Retinol-induced secretion of human retinol-binding protein in yeast

FEBS Lett. 1998 May 8;427(2):213-9. doi: 10.1016/s0014-5793(98)00428-1.

Abstract

Retinol-binding protein (RBP) functions as a transporter for retinol (vitamin A) in plasma in higher eukaryotes. We have successfully expressed human RBP in Saccharomyces cerevisiae, and its secretion was found to be induced by retinol also in this lower eukaryote. Reduced induction of secretion by retinol in a temperature-sensitive sec18-1 mutant that is blocked in secretion at the restricted temperature suggests that as in mammalian cells, RBP can be released from the endoplasmic reticulum upon addition of retinol. Thus, the molecular mechanism involved in retinol-dependent secretion of RBP appears to be conserved in yeast, and this points to yeast as a putative model system for studying retinol-regulated secretion of RBP. RBP purified from yeast was found to be indistinguishable from RBP purified from human plasma in several functional assays.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases*
  • Fenretinide
  • Fungal Proteins / genetics
  • Humans
  • Ligands
  • Mutation
  • Prealbumin / metabolism
  • Protein Binding
  • Recombinant Fusion Proteins
  • Retinoids / pharmacology
  • Retinol-Binding Proteins / genetics
  • Retinol-Binding Proteins / metabolism*
  • Retinol-Binding Proteins, Plasma
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Vesicular Transport Proteins*
  • Vitamin A / metabolism
  • Vitamin A / pharmacology*

Substances

  • Fungal Proteins
  • Ligands
  • Prealbumin
  • Recombinant Fusion Proteins
  • Retinoids
  • Retinol-Binding Proteins
  • Retinol-Binding Proteins, Plasma
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins
  • Vitamin A
  • Fenretinide
  • Adenosine Triphosphatases
  • SEC18 protein, S cerevisiae