Dipeptidylamino-tripeptidylcarboxypeptidase NEMP3 and DPP3 (DPP III) are the same protein.

Autor: Kropotova ES; Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute Named by B.P.Konstantinov of National Research Center 'Kurchatov Institute', Gatchina, Russian Federation; Laboratory of Natural Polymers, Institute of Macromolecular Compounds of the Russian Academy of Sciences, Saint-Petersburg, Russian Federation., Pavlova EN; Laboratory of Natural Polymers, Institute of Macromolecular Compounds of the Russian Academy of Sciences, Saint-Petersburg, Russian Federation., Naryzhny SN; Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute Named by B.P.Konstantinov of National Research Center 'Kurchatov Institute', Gatchina, Russian Federation., Mosevitsky MI; Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute Named by B.P.Konstantinov of National Research Center 'Kurchatov Institute', Gatchina, Russian Federation; Laboratory of Natural Polymers, Institute of Macromolecular Compounds of the Russian Academy of Sciences, Saint-Petersburg, Russian Federation. Electronic address: m_mosev@mail.ru.
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Aug 06; Vol. 616, pp. 110-114. Date of Electronic Publication: 2022 May 25.
DOI: 10.1016/j.bbrc.2022.05.078
Abstrakt: Earlier it was shown that a group of extracellular low-specific metallopeptidases is present in the mammalian brain Kropotova and Mosevitsky (2016) [1]. These enzymes are weakly connected to the axonal ends of neurons. They were named Neuron bound Extracellular MetalloPeptidases (NEMP). The enzyme named NEMP3 turned out to be a unique exopeptidase that exhibits two activities: it removes the dipeptide from the N-end of the peptide, and it can also remove the tripeptide from the C-end of the peptide. Therefore, NEMP3 possesses the activities of dipeptidylaminopeptidase and of tripeptidylcarboxypeptidase. Mass spectrometry has revealed a homology of NEMP3 with DPP3 (DPP III, EC3.4.14.4), known as cytosolic dipeptidylaminopeptidase. We isolated DPP3 from rat and bovine liver and brain by the procedures used for this purpose by other authors. The effect of DPP3 on test peptides is the same as that of NEMP3. In particular, all DPP3 samples delete the tripeptide (AKF) from the C-end of the test peptide blocked at the N-end. The data obtained show that NEMP3 and DPP3 are the same protein (enzyme). Thus, DPP3 has two exopeptidase activities: the previously known activity of dipeptidylaminopeptidase and the activity of tripeptidylcarboxypeptidase discovered in this study. Another discovery is the extracellular activity of DPP 3 in the mammalian brain near synapses, which controls neuropeptides. DPP3 is involved in various processes, but in many cases its role remains to be clarified. The results obtained in this study will be useful for solving these questions.
Competing Interests: Declaration of competing interest The authors declare no conflict of interests.
(Copyright © 2022 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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