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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
2000-10-23
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pubmed:abstractText |
Amyloid beta-peptide is generated by two sequential proteolytic cleavages mediated by beta-secretase (BACE) and gamma-secretase. BACE was recently identified as a membrane-associated aspartyl protease. We have now analyzed the maturation and pro-peptide cleavage of BACE. Pulse-chase experiments revealed that BACE is post-translationally modified during transport to the cell surface, which can be monitored by a significant increase in the molecular mass. The increase in molecular mass is caused by complex N-glycosylation. Treatment with tunicamycin and N-glycosidase F led to a BACE derivative with a molecular weight corresponding to an unmodified version. In contrast, the mature form of BACE was resistant to endoglycosidase H treatment. The cytoplasmic tail of BACE was required for efficient maturation and trafficking through the Golgi; a BACE variant lacking the cytoplasmic tail undergoes inefficient maturation. In contrast a soluble BACE variant that does not contain a membrane anchor matured more rapidly than full-length BACE. Pro-BACE was predominantly located within the endoplasmic reticulum. Pro-peptide cleavage occurred immediately before full maturation and trafficking through the Golgi.
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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/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid Precursor Protein Secretases,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
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/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide-N4-(N-acetyl-beta-glucosamin...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30849-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10801872-Amidohydrolases,
pubmed-meshheading:10801872-Amyloid Precursor Protein Secretases,
pubmed-meshheading:10801872-Anti-Bacterial Agents,
pubmed-meshheading:10801872-Aspartic Acid Endopeptidases,
pubmed-meshheading:10801872-Biological Transport,
pubmed-meshheading:10801872-Brain,
pubmed-meshheading:10801872-Cell Line,
pubmed-meshheading:10801872-Cell Membrane,
pubmed-meshheading:10801872-Cloning, Molecular,
pubmed-meshheading:10801872-Culture Media, Conditioned,
pubmed-meshheading:10801872-DNA, Complementary,
pubmed-meshheading:10801872-Endopeptidases,
pubmed-meshheading:10801872-Endoplasmic Reticulum,
pubmed-meshheading:10801872-Gene Library,
pubmed-meshheading:10801872-Glycoside Hydrolases,
pubmed-meshheading:10801872-Glycosylation,
pubmed-meshheading:10801872-Golgi Apparatus,
pubmed-meshheading:10801872-Humans,
pubmed-meshheading:10801872-Immunohistochemistry,
pubmed-meshheading:10801872-Microscopy, Fluorescence,
pubmed-meshheading:10801872-Mutagenesis, Site-Directed,
pubmed-meshheading:10801872-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:10801872-Peptides,
pubmed-meshheading:10801872-Precipitin Tests,
pubmed-meshheading:10801872-Protein Structure, Tertiary,
pubmed-meshheading:10801872-Time Factors,
pubmed-meshheading:10801872-Transfection,
pubmed-meshheading:10801872-Tunicamycin
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pubmed:year |
2000
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pubmed:articleTitle |
Maturation and pro-peptide cleavage of beta-secretase.
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pubmed:affiliation |
Adolf Butenandt-Institute, Department of Biochemistry, Laboratory for Alzheimer's Disease Research, Ludwig-Maximilians-University, 80336 Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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