Enzymatic activity of soluble and membrane tethered peptide pro-hormone convertase 1

Angela Bruzzaniti, Richard E. Mains

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Pro-hormone convertases PC1 and PC2 perform endoproteolytic cleavages of precursors in peptide-containing secretory granules. PC1 and PC2 are soluble, secreted with bioactive peptides. Evolutionarily related PCs have membrane tethers, not secreted. We tethered PC1 to the transmembrane-cytoplasmic domains (CD) of a granule enzyme (peptidylglycine-α-amidating monooxygenase; PAM) and Golgi-localized PC8. The tethered PC1 is far more stable to elevated temperature and denaturants than soluble PC1, and more active. Both tethers allow PC1 to visit the cell surface transiently, cleaving soluble molecules outside the cell. Both membrane-bound PC1 chimeras cleave membrane PAM into soluble active fragments when PAM is expressed on adjacent cells.

Original languageEnglish (US)
Pages (from-to)863-875
Number of pages13
JournalPeptides
Volume23
Issue number5
DOIs
StatePublished - 2002
Externally publishedYes

Fingerprint

Pulse amplitude modulation
Peptide Hormones
Hormones
Membranes
Peptides
Secretory Vesicles
Mixed Function Oxygenases
Molecules
Temperature
Enzymes

Keywords

  • Amidation
  • Biosynthesis
  • Michaelis constant
  • Peptide processing
  • Routing
  • V

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Enzymatic activity of soluble and membrane tethered peptide pro-hormone convertase 1. / Bruzzaniti, Angela; Mains, Richard E.

In: Peptides, Vol. 23, No. 5, 2002, p. 863-875.

Research output: Contribution to journalArticle

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