:11231279-Staphylococcal Protein A,
pubmed-meshheading:11231279-Swainsonine,
pubmed-meshheading:11231279-Transfection
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| pubmed:year |
2001
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| pubmed:articleTitle |
Overexpression of the Golgi-localized enzyme alpha-mannosidase IIx in Chinese hamster ovary cells results in the conversion of hexamannosyl-N-acetylchitobiose to tetramannosyl-N-acetylchitobiose in the N-glycan-processing pathway.
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| pubmed:affiliation |
Glycobiology Program, The Burnham Institute, La Jolla, CA 92037, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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