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Mutations and polymorphisms of the gene of the major human blood protein, serum albumin
Author(s) -
Minchiotti Lorenzo,
Galliano Monica,
KraghHansen Ulrich,
Peters Theodore
Publication year - 2008
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.20754
Subject(s) - frameshift mutation , point mutation , biology , albumin , nonsense mutation , genetics , mutation , serum albumin , microbiology and biotechnology , gene , exon , amino acid , biochemistry , missense mutation
Abstract We have tabulated the 77 currently known mutations of the familiar human blood protein, serum albumin (ALB). A total of 65 mutations result in bisalbuminemia. Physiological and structural effects of these mutations are included where observed. Most of the changes are benign. The majority of them were detected upon clinical electrophoretic studies, as a result of a point mutation of a charged amino acid residue. Three were discovered by their strong binding of thyroxine or triiodothyronine. A total of 12 of the tabulated mutations result in analbuminemia, defined as a serum albumin concentration of <1 g/L. These were generally detected upon finding a low albumin concentration in patients with mild edema, and involve either splicing errors negating translation or premature stop codons producing truncated albumin molecules. A total of nine mutations, five of those with analbuminemia and four resulting in variants modified near the C‐terminal end, cause frameshifts. Allotypes from three of the point mutations become N‐glycosylated and one C‐terminal frameshift mutation shows O‐glycosylation. Hum Mutat 0,1–10, 2008. © 2008 Wiley‐Liss, Inc.