Comparative Studies on the Half-Life of I131-Labeled Albumins and Nonradioactive Human Serum Albumin in a Case of Analbuminemia

Bennhold, H.; Kallee, E

doi:10.1172/jci103868

Cited by 98 publications

(44 citation statements)

References 19 publications

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“…Albumin metabolism in heritable analbuminemia differs from that in idiopathic hypoalbuminemia. In a number of cases of analbuminemia, clinically and biochemically similar to that described here, the metabolic half-life of infused 1311-labeled albumin is prolonged (2,3,31), whereas in the case of idiopathic hypoalbuminemia in the 4-year-old child, the labeled albumin was rapidly degraded and had a half-life one-sixth of normal (2). Increased catabolism of albumin is also a characteristic of familial hypercatabolic hypoproteinemia, which exhibits a marked reduction of both albumin and IgG (32).…”

Section: Resultsmentioning

confidence: 52%

A nucleotide insertion and frameshift cause analbuminemia in an Italian family.

Watkins

Madison

Galliano

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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In analbuminemia, a very rare inherited syndrome, subjects produce little or no albumin (1/100th to 1/1000th normal), presumably because of a mutation in the albumin gene; yet, they have only moderate edema and few related symptoms owing to a compensatory increase in other plasma proteins. Because of the virtual absence of albumin the defect must be identified at the DNA level. In this study the mutation causing analbuminemia in an Italian family was investigated by analysis of DNA from a mother and her daughter. The mother was homozygous for the trait and had a serum albumin value of <0.01 g/dl (about 1/500th normal); the daughter was heterozygous for the trait and had a nearly normal albumin value. Molecular cloning and sequence analysis of DNA from both mother and daughter showed that the mutation is caused by a nucleotide insertion in exon 8; this produces a frameshift leading to a premature stop, seven codons downstream. The methods of heteroduplex hybridization and single-strand conformation polymorphism were used to compare the DNA of the mother and daughter to the DNA of two unrelated analbuminemic individuals (one Italian and one American). This showed that all three analbuminemic individuals had different mutations; these also differed from the mutation in the only human case previously studied at the DNA level, which was a splicing defect affecting the ligation of the exon 6-exon 7 sequences. Thus, analbuminemia may result from a variety of mutations and is genetically heterogeneous.Serum albumin is the most abundant secreted protein in the body; it comprises about 50%o of the total protein in serum where it has a normal concentration of 3.5-4.5 g/dl (1

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Section: Resultsmentioning

confidence: 52%

A nucleotide insertion and frameshift cause analbuminemia in an Italian family.

Watkins

Madison

Galliano

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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“…Normal survival has been observed for fibrinogen in afibrinogenemia (23), ceruloplasmin in Wilson's disease (24), and IgM and IgA in agammaglobulinemia (10,25). The survival of albumin in analbuminemia (26)(27)(28) and IgG in agammaglobulinemia (16) (29,30) and by the newborn gut in certain species (31) (32), liver disease (33), and multiple myeloma (9, 34), or after infusion of IgG (35,36).…”

Section: Methodsmentioning

confidence: 99%

Accelerated breakdown of immunoglobulin G (IgG) in myotonic dystrophy: a hereditary error of immunoglobulin catabolism.

Wochner¹,

Drews²,

Strober³

et al. 1966

J. Clin. Invest.

154

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“…The k 12 and k 21 for albumin were recalculated to be 0.497 d -1 and 0.402 d -1 , respectively, based on the two-compartment model from the original albumin decay data [31], and V 1 was 45.5 mL/ kg [16]. Third, the k cat values for albumin in analbuminemic patients were relatively well studied [32][33][34]. As these patients showed normal IgG concentration and catabolism, FcRn expression in these patients appears to be normal.…”

Section: In Vivo Kinetic Characterization Of Fcrn-mediated Albumin Rementioning

confidence: 99%

Kinetics of FcRn-mediated recycling of IgG and albumin in human: Pathophysiology and therapeutic implications using a simplified mechanism-based model

Kim

Hayton

Robinson

et al. 2007

Clinical Immunology

171

122

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The nonclassical MHC class-I molecule, FcRn, salvages both IgG and albumin from degradation. Here we introduce a mechanism-based kinetic model for human to quantify FcRn-mediated recycling of both ligands based on saturable kinetics and data from the literature using easily measurable plasma concentrations rather than unmeasurable endosomal concentrations. The FcRn-mediated fractional recycling rates of IgG and albumin were 142% and 44% of their fractional catabolic rates, respectively. Clearly, FcRn-mediated recycling is a major contributor to the high endogenous concentrations of these two important plasma proteins. While familial hypercatabolic hypoproteinemia is caused by complete FcRn deficiency, the hypercatabolic IgG deficiency of myotonic dystrophy could be explained, based on the kinetic analyses, by a normal number of FcRn with lowered affinity for IgG but normal affinity for albumin. A simulation study demonstrates that the plasma concentrations of IgG and albumin could be dynamically controlled by both FcRn-related and -unrelated parameters.

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Comparative Studies on the Half-Life of I131-Labeled Albumins and Nonradioactive Human Serum Albumin in a Case of Analbuminemia

Cited by 98 publications

References 19 publications

A nucleotide insertion and frameshift cause analbuminemia in an Italian family.

A nucleotide insertion and frameshift cause analbuminemia in an Italian family.

Accelerated breakdown of immunoglobulin G (IgG) in myotonic dystrophy: a hereditary error of immunoglobulin catabolism.

Kinetics of FcRn-mediated recycling of IgG and albumin in human: Pathophysiology and therapeutic implications using a simplified mechanism-based model

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