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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1995-4-10
|
| pubmed:abstractText |
The present study investigated expression and processing of amyloid precursor protein by neuronally differentiated IMR-32 neuroblastoma cells. APP mRNA in these cells was found to consist of approximately 58% APP695, 38% APP751, and < 4% APP770. APP-immunoreactive bands detected in western blots of cellular protein extracts were only detected by anti-APP antibodies to peptides with strong homology to APLP2, suggesting that these bands represent APP-like proteins and not APP itself. This result suggests that previous studies claiming immunodetection of cellular forms of APP may have to be re-evaluated. Four main species of C-terminal truncated, secreted APP were detected in blots of protein extracts from medium conditioned by these cells. The immunoreactive profile of these bands suggested a cleavage site N-terminal to the Lys16-Leu17 bond of alpha-secretase. This, together with differences in number and molecular mass of APP-immunoreactive bands between secreted APP from IMR-32 cells and that from the commonly used PC-12 cells, suggests differences in APP processing between these two neuronally differentiated cell lines. In theory, IMR-32 cells being of human neuronal origin may be a more appropriate cell line to study APP-processing in relation to Alzheimer's disease than the rat phaeochromocytoma PC-12 cell line. Therefore, these detected differences warrant further investigation. Additionally IMR-32 cells under certain tissue culture conditions can form intracellular fibrillary material that reacts with anti-PHF specific antibodies. Neuronally differentiated IMR-32 cells could therefore be used as a model system to investigate possible interactions between APP-processing and PHF formation.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0360-4012
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
39
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
482-93
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7884825-Alzheimer Disease,
pubmed-meshheading:7884825-Amino Acid Sequence,
pubmed-meshheading:7884825-Amyloid beta-Protein Precursor,
pubmed-meshheading:7884825-Antibodies,
pubmed-meshheading:7884825-Antibodies, Monoclonal,
pubmed-meshheading:7884825-Base Sequence,
pubmed-meshheading:7884825-Blotting, Northern,
pubmed-meshheading:7884825-Cell Differentiation,
pubmed-meshheading:7884825-Cell Line,
pubmed-meshheading:7884825-Humans,
pubmed-meshheading:7884825-Immunohistochemistry,
pubmed-meshheading:7884825-Models, Neurological,
pubmed-meshheading:7884825-Molecular Sequence Data,
pubmed-meshheading:7884825-Neuroblastoma,
pubmed-meshheading:7884825-Neurons,
pubmed-meshheading:7884825-Oligonucleotide Probes,
pubmed-meshheading:7884825-Peptide Fragments,
pubmed-meshheading:7884825-RNA, Messenger,
pubmed-meshheading:7884825-Sequence Homology, Amino Acid,
pubmed-meshheading:7884825-Tumor Cells, Cultured
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Human IMR-32 neuroblastoma cells as a model cell line in Alzheimer's disease research.
|
| pubmed:affiliation |
School of Biology and Biochemistry, Queen's University of Belfast, Northern Ireland.
|
| pubmed:publicationType |
Journal Article,
Comparative Study
|