Source:http://linkedlifedata.com/resource/pubmed/id/16802341
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2006-8-30
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| pubmed:abstractText |
Presenilin-dependent intramembranous proteolysis mediates the dual cleavage of the Notch-1 protein (S4 and S3) as well as the beta amyloid precursor protein (betaAPP) (gamma40 and epsilon-site). betaAPP has a valine residue just before the gamma40 (amyloid beta [Abeta] numbering) site and after the epsilon-site. Both gamma40 and epsilon have multiple cleavage sites, and the varieties of gamma40 cleavage are associated with Alzheimer's disease (AD). These lines of evidence suggest that valine plays a role in the intramembranous proteolysis. S4 cleavage in the middle of the Notch-1 transmembrane domain (TMD) corresponds to the gamma40 cleavage of betaAPP. The cleavage site is in the center of four sequential alanine residues between Ala1731 and Ala1732, neither of which has a valine residue. To investigate the effects of valine on presenilin-dependent intramembranous proteolysis, we replaced the transmembrane domain residue of Notch-1 with valine and analyzed the efficiency and precision at S4 and S3. We observed that all valine-mutated Notch-1 proteins have a dominant cleavage site (S4) between Ala1731 and Ala1732 with some variations of cleavage precision, suggesting that valine is not indispensable for determining the cleavage site of the Notch-1 transmembrane domain, but affects the efficiency and precision at S4 cleavage of the Notch-1 transmembrane domain.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/NOTCH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Nexins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Notch1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0360-4012
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
84
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
918-25
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:16802341-Amino Acid Sequence,
pubmed-meshheading:16802341-Amyloid beta-Protein Precursor,
pubmed-meshheading:16802341-Analysis of Variance,
pubmed-meshheading:16802341-Animals,
pubmed-meshheading:16802341-Blotting, Western,
pubmed-meshheading:16802341-Cell Line, Transformed,
pubmed-meshheading:16802341-Cell Membrane,
pubmed-meshheading:16802341-Humans,
pubmed-meshheading:16802341-Immunoprecipitation,
pubmed-meshheading:16802341-Mice,
pubmed-meshheading:16802341-Mutagenesis, Site-Directed,
pubmed-meshheading:16802341-Mutation,
pubmed-meshheading:16802341-Peptide Fragments,
pubmed-meshheading:16802341-Protease Nexins,
pubmed-meshheading:16802341-Protein Structure, Tertiary,
pubmed-meshheading:16802341-Receptor, Notch1,
pubmed-meshheading:16802341-Receptors, Cell Surface,
pubmed-meshheading:16802341-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:16802341-Transfection,
pubmed-meshheading:16802341-Valine
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| pubmed:year |
2006
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| pubmed:articleTitle |
Effect of valine on the efficiency and precision at S4 cleavage of the Notch-1 transmembrane domain.
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| pubmed:affiliation |
Department of Psychiatry, Institute of Neuroscience, Mie University Graduate School of Medicine, Mie, Japan. h-tanii@clin.medic.mie-u.ac.jp
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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