Subcellular Localization, Partial Purification, and Characterization of a Dynorphin Processing Endopeptidase from Bovine Pituitary

@article{Devi1991SubcellularLP,
  title={Subcellular Localization, Partial Purification, and Characterization of a Dynorphin Processing Endopeptidase from Bovine Pituitary},
  author={Lakshmi Devi and P Gupta and Lloyd D Fricker},
  journal={Journal of Neurochemistry},
  year={1991},
  volume={56}
}
Abstract: An enzyme capable of cleaving dynorphin B‐29 to dynorphin B‐13 is present in bovine pituitary, with 40‐ to 50‐fold higher specific activity in the posterior and intermediate lobes than in the anterior lobe. Subcellular fractionation of bovine neurointermediate pituitary shows that this enzyme is present in the peptide‐containing secretory vesicles. The enzyme has been purified 2,800‐fold from whole bovine pituitaries using ion‐exchange and gel filtration chromatography. Purified… 
Purification and Characterization of a Dynorphin-processing Endopeptidase (*)
TLDR
Cleavage site determination with matrix-assisted laser desorption ionization time of flight (MALDITOF) mass spectrometry shows that DCE cleaves only those peptides that fit the predicted “consensus motif” for monobasic processing, consistent with a broader role for the dynorphin converting enzyme in the biosynthesis of many peptide hormones and neuropeptides by processing at monobAsic sites.
Posttranslational Processing of Carboxypeptidase E, a Neuropeptide‐Processing Enzyme, in AtT‐20 Cells and Bovine Pituitary Secretory Granules
TLDR
The data indicate that posttranslational processing of CPE occurs in secretory granules and that this activity may be mediated by a prohormone convertase‐like enzyme.
Specificity of the Dynorphin‐Processing Endoprotease: Comparison with Prohormone Convertases
TLDR
The results suggest that the cleavage specificity of the dynorphin converting enzyme is distinct but related to the Cleavage Specificity of the prohormone convertases and that multiple enzymes could be involved in the processing of peptide hormones and neuropeptides at monobasic and dibasic sites.
Purification and Characterization of Carboxypeptidase D, a Novel Carboxypeptidase E-like Enzyme, from Bovine Pituitary (*)
TLDR
Results suggest that CPD is a novel secretory pathway enzyme that may be the bovine homologue of gp180, a hepatitis B virus particle binding protein that shows 47% homology to CPE.
Processing of Procarboxypeptidase E into Carboxypeptidase E Occurs in Secretory Vesicles
TLDR
Pulse/chase analysis and findings suggest that the conversion of proCPE into CPE occurs primarily in secretory vesicles, and suggests that efficient proCPe processing requires an acidic post‐Golgi compartment.
Secretion and regulation of a neuropeptide-processing enzyme by AtT-20 cells.
  • L. Devi
  • Biology, Chemistry
    Endocrinology
  • 1992
TLDR
A role for DCE in posttranslational processing of regulatory peptides in AtT-20 cells is supported, suggesting that DCE activity is in the regulated pathway of secretion.
Prodynorphin Processing by Proprotein Convertase 2
TLDR
PC2 cleavages at single and paired basic residues were enhanced when carried out in the presence of carboxypeptidase (CP) E, and Enhancement was blocked by GEMSA, a specific inhibitor of CPE activity, and could be duplicated by other carboxypesptidases, including CPD, CPB, or CPM.
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TLDR
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