Recombinant human monoclonal autoantibodies specific for citrulline-containing peptides from phage display libraries derived from patients with rheumatoid arthritis.

Objective: To isolate and characterize monoclonal autoantibodies (Mab) directed to citrullinated antigens from patients with rheumatoid arthritis (RA).

Methods: Using lymphocytes from bone marrow or peripheral blood from RA patients, we constructed antibody fragment libraries representing the antibody repertoire of these individuals. Antibody fragments recognizing a citrulline-containing peptide were selected from these patient libraries.

Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1.

Integrin alpha2beta1 is the principal adhesive receptor for collagen but platelets also adhere through glycoprotein VI (GPVI). Integrin alphaIIbbeta3 may augment platelet adhesion. We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin, and collagen.