Glycan chains modulate prion protein binding to immobilized metal ions - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Neurochemistry International Année : 2007

Glycan chains modulate prion protein binding to immobilized metal ions

Résumé

PrPc is the normal isoform of the prion protein which can be converted into PrPSc, the pathology-associated conformer in prion diseases. It contains two N-linked glycan chains attached to the C-proximal globular domain. While the biological functions of PrPc are still unknown, its ability to bind Cu2+ is well documented. The main Cu2+-binding sites are located in the N-proximal, unstructured region of the molecule. Here we report that PrPc glycans influence the capacity of PrPc from sheep brain or cultured Rov cells to bind IMAC columns loaded with Cu2+ or Co2+. Using different anti-PrP antibodies and PrPc glycosylation mutants, we show that the full length non-glycosylated form of PrPc has a higher binding efficiency for column-bound Cu2+ and Co2+ than the corresponding glycosylated form. Our findings raise the possibility that the accessibility of the PrPc metal ion-binding sites might be controlled by the glycan chains.

Dates et versions

hal-02661336 , version 1 (30-05-2020)

Identifiants

Citer

Mohammed M. Moudjou, Julie Bernard, Elifsu Sabuncu, Christelle C. Langevin, Hubert H. Laude. Glycan chains modulate prion protein binding to immobilized metal ions. Neurochemistry International, 2007, 50 (5), pp.689-695. ⟨10.1016/j.neuint.2007.01.001⟩. ⟨hal-02661336⟩
3 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More