Production and properties of a recombinant soluble form of aminopeptidase A

Gilles Vazeux, Sherwin Wilk, Elizabeth Wilk, Pierre Corvol, Catherine Llorens-Cortès

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11 Scopus citations


Aminopeptidase A is a homodimeric membrane-bound zinc metallopeptidase anchored at the plasma membrane by a 22-amino-acid hydrophobic segment. The anchor segment separates a small N-terminal cytoplasmic domain from a large ectodomain that contains the active site. Site-directed mutagenesis was performed to investigate the role of the cytoplasmic domain of aminopeptidase A in membrane anchoring and routing of the enzyme. Expression in COS-7 cells of a mutant lacking the N-terminal cytoplasmic domain resulted in the efficient secretion of a catalytically active enzyme in the medium. The soluble mutated aminopeptidase A, purified from the medium of a stable cell line, exhibited similar biochemical features to those of the wild-type enzyme. Pulse/chase metabolic labeling experiments revealed that the soluble form is generated intracellularly at an early stage of biosynthesis, suggesting that the signal peptide/membrane anchor domain of aminopeptidase A is removed in the endoplasmic reticulum through the action of the signal peptidase.

Original languageEnglish
Pages (from-to)671-678
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number3
StatePublished - 15 Jun 1998


  • Aminopeptidase A
  • Ectopeptidase
  • Solubilization
  • Type II protein
  • Zinc metallopeptidase


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