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Proteins that bind to the RERMS region of beta amyloid precursor protein.

Abstract：

:The main objective of this study was to investigate the biological function of beta amyloid precursor protein (APP), in particular its nerve growth factor-like activity. We hypothesize that the extracellular domain containing the sequence RERMS, amino acids 328-332 of APP(695), represents the active site for this function. Binding assays using peptide fragments of this domain have demonstrated specific and saturable binding to the cell surface with affinity in the low nanomolar range. This induced our quest for an APP-specific receptor. We chose different peptide fragments of the RERMS domain as ligands and displacing agents on affinity columns to purify APP-binding molecules. Amino acid microsequencing yielded partial sequences of serum albumin, actin, two novel proteins of 41 and 63kDa, and human Collapsin Response Mediator Protein-2 (hCRMP-2). Because both APP and hCRMP-2 promote neuronal outgrowth and use a common signaling pathway, APP could be acting through a semaphorin receptor as well.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Pawlik M,Otero DA,Park M,Fischer WH,Levy E,Saitoh T

doi

10.1016/j.bbrc.2007.02.047

subject

Has Abstract

pub_date

2007-04-20 00:00:00

pages

907-12

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00323-3

journal_volume

355

pub_type

杂志文章

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