Linked Life Data

8576160

Source:http://linkedlifedata.com/resource/pubmed/id/8576160

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-3-11
pubmed:abstractText
The specific binding of the amyloid precursor protein (APP) to extracellular matrix molecules suggests that APP regulates cell interactions and has a function as a cell adhesion molecule and/or substrate adhesion molecule. On the molecular level APP has binding sites for collagen, laminin, and glycosaminoglycans which is a characteristic feature of cell adhesion molecules. We have examined the interactions between the APP and collagen types I and IV and identified the corresponding binding sites on APP and collagen type I. We show that APP bound most efficiently to collagen type I in a concentration-dependent and specific manner in the native and heat-denatured states, suggesting an involvement of a contiguous binding site on collagen. This binding site was identified on the cyanogen bromide fragment alpha 1(I)CB6 of collagen type I, which also binds heparin. APP did not bind to collagen type I-heparin complexes, which suggests that there are overlapping binding sites for heparin and APP on collagen. We localized the site of APP that mediates collagen binding within residues 448-465 of APP695, which are encoded by the ubiquitously expressed APP exon 12, whereas the high affinity heparin binding site of APP is located in exon 9. Since a peptide encompassing this region binds to collagen type I and inhibits APP-collagen type I binding in nanomolar concentrations, this region may comprise the major part of the collagen type I binding site of APP. Moreover, our data also indicate that the collagen binding site is involved in APP-APP interaction that can be modulated by Zn(II) and heparin. Taken together, the data suggest that the regulation of APP binding to collagen type I by heparin occurs through the competitive binding of heparin and APP to collagen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1613-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8576160-Amino Acid Sequence, pubmed-meshheading:8576160-Amyloid beta-Protein Precursor, pubmed-meshheading:8576160-Animals, pubmed-meshheading:8576160-Base Sequence, pubmed-meshheading:8576160-Binding Sites, pubmed-meshheading:8576160-Brain, pubmed-meshheading:8576160-Cattle, pubmed-meshheading:8576160-Collagen, pubmed-meshheading:8576160-Exons, pubmed-meshheading:8576160-Female, pubmed-meshheading:8576160-Heparin, pubmed-meshheading:8576160-Humans, pubmed-meshheading:8576160-Kinetics, pubmed-meshheading:8576160-Mice, pubmed-meshheading:8576160-Molecular Sequence Data, pubmed-meshheading:8576160-Oligodeoxyribonucleotides, pubmed-meshheading:8576160-Peptide Fragments, pubmed-meshheading:8576160-Placenta, pubmed-meshheading:8576160-Plasmids, pubmed-meshheading:8576160-Pregnancy, pubmed-meshheading:8576160-Protein Binding, pubmed-meshheading:8576160-Protein Structure, Secondary, pubmed-meshheading:8576160-Rats, pubmed-meshheading:8576160-Recombinant Proteins, pubmed-meshheading:8576160-Sequence Homology, Amino Acid, pubmed-meshheading:8576160-Zinc
pubmed:year
1996
pubmed:articleTitle
Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I.
pubmed:affiliation
Center for Molecular Biology Heidelberg (ZMBH), University of Heidelberg, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't