Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides
- 2 November 2010
- journal article
- review article
- Published by Elsevier in Neuropeptides
- Vol. 44 (6) , 457-466
- https://doi.org/10.1016/j.npep.2010.08.003
Abstract
No abstract availableKeywords
This publication has 57 references indexed in Scilit:
- Analysis of peptides in prohormone convertase 1/3 null mouse brain using quantitative peptidomicsJournal of Neurochemistry, 2010
- Effects of chromogranin A deficiency and excess in vivo: biphasic blood pressure and catecholamine responsesJournal Of Hypertension, 2010
- Neuropeptidomic analysis establishes a major role for prohormone convertase‐2 in neuropeptide biosynthesisJournal of Neurochemistry, 2010
- Catestatin: A multifunctional peptide from chromogranin APublished by Elsevier ,2010
- Cathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: Protease gene knockout and inhibitor studiesPeptides, 2009
- Human pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, α-MSH, and β-endorphinEndocrine, 2009
- Major Role of Cathepsin L for Producing the Peptide Hormones ACTH, β-Endorphin, and α-MSH, Illustrated by Protease Gene Knockout and ExpressionPublished by Elsevier ,2008
- Cathepsin L Proteolytically Processes Histone H3 During Mouse Embryonic Stem Cell DifferentiationCell, 2008
- Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expressionJournal of Neurochemistry, 2008
- Dynorphin and the pathophysiology of drug addictionPharmacology & Therapeutics, 2007