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Title: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
; ; ; ;  [1]; ;  [2]
  1. Indiana Univ., Bloomington (United States)
  2. Univ. of Pavia (Italy)

At least 35 allelic variants of human serum albumin have been sequenced at the protein level. All except two COOH-terminal variants, Catania and Venezia, are readily explainable as single-point substitutions. The two chain-termination variants are clustered in certain locations in Italy and are found in numerous unrelated individuals. In order to correlate the protein change in these variants with the corresponding DNA mutation, the two variant albumin genes have been cloned, sequenced, and compared to normal albumin genomic DNA. In the Catania variant, a single base deletion and subsequent frameshift leads to a shortened and altered COOH terminus. Albumin Venezia is caused by a mutation that alters the first consensus nucleotide of the 5{prime} donor splice junction of intron 14 and the 3{prime} end of exon 14, which is shortened from 68 to 43 base pairs. This change leads to an exon skipping event resulting in direct splicing of exon 13 to exon 15. The predicted Venezia albumin product has a truncated amino acid sequence (580 residues instead of 585), and the COOH-terminal sequence is altered after Glu-571. The variant COOH terminus ends with the dibasic sequence Arg-Lys that is apparently removed through stepwise cleavage by serum carboxypeptidase B to yield several forms of circulating albumin.

OSTI ID:
6056241
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:14; ISSN 0027-8424
Country of Publication:
United States
Language:
English