Efficient amidation of C-peptide deleted NPY precursors by non-endocrine cells is affected by the presence of Lys-Arg at the C-terminus

Birgitte S. Wulff, Branimir Catipovic, Hiroshi Okamoto, Ulrik Gether, Thue W. Schwartz, Teit Eliot Johansen

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Post-translational processing of peptide precursors producing amidated, biologically active peptides generally occurs in specially differentiated endocrine or neural cells. However, we have previously shown that a C-peptide-deleted precursor of neuropeptide Y (NPY1-39) in which the precursor terminates in the sequence Gly-Lys-Arg was partially amidated by the non-endocrine cell line, CHO. In the present study we show that two other non-endocrine cell lines, NIH 3T3 and BHK, also possess amidating activities and that the NPY1-39 precursor was completely converted to NPY1-36 amide by the NIH 3T3 cell line. The role of the two basic residues (Lys-Arg) in the C-terminus was studied by transfection of a construct encoding a NPY precursor terminating with glycine alone. Both the CHO and NIH 3T3 cell lines, transfected with this construct, secreted a significantly smaller fraction of NPY reactive material as amidated NPY compared to the fraction of amidated NPY secreted by the cells transfected with the NPY1-39 precursor. It is concluded that the capacity to perform C-terminal amidation appears to be a universal feature of eukaryotic cells and that the carboxypeptidase E-like enzyme influences the amidation process, beyond its known ability to remove the C-terminal basic residues.

Original languageEnglish
Pages (from-to)135-141
Number of pages7
JournalMolecular and Cellular Endocrinology
Volume91
Issue number1-2
DOIs
Publication statusPublished - 1993 Feb

Keywords

  • Amidation
  • Neuropeptide Y
  • Non-endocrine cell line
  • Peptide precursor processing
  • Recombinant DNA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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