Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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CHO Cells
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Cattle
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Cricetinae
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Half-Life
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Histocompatibility Antigens Class I
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Hydrogen-Ion Concentration
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Immunoglobulin G / metabolism
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In Vitro Techniques
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Major Histocompatibility Complex
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Mice
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Mice, Inbred C57BL
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Mice, Knockout
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Protein Binding
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Rats
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Receptors, Fc / deficiency
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Receptors, Fc / genetics
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Receptors, Fc / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Serum Albumin, Bovine / metabolism*
Substances
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Histocompatibility Antigens Class I
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Immunoglobulin G
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Receptors, Fc
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Recombinant Proteins
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Serum Albumin, Bovine
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Fc receptor, neonatal