File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Expression of a ubiquitous, cross-reactive homologue of the mouse β- amyloid precursor protein (APP)

TitleExpression of a ubiquitous, cross-reactive homologue of the mouse β- amyloid precursor protein (APP)
Authors
Issue Date1994
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1994, v. 269 n. 4, p. 2637-2644 How to Cite?
AbstractAlzheimer's disease is characterized by the presence of senile plaques comprised primarily of deposits of the β-amyloid protein (Aβ) derived from larger amyloid precursor proteins (APP). We have identified a cDNA that encodes a 751-amino acid APP-like protein (designated APLP2) from the mouse that, with exception of the Aβ region, is highly homologous to APP. In situ hybridization and quantitative polymerase chain reaction reveal that APLP2 and APP mRNA are expressed in similar, if not identical, neuronal populations and at similar levels. APLP2 appears to mature through the same unusual secretory/cleavage pathway as APP. Furthermore, widely utilized antibodies generated against non-overlapping epitopes of APP do not discriminate between APP and APLP2. Although APLP2 cannot give rise to Aβ, its near identity to APP outside the Aβ domain confounds the interpretation of previous immunocytochemical and biochemical characterizations of APP biosynthesis and metabolism.
Persistent Identifierhttp://hdl.handle.net/10722/176338
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSlunt, HHen_US
dc.contributor.authorThinakaran, Gen_US
dc.contributor.authorVon Koch, Cen_US
dc.contributor.authorLo, ACYen_US
dc.contributor.authorTanzi, REen_US
dc.contributor.authorSisodia, SSen_US
dc.date.accessioned2012-11-26T09:10:39Z-
dc.date.available2012-11-26T09:10:39Z-
dc.date.issued1994en_US
dc.identifier.citationJournal Of Biological Chemistry, 1994, v. 269 n. 4, p. 2637-2644en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/176338-
dc.description.abstractAlzheimer's disease is characterized by the presence of senile plaques comprised primarily of deposits of the β-amyloid protein (Aβ) derived from larger amyloid precursor proteins (APP). We have identified a cDNA that encodes a 751-amino acid APP-like protein (designated APLP2) from the mouse that, with exception of the Aβ region, is highly homologous to APP. In situ hybridization and quantitative polymerase chain reaction reveal that APLP2 and APP mRNA are expressed in similar, if not identical, neuronal populations and at similar levels. APLP2 appears to mature through the same unusual secretory/cleavage pathway as APP. Furthermore, widely utilized antibodies generated against non-overlapping epitopes of APP do not discriminate between APP and APLP2. Although APLP2 cannot give rise to Aβ, its near identity to APP outside the Aβ domain confounds the interpretation of previous immunocytochemical and biochemical characterizations of APP biosynthesis and metabolism.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAlzheimer Disease - Metabolismen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAmyloid Beta-Protein Precursor - Biosynthesis - Immunologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBrain - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCross Reactionsen_US
dc.subject.meshDna Primersen_US
dc.subject.meshDna, Complementary - Isolation & Purification - Metabolismen_US
dc.subject.meshEmbryo, Mammalianen_US
dc.subject.meshGene Libraryen_US
dc.subject.meshGolgi Apparatus - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshIn Situ Hybridizationen_US
dc.subject.meshMiceen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNerve Tissue Proteins - Biosynthesisen_US
dc.subject.meshOrgan Specificityen_US
dc.subject.meshPolymerase Chain Reactionen_US
dc.subject.meshRna Probesen_US
dc.subject.meshRna, Messenger - Analysis - Metabolismen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.meshTranscription, Geneticen_US
dc.subject.meshTransfectionen_US
dc.titleExpression of a ubiquitous, cross-reactive homologue of the mouse β- amyloid precursor protein (APP)en_US
dc.typeArticleen_US
dc.identifier.emailLo, ACY: amylo@hkucc.hku.hken_US
dc.identifier.authorityLo, ACY=rp00425en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid8300594-
dc.identifier.scopuseid_2-s2.0-0028059841en_US
dc.identifier.volume269en_US
dc.identifier.issue4en_US
dc.identifier.spage2637en_US
dc.identifier.epage2644en_US
dc.identifier.isiWOS:A1994MV43200045-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridSlunt, HH=35394062700en_US
dc.identifier.scopusauthoridThinakaran, G=7003798470en_US
dc.identifier.scopusauthoridVon Koch, C=36869679500en_US
dc.identifier.scopusauthoridLo, ACY=7102780640en_US
dc.identifier.scopusauthoridTanzi, RE=7102180916en_US
dc.identifier.scopusauthoridSisodia, SS=7102763509en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats