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Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms
- Source :
- FEBS Letters. 337:60-65
- Publication Year :
- 1994
- Publisher :
- Wiley, 1994.
-
Abstract
- Processing of rat prodynorphin (proDyn) by the mouse prohormone convertase PCI was investigated. Recombinant vaccinia virus vectors were used to coexpress proDyn and PC1 in rat PC12 pheochromocytoma and mouse AtT-20 corticotroph cells. In vitro experiments were also conducted by co-incubating purified proDyn and PC1. The results demonstrate that PC1 cleaves proDyn at pairs of basic residues to yield 10 and 16 kDa high molecular weight (HMW) intermediates. Additionally, PC1 cleaves proDyn at a single arginine residue to yield an 8 kDa product and the C-peptide. This demonstrates that PC1 cleaves proDyn at single and pairs of basic residues.
- Subjects :
- endocrine system
Arginine
Overexpression
Genetic Vectors
Molecular Sequence Data
Biophysics
Prohormone convertase
Neuropeptide
Vaccinia virus
CHO Cells
Dynorphin
Processing
Peptide hormone
Biology
Transfection
Cleavage (embryo)
PC12 Cells
Biochemistry
Cell Line
Structural Biology
Cricetinae
Genetics
Animals
Aspartic Acid Endopeptidases
Amino Acid Sequence
Protein Precursors
Molecular Biology
PC12 cell
chemistry.chemical_classification
Binding Sites
C-Peptide
Enkephalins
Cell Biology
Molecular biology
Recombinant Proteins
In vitro
Rats
Molecular Weight
Enzyme
Proprotein Convertase 1
chemistry
Proprotein Convertases
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 337
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....345800baa90cf5f294e3f76adf147b1b