Nonhuman cells correctly sort and process the human lysosomal enzyme cathepsin D

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

Research output: Contribution to journalArticle

14 Citations (Scopus)

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
Pages (from-to)3530-3533
Number of pages4
JournalBiochemistry
Volume28
Issue number8
StatePublished - Dec 1 1989

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Cathepsin D
Enzymes
Processing
Fibroblasts
Protein Sorting Signals
Lysosomes
Sorting
Complementary DNA
Chemical activation
Cells
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Nonhuman cells correctly sort and process the human lysosomal enzyme cathepsin D. / Conner, Gregory E; Udey, Jenny A.; Sola, Juan E; Sola, Juan.

In: Biochemistry, Vol. 28, No. 8, 01.12.1989, p. 3530-3533.

Research output: Contribution to journalArticle

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