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PubMed · 7688497

Interaction between the beta-amyloid peptide precursor and histones.

A Potempska·N Ramakrishna·H M Wisniewski·D L Miller
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Abstract

The function of the beta-amyloid peptide precursors (beta-APPs) remains undefined. In a search for ligands of beta-APP we found that the most prominent beta-APP-binding proteins were histones. To measure the specificity of binding the secreted or extracellular form of beta-APP(751), beta-APP-S, was purified from recombinant baculovirus-infected Sf-9 cells and was labeled with iodine-125. The labeled beta-APP-S bound to each of the histones, which had previously been adsorbed to nitrocellulose membranes. Differences in their apparent affinities were small. beta-APP-S did not bind to histones incorporated into chromatin. beta-APP-S bound relatively weakly to fibronectin, laminin, collagen type I, or collagen type IV. It did not bind to other basic proteins tested, myelin basic protein, or cytochrome c. The beta-APP-S-histone complex adhered to most filters and gel media, which precluded a direct determination of its stability. The apparent dissociation constant of beta-APP-S bound to histone-4-Sepharose was about 30 nM. Although beta-APP normally does not contact histones, it may bind those that are released from damaged cells. A function of beta-APP may be to bind and recycle substances such as histones, proteases, and matrix proteins from the extracellular medium.

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Amyloid beta-Protein PrecursorAnimalsCytochrome c GroupHistonesHumansMyelin Basic ProteinRatsRecombinant ProteinsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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A Potempska, N Ramakrishna, H M Wisniewski, D L Miller. 1993-08-01. Interaction between the beta-amyloid peptide precursor and histones.. https://doi.org/10.1006/abbi.1993.1374

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