دورية أكاديمية
A Group of Weakly Bound to Neurons Extracellular Metallopeptidases (NEMPs).
| العنوان: | A Group of Weakly Bound to Neurons Extracellular Metallopeptidases (NEMPs). |
|---|---|
| المؤلفون: | Kropotova ES; Division of Molecular Biophysics, Petersburg Nuclear Physics Institute, Gatchina, 188300, Russia.; Institute of Macromolecular Compounds, Russian Academy of Sciences, Sanct Petersburg, 199034, Russia., Mosevitsky MI; Division of Molecular Biophysics, Petersburg Nuclear Physics Institute, Gatchina, 188300, Russia. m_mosev@mail.ru.; Institute of Macromolecular Compounds, Russian Academy of Sciences, Sanct Petersburg, 199034, Russia. m_mosev@mail.ru. |
| المصدر: | Neurochemical research [Neurochem Res] 2016 Oct; Vol. 41 (10), pp. 2666-2674. Date of Electronic Publication: 2016 Jun 27. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Kluwer Academic/Plenum Publishers Country of Publication: United States NLM ID: 7613461 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1573-6903 (Electronic) Linking ISSN: 03643190 NLM ISO Abbreviation: Neurochem Res Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 1999- : New York, NY : Kluwer Academic/Plenum Publishers Original Publication: New York, Plenum Press |
| مواضيع طبية MeSH: | Brain/*enzymology , Metalloproteases/*metabolism , Neurons/*enzymology, Animals ; Cattle ; Extracellular Space/enzymology ; Neuropeptides/metabolism ; Peptide Hydrolases/metabolism ; Rats ; Synaptosomes/metabolism |
| مستخلص: | We have found that isolated from mammalian brain (rat, bovine) axonal endings (synaptosomes) degrade peptides of different composition. With the use of low concentration of non ionic detergent Triton X-100 (0.05-0.1 %) four low specific metallopeptidases were detached from synaptosomes. These peptidases were named Neuronal EctoMetalloPeptidases (NEMPs). Using specially designed test-peptides they were characterized as: carboxypeptidase (NEMP1), aminopeptidase (NEMP2) and endopeptidases NEMP3 and NEMP4. NEMPs are true peptidases (oligopeptidases), because they are able efficiently degrade peptides containing less than 40 amino acid residues. Specific properties of some NEMPs were revealed. NEMP1 is a small protein (molecular mass of about 10 kDa), which tends to dynamic oligomerization. NEMP3 needs activation. Some amino acids activate this enzyme. As far as we know, these properties were not ascribed to the known similarly localized peptidases. A possible physiological function of low specific NEMPs is participation in control of wide range of neuropeptides secreted in the synaptic cleft. However, NEMPs also due to their low specificity can destroy introduced in brain therapeutic peptides. The data obtained in this study open new opportunities for the protection of synthetic therapeutic peptides in brain and, possibly, in other tissues. |
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| فهرسة مساهمة: | Keywords: Axonal ends; Extracellular peptidases; Neuropeptides; Protection of therapeutic peptides; Synaptosomes |
| المشرفين على المادة: | 0 (Neuropeptides) EC 3.4.- (Metalloproteases) EC 3.4.- (Peptide Hydrolases) EC 3.4.- (oligopeptidase) |
| تواريخ الأحداث: | Date Created: 20160629 Date Completed: 20170404 Latest Revision: 20181113 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1007/s11064-016-1979-9 |
| PMID: | 27350576 |
| قاعدة البيانات: | MEDLINE |
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