Abstract
Prolyl endopeptidase (E.C. 3.4.21.26, PREP) also known as prolyl oligopeptidase is an enzyme which cleaves several peptides at the carboxyl side of proline residues. Since brain contains relatively large amounts of this enzyme and because of its substrate specificity it has been suggested to play a role in the metabolism of neuropeptides, acting both on their maturation and their degradation. The final step of neuropeptide processing occurs in the synaptic vesicles and degradation of most of these peptides takes place in the synaptic cleft. Thus, a localization of PREP in these cellular compartments appears to be feasible. Here we summarize recent data and provide novel evidence for the subcellular localization of PREP. Most importantly, immunocytochemical double labelling, confocal laser scanning and electron microscopic procedures as well as functional assays strongly suggest a role for PREP in intracellular transport mechanisms and in protein secretion.
Keywords: β-amyloid, intracellular transport, prolyl endopeptidase, subcellular localization, POP, PREP, Protein Secretion, Amyloid precursor protein, Alzheimers disease, Nocodazole, Sarcophaga Peregrine
CNS & Neurological Disorders - Drug Targets
Title: Role of Prolyl Endopeptidase in Intracellular Transport and Protein Secretion
Volume: 10 Issue: 3
Author(s): M. Morawski, I. Schulz, U. Zeitschel, M. Blosa, G. Seeger and S. Roßner
Affiliation:
Keywords: β-amyloid, intracellular transport, prolyl endopeptidase, subcellular localization, POP, PREP, Protein Secretion, Amyloid precursor protein, Alzheimers disease, Nocodazole, Sarcophaga Peregrine
Abstract: Prolyl endopeptidase (E.C. 3.4.21.26, PREP) also known as prolyl oligopeptidase is an enzyme which cleaves several peptides at the carboxyl side of proline residues. Since brain contains relatively large amounts of this enzyme and because of its substrate specificity it has been suggested to play a role in the metabolism of neuropeptides, acting both on their maturation and their degradation. The final step of neuropeptide processing occurs in the synaptic vesicles and degradation of most of these peptides takes place in the synaptic cleft. Thus, a localization of PREP in these cellular compartments appears to be feasible. Here we summarize recent data and provide novel evidence for the subcellular localization of PREP. Most importantly, immunocytochemical double labelling, confocal laser scanning and electron microscopic procedures as well as functional assays strongly suggest a role for PREP in intracellular transport mechanisms and in protein secretion.
Export Options
About this article
Cite this article as:
Morawski M., Schulz I., Zeitschel U., Blosa M., Seeger G. and Roßner S., Role of Prolyl Endopeptidase in Intracellular Transport and Protein Secretion, CNS & Neurological Disorders - Drug Targets 2011; 10 (3) . https://dx.doi.org/10.2174/187152711794653805
DOI https://dx.doi.org/10.2174/187152711794653805 |
Print ISSN 1871-5273 |
Publisher Name Bentham Science Publisher |
Online ISSN 1996-3181 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Human Neural Stem and Progenitor Cells: In Vitro and In Vivo Properties, and Potential for Gene Therapy and Cell Replacement in the CNS
Current Gene Therapy Nanofibers: New Insights for Drug Delivery and Tissue Engineering
Current Topics in Medicinal Chemistry Advances in Photodynamic Therapy Assisted by Electroporation
Current Drug Metabolism Editorial [Hot Topic: TGF-β As Target in Oncology (Guest Editor: Karl-Hermann Schlingensiepen)]
Current Pharmaceutical Biotechnology Synthesis and In Vitro Evaluation of Some Isatin-Thiazolidinone Hybrid Analogues as Anti-Proliferative Agents
Medicinal Chemistry Design and Synthesis of Tetrahydroisoquinoline Derivatives as Anti-Angiogenesis and Anti-Cancer Agents
Anti-Cancer Agents in Medicinal Chemistry Melatonin Regulates Angiogenic Factors under Hypoxia in Breast Cancer Cell Lines
Anti-Cancer Agents in Medicinal Chemistry Liquid Crystal Nanodispersions Enable the Cutaneous Delivery of Photosensitizer for Topical PDT: Fluorescence Microscopy Study of Skin Penetration
Current Nanoscience The Safety of the Temozolomide in Patients with Malignant Glioma
Current Drug Safety Dual-target Inhibitors Based on BRD4: Novel Therapeutic Approaches for Cancer
Current Medicinal Chemistry Nasal Polyposis: An Overview of Differential Diagnosis and Treatment
Recent Patents on Inflammation & Allergy Drug Discovery Update on Cancer Related Issues of Mesenchymal Stem Cell-Based Therapies
Current Stem Cell Research & Therapy Current Overview of Inorganic Nanoparticles for the Treatment of Central Nervous System (CNS) Diseases
Current Nanomaterials Suppression of HIV Replication In Vitro by CpG and CpG Conjugated to the Non Toxic B Subunit of Cholera Toxin
Current HIV Research Entropy and Enthalpy in the Activity of Tubulin-Based Antimitotic Agents
Current Chemical Biology Water and Ion Channels: Crucial in the Initiation and Progression of Apoptosis in Central Nervous System?
Current Neuropharmacology Patent Selections
Recent Patents on Inflammation & Allergy Drug Discovery Nonsynaptic Receptors for GABA and Glutamate
Current Topics in Medicinal Chemistry Targeted Therapies in Gynecologic Cancers
Current Cancer Drug Targets Gold Nanoparticle-Based Drug Delivery Platform for Antineoplastic Chemotherapy
Current Drug Metabolism