Secretion of human insulin by a transformed yeast cell

FEBS Lett. 1987 Feb 23;212(2):307-12. doi: 10.1016/0014-5793(87)81366-2.

Abstract

A yeast expression plasmid encoding a mini-proinsulin molecule was constructed and transformed into Saccharomyces cerevisiae. The plasmid encoded the sequence: B-Arg-Arg-Leu-Gln-Lys-Arg-A in which B represents the B-chain (30 amino acid residues) and A represents the A-chain (21 amino acid residues) of human insulin. The secreted peptides were shown to be a mixture of human insulin and des(B-30)human insulin. Thus, correct disulphide bridges can be established in proinsulin-like molecules devoid of a normal C-peptide region. Furthermore, the specificity of the yeast processing enzymes is so similar to the proinsulin converting enzymes in the human pancreatic beta-cell that it allows the processing of the mini-proinsulin to insulin.

MeSH terms

  • Amino Acid Sequence
  • Genes*
  • Humans
  • Insulin / biosynthesis
  • Insulin / genetics*
  • Peptide Mapping
  • Plasmids
  • Recombinant Proteins / isolation & purification
  • Saccharomyces cerevisiae / genetics*
  • Transformation, Genetic*

Substances

  • Insulin
  • Recombinant Proteins