2003/01/27 by Chaity Chaudhury, Samina Mehnaz, John M. Robinson +4 · 641 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Medicine · #Albumin #Antibody #Antigen #Biochemistry #Biology #Blood groups and transfusion #Catabolism #Cell biology #Chemistry #Immunoglobulin G #Immunology #Major histocompatibility complex #Metabolism #Monoclonal and Polyclonal Antibodies Research #Neonatal Fc receptor #Plasma protein binding #Protein purification and stability #Receptor #Serum albumin
paper · pdf · doi:10.1084/jem.20021829
published in The Journal of Experimental Medicine 197(3), 315-322 (Rockefeller University Press)
openalex publication_date 2003/01/27 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/06
The inverse relationship between serum albumin concentration and its half-life suggested to early workers that albumin would be protected from a catabolic fate by a receptor-mediated mechanism much like that proposed for IgG. We show here that albumin binds FcRn in a pH dependent fashion, that the lifespan of albumin is shortened in FcRn-deficient mice, and that the plasma albumin concentration of FcRn-deficient mice is less than half that of wild-type mice. These results affirm the hypothesis that the major histocompatibility complex-related Fc receptor protects albumin from degradation just as it does IgG, prolonging the half-lives of both.