Identification of glutamine and lysine residues in Alzheimer amyloid βA4 peptide responsible for transglutaminase‐catalysed homopolymerization and cross‐linking to α2M receptor

FEBS Letters

Rasmussen, Lone K.¹  Petersen, Torben E.¹  Gliemann, Jørgen²  Jensen, Poul Henning²  Sørensen, Esben S.¹ 

[1] Protein Chemistry Laboratory, University of Aarhus, The Science Park, DK-8000 Aarhus, Denmark;Institute of Medical Biochemistry, University of Aarhus, DK-8000 Aarhus C, Denmark

关键词: Alzheimer;    β-Amyloid peptide;    Transglutaminase;    Glutamine;    Lysine;    α2M receptor;    AD;    Alzheimer's disease;    APP;    amyloid precursor protein;    βA4;    β-amyloid peptide;    Dns-peptide;    dansyl conjugated to Pro-Gly-Gly-Gln-Gln-Ile-Val;    PTH;    phenylthiohydantoin;    TG;    transglutaminase;    α2M receptor;    α2-macroglobulin receptor;   

DOI  :  10.1016/0014-5793(94)80356-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The β-amyloid peptide (βA4), derived from a larger amyloid precursor protein, is the principal component of senile plaques in Alzheimer's disease. Here we report that the full-length (1–40) synthetic βA4 peptide, containing one glutamine and two lysine residues, is able to form homopolymers in a transglutaminase-mediated reaction. Moreover, transglutaminase catalysed the formation of heteropolymers in reactions of βA4 with α₂M receptor, a constituent of amyloid plaques, and with extracellular matrix proteins. Incorporation of site-specific probes followed by enzymatic digestion and sequencing of tracer-containing fractions demonstrated that both Lys¹⁶, Lys²⁸ and Gin¹⁵ in βA4 were susceptible to cross-linking by transglutaminase.

【 授权许可】

Unknown