Nonhuman Cells Correctly Sort and Process the Human Lysosomal Enzyme Cathepsin D

Gregory E. Conner, Jenny A. Udey, Juan Sola, Cristina Pinto

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Cathepsin D, like most lysosomal enzymes, undergoes multiple proteolytic cleavages during its lifetime. Although the significance of the earliest cleavages of cathepsin D is apparent (loss of the NH2-terminal signal peptide and activation peptide), functions of the two later cleavages are not understood and do not occur in all species. To examine these later events, a cDNA coding for human cathepsin D, which is normally processed to a two-chain form, was isolated and then expressed in mammalian cells from species which do not process the enzyme to the two-chain form. Analysis of the expressed human cathepsin D demonstrated proteolytic processing identical with that seen in normal human fibroblasts. Since processing to the two-chain form of the enzyme occurs in the lysosome, these studies revealed that the human cathepsin D was correctly sorted. The data also indicated that the sorting mechanism was conserved between diverse species and that late proteolytic processing in a variety of species was not determined by the presence or absence of the processing enzymes in the cell.

Original languageEnglish (US)
Pages (from-to)3530-3533
Number of pages4
JournalBiochemistry
Volume28
Issue number8
DOIs
StatePublished - Apr 1 1989

ASJC Scopus subject areas

  • Biochemistry

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