The Major Histocompatibility Complex–related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its Lifespan
By C. Chaudhury, Samina Mehnaz, J. M. Robinson, W. Hayton, Dennis K. Pearl, D. Roopenian, C. Anderson. Journal of Experimental Medicine, 2003
630 citations recorded by the source corpus.
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.
Subfields: Hematology, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/6df9f9dcee03e32edeb1cd1e52144e7aa9816122
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Citations in the corpus
- Signaling mechanisms regulating endothelial permeability. (2006, background): “Interestingly, like IgG, the albumin was shown to bind the major histocompatibility complex-related Fc receptor (FcRn) at low pH and be shielded from degradation, which significantly prolonged the plasma half-life of both proteins (156).”
- Albumin-based drug delivery: harnessing nature to cure disease (2016, background): “Work by the same group revealed that the serum concentration of albumin in FcRn deficient mice was reduced compared to wild-type mice and that FcRn-deficient mice had shortened half-life of albumin [28].”
- FcRn: the neonatal Fc receptor comes of age (2007, background): “Although a role for FcRn in IgG homeostasis is well accepted, it has recently been shown that FcRn also extends the serum half-life of albumi”
- Unraveling the mysteries of serum albumin—more than just a serum protein (2014, background): “…by binding both proteins with high affinity only at a low pH (pH < 6.5) in acidic endosomes, preventing their degradation via the lysosomal pathway and returning them to the extracellular space (pH 7.4) (Chaudhury et al., 2003; Ober et al., 2004; Anderson et al., 2006; Andersen et al., 2012).”