Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites

J Biochem. 1991 Jun;109(6):803-6. doi: 10.1093/oxfordjournals.jbchem.a123461.

Abstract

We cloned and sequenced a cDNA from a library of mouse pituitary AtT-20 cells which are known to cleave an endogenous and various foreign prohormones at dibasic sites. This cDNA encodes a novel 753-residue protein, named PC3, which is structurally related to the yeast Kex2 protease involved in precursor cleavage at dibasic sites and to recently identified mammalian Kex2-like proteins, furin and PC2. Among examined cell lines and tissues, PC3 mRNA was only detected in AtT-20 cells. The substrate specificity of PC3 expressed in mammalian cells was similar to that observed in AtT-20 cells. We conclude that PC3 is a resident prohormone processing endoprotease in AtT-20 cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Cell Line
  • Cloning, Molecular
  • DNA / genetics
  • Gene Expression Regulation, Enzymologic
  • Hormones / metabolism*
  • Mice
  • Molecular Sequence Data
  • Pro-Opiomelanocortin / biosynthesis
  • Pro-Opiomelanocortin / genetics*
  • Proprotein Convertases
  • Receptors, Cell Surface / metabolism
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*
  • Substrate Specificity

Substances

  • Hormones
  • Receptors, Cell Surface
  • Pro-Opiomelanocortin
  • DNA
  • Proprotein Convertases
  • Serine Endopeptidases

Associated data

  • GENBANK/M63255
  • GENBANK/M64332
  • GENBANK/S57661
  • GENBANK/S57664
  • GENBANK/S64490
  • GENBANK/S69601
  • GENBANK/S69604
  • GENBANK/S69828
  • GENBANK/S69830
  • GENBANK/X57088