Low plasma concentrations of retinol-binding protein in individuals with mutations affecting position 84 of the transthyretin molecule

Ric P. Waits, Toshiyuki Yamada, Tomoyuki Uemichi, Merrill D. Benson

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Retinol-binding protein (RBP), the principal carrier for vitamin A, is known to form a complex with transthyretin (TTR) for transport in plasma. Individuals from a kindred with the amino acid substitution of serine for isoleucine at position 84 (Ser84) of the TTR molecule show substantial reduction in plasma concentrations of RBP. In the present study, we measured plasma RBP in individuals from several kindreds, demonstrating 17 different point mutations within the TTR gene. In each case, these mutations caused single amino acid substitutions at various positions throughout the TTR molecule. Of all the individuals examined, only those with mutations causing amino acid substitutions at position 84 of the TTR molecule (Ser84 and Asn84) demonstrated substantial decreases in plasma concentrations of RBP. These results suggest that the isoleucine at position 84 on the TTR molecule may be critically involved in mediating RBP binding. Further, these findings demonstrate the importance of considering TTr gene mutations when clinically evaluating patients with low RBP.

Original languageEnglish (US)
Pages (from-to)1288-1291
Number of pages4
JournalClinical chemistry
Volume41
Issue number9
DOIs
StatePublished - 1995

Keywords

  • enzyme-linked immunosorbent assay
  • familial amyloidotic polyneuropathy
  • prealbumin

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, medical

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