The Major Histocompatibility Complex–related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its Lifespan
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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.
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In health, FcRn is bound to albumin and prolongs the half-life of albumin while there is substantial cycling of serum albumin into and out of the cell.
“In health, this receptor is bound to albumin and has been found to prolong the half‐life of albumin while there is substantial cycling of serum albumin into and out of the cell,21”
From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [21]
The Discussion (page unavailable) concludes that FcRn binds albumin and extends its lifespan. It describes albumin entering cells, binding FcRn, and being released intact as an envisioned mechanism, not an observed or quantified finding of substantial cycling. Binding is also described as pH-dependent, rather than continuous. (LLM, conf=0.86)
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- Authors
- Chaudhury, C., Mehnaz, S., Robinson, J. M., Hayton, W. L., Pearl, D. K., Roopenian, D. C., & Anderson, C. L.
- Affiliations
- The Ohio State University (US)
- Jackson Laboratory (US)
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2003-01-27
- Volume
- 197
- Issue
- 3
- Pages
- 315-322
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2193842
- OpenAlex
- W2127401827
- Cited by
- 640
- References
- 37
- Citations by year
- 2026: 27 · 2025: 39 · 2024: 35 · 2023: 29 · 2022: 40 · 2021: 50 · 2020: 33 · 2019: 34 · 2018: 41 · 2017: 28 · 2016: 31 · 2015: 29 · 2014: 35 · 2013: 29 · 2012: 30
- FWCI
- 8.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
- Funders
- Lupus Research Alliance
- National Institutes of Health
- National Cancer Institute (CA88053, R01CA088053)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-56597, R01DK056597)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD038764, HD-38764)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
- Keywords
- neonatal Fc receptor, albumin, pH-dependent binding, plasma protein turnover, IgG half-life
- MeSH terms
- Animals, Cattle, Half-Life, Cricetinae, Hydrogen-Ion Concentration, Immunoglobulin G, Major Histocompatibility Complex, Mice, Inbred C57BL, Protein Binding, Receptors, Fc, Recombinant Proteins, Serum Albumin, Bovine, Histocompatibility Antigens Class I, CHO Cells, Mice, Knockout, Mice, Rats, In Vitro Techniques
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