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Am J Physiol Gastrointest Liver Physiol 290: G352-G360, 2006. First published October 6, 2005; doi:10.1152/ajpgi.00286.2005
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LIVER AND BILIARY TRACT

Albumin turnover: FcRn-mediated recycling saves as much albumin from degradation as the liver produces

Jonghan Kim,1,2 C. L. Bronson,1 William L. Hayton,2 Michael D. Radmacher,3 Derry C. Roopenian,5 John M. Robinson,4 and Clark L. Anderson1

1Department of Internal Medicine, 2College of Pharmacy, 3Center for Biostatistics, and 4Department of Physiology and Cell Biology, The Ohio State University, Columbus, Ohio; and 5The Jackson Laboratory, Bar Harbor, Maine

Submitted 27 June 2005 ; accepted in final form 3 October 2005

It is now understood that the nonclassical major histocompatibility complex-I molecule FcRn binds albumin and retrieves it from an intracellular degradative fate. Whether FcRn in the liver modulates albumin turnover through effects on biosynthesis and production is not known. Thus we quantified the appearance of biosynthetically labeled albumin in plasma after an intravenous bolus injection of [3H]leucine in FcRn-deficient mice. The production rates for both albumin (FcRn substrate) and transferrin (nonsubstrate) are increased by ~20% in FcRn-deficient mice compared with normal mice, likely compensating for the lowered plasma oncotic pressure caused by hypoalbuminemia in FcRn-deficient mice. Determining the magnitude of FcRn-mediated effects on albumin turnover, we then measured the steady-state plasma concentrations of biosynthetically labeled albumin and transferrin during [3H]leucine infusion. The concentration of albumin was ~40% lower in FcRn-deficient mice compared with normal mice. Furthermore, the ~40% lower plasma albumin concentration in FcRn-deficient mice along with the ~20% increase in albumin production indicate, by the mass-balance equation, that albumin degradation in FcRn-deficient mice is twice that of normal mice. These studies of biosynthetically labeled, and thus native, albumin support our previous finding that FcRn protects albumin from degradation. Permitting quantification of the magnitude of FcRn-mediated recycling, they further indicate that FcRn has extraordinary capacity: the amount of albumin saved from degradation by FcRn-mediated recycling is the same as that produced by the liver.

production; clearance; steady-state; kinetics; Fc receptor


Address for reprint requests and other correspondence: C. L. Anderson, Dept. of Internal Medicine, The Ohio State Univ., 425 Davis Heart and Lung Research Institute, 473 West Twelfth Ave., Columbus, OH 43210 (e-mail: anderson.48{at}osu.edu)




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