PMID: 9194688Jan 1, 1997Paper

Pharmacologic inhibition of transglutaminase-induced cross-linking of Alzheimer's amyloid beta-peptide

Life Sciences
W ZhangT D Bjornsson

Abstract

The brain of Alzheimer's disease (AD) patients contains deposits of amyloid beta-peptide (A beta). Recent studies have shown that A beta is a substrate for tissue transglutaminase (TGase), which induces the formation of cross-linked dimers and polymers, and that tacrine, indomethacin and deferoxamine, which have widely different chemical structures, attenuate the progression of symptoms of AD. This report evaluated the potential of a total of ten different pharmacological agents to inhibit TGase-induced cross-linking of A beta, including known TGase inhibitors (dansylcadaverine, spermine), non-steroidal anti-inflammatory drugs (indomethacin, meclofenamic acid, diflunisal, salicylic acid), monoamine oxidase inhibitors (tranylcypromine, phenelzine), an acetylcholinesterase inhibitor (tacrine), and an iron chelating agent (deferoxamine). All but one (salicylic acid) of these ten agents had an inhibitory effect on TGase-induced A beta cross-linking. These results suggest that inhibition of TGase-induced cross-linking of A beta is a potential pharmacologic target for the treatment of AD. A method is also presented for the determination of percent inhibition of TGase-induced A beta cross-linking based on the separated monomer, dimer ...Continue Reading

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Citations

Sep 11, 1999·The International Journal of Biochemistry & Cell Biology·J S Chen, K Mehta
Jun 19, 2010·American Journal of Respiratory Cell and Molecular Biology·Yinglin LiuBarry L Fanburg
May 18, 2001·Analytical Biochemistry·T M JeitnerA J Cooper
Oct 3, 2000·The Journal of Biological Chemistry·B A CitronB W Festoff
Dec 1, 2017·BMB Reports·Boram Min, Kwang Chul Chung

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