Dataset Information


Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells.

ABSTRACT: To contribute to the question of the putative role of cystatins in Alzheimer disease and in neuroprotection in general, we studied the interaction between human stefin B (cystatin B) and amyloid-beta-(1-40) peptide (Abeta). Using surface plasmon resonance and electrospray mass spectrometry we were able to show a direct interaction between the two proteins. As an interesting new fact, we show that stefin B binding to Abeta is oligomer specific. The dimers and tetramers of stefin B, which bind Abeta, are domain-swapped as judged from structural studies. Consistent with the binding results, the same oligomers of stefin B inhibit Abeta fibril formation. When expressed in cultured cells, stefin B co-localizes with Abeta intracellular inclusions. It also co-immunoprecipitates with the APP fragment containing the Abeta epitope. Thus, stefin B is another APP/Abeta-binding protein in vitro and likely in cells.

PROVIDER: S-EPMC2823404 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

| S-EPMC6952955 | BioStudies
| S-EPMC4390278 | BioStudies
1990-01-01 | S-EPMC551902 | BioStudies
| S-EPMC7913475 | BioStudies
| S-EPMC3469841 | BioStudies
| S-EPMC5727476 | BioStudies
| S-EPMC6109925 | BioStudies
2004-01-01 | S-EPMC1224237 | BioStudies
| S-EPMC3094694 | BioStudies
| S-EPMC1187909 | BioStudies