Unknown

Dataset Information

0

Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner.


ABSTRACT: Serum amyloid A action in immune response and deposition in inflammation-linked amyloidosis involve SAA-lipid interactions. We show that SAA sequesters neutral and anionic phospholipids and their hydrolytic products to form nanoparticles, suggesting a synergy with phospholipase A2. The lipid charge and shape affect SAA protection from proteolysis, aggregation and fibrillogenesis.

SUBMITTER: Jayaraman S 

PROVIDER: S-EPMC5882536 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner.

Jayaraman Shobini S   Gantz Donald L DL   Haupt Christian C   Fändrich Marcus M   Gursky Olga O  

Chemical communications (Cambridge, England) 20180401 28


Serum amyloid A action in immune response and deposition in inflammation-linked amyloidosis involve SAA-lipid interactions. We show that SAA sequesters neutral and anionic phospholipids and their hydrolytic products to form nanoparticles, suggesting a synergy with phospholipase A2. The lipid charge and shape affect SAA protection from proteolysis, aggregation and fibrillogenesis. ...[more]

Similar Datasets

| S-EPMC8637590 | biostudies-literature
| S-EPMC2717229 | biostudies-literature
| S-EPMC7898819 | biostudies-literature
| S-EPMC314143 | biostudies-literature
| S-EPMC5816019 | biostudies-literature
| S-EPMC10704437 | biostudies-literature
| S-EPMC3399535 | biostudies-literature
| S-EPMC1482631 | biostudies-literature
| S-EPMC3285303 | biostudies-literature
| S-EPMC10980705 | biostudies-literature