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Article: Metabolism of the amyloid precursor-like protein 2 in MDCK cells. Polarized trafficking occurs independent of the chondroitin sulfate glycosaminoglycan chain

TitleMetabolism of the amyloid precursor-like protein 2 in MDCK cells. Polarized trafficking occurs independent of the chondroitin sulfate glycosaminoglycan chain
Authors
Issue Date1995
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, 1995, v. 270 n. 21, p. 12641-12645 How to Cite?
AbstractDeposition of β-amyloid peptide in senile plaques is a principal neuropathological hallmark of Alzheimer's disease. β-Amyloid peptide is derived from larger amyloid precursor proteins. Amyloid precursor protein is a member of a family of integral membrane glycoproteins that includes amyloid precursor-like protein (APLP) 1 and 2. Alternatively spliced pre-mRNAs encode several APLP2 isoforms; the APLP2-751 isoform is a substrate for modifications by a chondroitin sulfate glycosaminoglycan (CS GAG) chain, whereas the APLP2-763 isoform does not undergo CS GAG modification. In this report, we have examined the sorting and metabolism of APLP2-751 and APLP2- 763 in polarized epithelial Madin-Darby canine kidney (MDCK) cells. We demonstrate that, despite differences in post-translational modifications, both the APLP2-751 proteoglycan and APLP2-763 isoform were targeted and secreted to the basolateral compartment of MDCK cells. We document that the kinetics of intracellular maturation of full-length forms and secretion of soluble derivatives generated from each isoform were indistinguishable. Our results are consistent with the view that, in MDCK cells, the CS GAG chain of APLP2 has little influence on intracellular trafficking and that the principal basolateral targeting determinants are likely to reside in the APLP2 core protein.
Persistent Identifierhttp://hdl.handle.net/10722/176342
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151

 

DC FieldValueLanguage
dc.contributor.authorLo, ACYen_US
dc.contributor.authorThinakaran, Gen_US
dc.contributor.authorSlunt, HHen_US
dc.contributor.authorSisodia, SSen_US
dc.date.accessioned2012-11-26T09:10:42Z-
dc.date.available2012-11-26T09:10:42Z-
dc.date.issued1995en_US
dc.identifier.citationJournal Of Biological Chemistry, 1995, v. 270 n. 21, p. 12641-12645en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/176342-
dc.description.abstractDeposition of β-amyloid peptide in senile plaques is a principal neuropathological hallmark of Alzheimer's disease. β-Amyloid peptide is derived from larger amyloid precursor proteins. Amyloid precursor protein is a member of a family of integral membrane glycoproteins that includes amyloid precursor-like protein (APLP) 1 and 2. Alternatively spliced pre-mRNAs encode several APLP2 isoforms; the APLP2-751 isoform is a substrate for modifications by a chondroitin sulfate glycosaminoglycan (CS GAG) chain, whereas the APLP2-763 isoform does not undergo CS GAG modification. In this report, we have examined the sorting and metabolism of APLP2-751 and APLP2- 763 in polarized epithelial Madin-Darby canine kidney (MDCK) cells. We demonstrate that, despite differences in post-translational modifications, both the APLP2-751 proteoglycan and APLP2-763 isoform were targeted and secreted to the basolateral compartment of MDCK cells. We document that the kinetics of intracellular maturation of full-length forms and secretion of soluble derivatives generated from each isoform were indistinguishable. Our results are consistent with the view that, in MDCK cells, the CS GAG chain of APLP2 has little influence on intracellular trafficking and that the principal basolateral targeting determinants are likely to reside in the APLP2 core protein.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.meshAlternative Splicingen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAmyloid Beta-Protein Precursor - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Compartmentationen_US
dc.subject.meshCell Polarityen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshChondroitin Sulfates - Metabolismen_US
dc.subject.meshDogsen_US
dc.subject.meshGlycosaminoglycans - Metabolismen_US
dc.subject.meshMiceen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNerve Tissue Proteins - Metabolismen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshRecombinant Proteins - Metabolismen_US
dc.titleMetabolism of the amyloid precursor-like protein 2 in MDCK cells. Polarized trafficking occurs independent of the chondroitin sulfate glycosaminoglycan chainen_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.doi10.1074/jbc.270.21.12641en_US
dc.identifier.pmid7759513-
dc.identifier.scopuseid_2-s2.0-0029051346en_US
dc.identifier.volume270en_US
dc.identifier.issue21en_US
dc.identifier.spage12641en_US
dc.identifier.epage12645en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLo, ACY=7102780640en_US
dc.identifier.scopusauthoridThinakaran, G=7003798470en_US
dc.identifier.scopusauthoridSlunt, HH=35394062700en_US
dc.identifier.scopusauthoridSisodia, SS=7102763509en_US

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