Therapeutic effects of systemic administration of chaperone αB-crystallin associated with binding proinflammatory plasma proteins.

ABSTRACT: The therapeutic benefit of the small heat shock protein αB-crystallin (HspB5) in animal models of multiple sclerosis and ischemia is proposed to arise from its increased capacity to bind proinflammatory proteins at the elevated temperatures within inflammatory foci. By mass spectral analysis, a common set of ∼70 ligands was precipitated by HspB5 from plasma from patients with multiple sclerosis, rheumatoid arthritis, and amyloidosis and mice with experimental allergic encephalomyelitis. These proteins were distinguished from other precipitated molecules because they were enriched in the precipitate as compared with their plasma concentrations, and they exhibited temperature-dependent binding. More than half of these ligands were acute phase proteins or members of the complement or coagulat

SUBMITTER: Rothbard JB 

PROVIDER: S-EPMC3322989 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature