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The intracellular amyloid beta-peptide (A beta) binding protein, ERAB, a member of the short-chain dehydrogenase/reductase (SDR) family, is known to mediate apoptosis in different cell lines and to be a class II hydroxyacyl-CoA dehydrogenase. The A beta peptide inhibits the enzymatic reaction in a mixed type fashion with a Ki of 1.2 micromol/l and a KiES of 0.3 micromol/l, using 3-hydroxybutyryl-CoA. The peptide region necessary for inhibition comprises residues 12-24 of A beta1-40, covering the 16-20 fragment, which is the minimum sequence for the blockade of A beta polymerization, but that minimal fragment is not sufficient for more than marginal inhibition. The localization of ERAB to the endoplasmic reticulum and mitochondria suggests a complex interaction with components of the programmed cell death machinery. The interaction of A beta with ERAB further links oxidoreductase activity with both apoptosis and amyloid toxicity.

Original publication

DOI

10.1016/s0014-5793(99)00586-4

Type

Journal article

Journal

FEBS letters

Publication Date

05/1999

Volume

451

Pages

238 - 242

Addresses

Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. udo.oppermann@mbb.ki.se

Keywords

Mitochondria, Humans, Alzheimer Disease, 3-Hydroxyacyl CoA Dehydrogenases, Carrier Proteins, Sequence Alignment, Apoptosis, Enzyme Activation, Amino Acid Sequence, Molecular Sequence Data, Amyloid beta-Peptides