Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-9-7
pubmed:abstractText
The proteolytic fragments derived from the amyloid precursor protein (APP) in primary cultures of rat hippocampal neurons were analyzed by two-dimensional gel electrophoresis. The Semliki Forest Virus expression vector was used to express human APP695 and a mutant form associated with familial Alzheimer's disease (APP-FAD670/671). Hippocampal neurons expressing wtAPP695 or APP-FAD670/671 secrete at least six APP fragments of 100-110 kDa with isoelectric focusing points ranging from 4.5 to 4.0. The heterogeneity of the secreted APP forms is shown to be in part due to differences in glycosylation. In contrast to wtAPP695, neurons producing the APP-FAD670/671 variant did not secrete detectable amounts of secretory APP derived from cleavage within the amyloid beta A4 domain. This result suggests that there is little alpha-secretase cleavage in neurons expressing the APP-FAD670/671 mutant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
368
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
363-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7628638-Alzheimer Disease, pubmed-meshheading:7628638-Amyloid, pubmed-meshheading:7628638-Amyloid Precursor Protein Secretases, pubmed-meshheading:7628638-Animals, pubmed-meshheading:7628638-Aspartic Acid Endopeptidases, pubmed-meshheading:7628638-Cells, Cultured, pubmed-meshheading:7628638-Endopeptidases, pubmed-meshheading:7628638-Genetic Vectors, pubmed-meshheading:7628638-Glycosylation, pubmed-meshheading:7628638-Hippocampus, pubmed-meshheading:7628638-Humans, pubmed-meshheading:7628638-Isoelectric Point, pubmed-meshheading:7628638-Molecular Weight, pubmed-meshheading:7628638-Neurons, pubmed-meshheading:7628638-Peptide Mapping, pubmed-meshheading:7628638-Prions, pubmed-meshheading:7628638-Protein Precursors, pubmed-meshheading:7628638-Protein Processing, Post-Translational, pubmed-meshheading:7628638-Rats, pubmed-meshheading:7628638-Semliki forest virus
pubmed:year
1995
pubmed:articleTitle
Two-dimensional gel mapping of the processing of the human amyloid precursor protein in rat hippocampal neurons.
pubmed:affiliation
Center for Molecular Biology Heidelberg (ZMBH), University of Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't