Catabolism of the octadecaneuropeptide ODN by prolyl endopeptidase: Identification of an unusual cleavage site

Leprince, Jérôme; Cosquer, David; Bellemère, Gaëlle; Chatenet, David; Tollemer, Hélène; Jégou, Sylvie; Tonon, Marie‐Christine; Vaudry, Hubert

doi:10.1016/j.peptides.2005.11.024

Cited by 11 publications

(6 citation statements)

References 48 publications

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“…Proline‐specific peptidases have been studied in many organisms and they include endopeptidases (postproline cleaving enzyme and proline‐specific endopeptidase), N‐terminal exopeptidases (postproline dipeptidyl aminopeptidase, proline iminopeptidase and aminopeptidase P), C‐terminal exopeptidases (prolylcarboxypeptidase and carboxypeptidase P) and dipeptidases (prolyl dipeptidase and proline dipeptidase) 15–17. To our best knowledge, their use in mass spectrometry (MS) of proteins and peptides is not frequent 18…”

Section: Introductionmentioning

confidence: 99%

Identification of N‐glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

et al. 2009

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An acidic prolyl endoprotease from Aspergillus niger was isolated from the commercial product Brewers Clarex to evaluate its possible application in proteomics. The chromatographic purification yielded a single protein band in sodium dodecyl sulfate polyacrylamide gel electrophoresis providing an apparent molecular mass of 63 kDa and a broad peak (m/z 58,061) in linear matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) indicating the glycoprotein nature of the enzyme. Indeed, a colorimetric assessment with phenol and sulfuric acid showed the presence of neutral sugars (9% of weight). The subsequent treatment with N-glycosidase F released a variety of high-mannose type N-glycans, which were successfully detected using MALDI-TOF MS. MALDI-TOF/TOF tandem MS analysis of glycopeptides from a tryptic digest of prolyl endoprotease unraveled the identity of the N-glycosylation site in the primary structure. The data obtained also show that the enzyme is present in its processed form, i.e. without putative signal and propeptide parts. Spectrophotometric measurements demonstrated optimal activity at pH 4.0-4.5 and also high thermostability for the cleavage at the C-terminal part of proline residues. In-solution digestion of standard proteins (12-200 kDa) allowed to evaluate the cleavage specificity. The enzyme acts upon proline and alanine residues, but there is an additional minor cleavage at some other residues like Gly, Leu, Arg, Ser and Tyr. The digestion of a honeybee peptide comprising six proline residues (apidaecin 1A) led to the detection of specific peptides terminated by proline as it was confirmed by MALDI postsource decay analysis.

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Section: Introductionmentioning

confidence: 99%

Identification of N‐glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

et al. 2009

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“…POP is able to hydrolyze also some other peptide bonds in addition to -Pro-Xaa. Leprince et al (2006) observed that POP can break Ala-Thr and Val-Gly peptide bonds of octadecaneuropeptide in a POP inhibitor–sensitive manner but with lower efficacy than the proline bond. POP has also been shown to hydrolyze the Cys-Xaa peptide bond in the novel neuroprotective peptide, humanin (Bär et al 2006).…”

mentioning

confidence: 99%

“…POP is able to hydrolyze also some other peptide bonds in addition to -Pro-Xaa. Leprince et al (2006) observed that POP can break Ala-Thr and Val-Gly peptide bonds of octadecaneuropeptide in a POP inhibi- Kato et al 1980a;Fuse et al 1990;Agirregoitia et al 2007 Changes in POP protein localization during maturation Moreno-Baylach et al 2008 Nuclear localization in peripheral tissues Myöhänen et al 2008c Blockade of cell differentiation and proliferation after POP inhibitor administration Ohtsuki et al 1994Ohtsuki et al ,1997b Inositol (1,4,5)-triphosphate (IP 3 ) signalling Increased IP 3 levels after POP inhibitor dosing Schulz et al 2002;Williams et al 2002 Neuronal protection POP inhibitors prevented the formation of cell stress-related factors Puttonen et al 2006 Protein secretion POP closely localized with microtubules Schulz et al 2005 POP, prolyl oligopeptidase.…”

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confidence: 99%

Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity

Myöhänen

Garcı́a-Horsman

Tenorio-Laranga

et al. 2009

J Histochem Cytochem.

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Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30 amino acids. POP may be associated with cognitive functions, possibly via the cleavage of neuropeptides. Recent studies have also suggested novel non-hydrolytic and non-catalytic functions for POP. Moreover, POP has also been proposed as a regulator of inositol 1,4,5-triphosphate signaling and several other functions such as cell proliferation and differentiation, as well as signal transduction in the central nervous system, and it is suspected to be involved in pathological conditions such as Parkinson's and Alzheimer's diseases and cancer. POP inhibitors have been developed to restore the depleted neuropeptide levels encountered in aging or in neurodegenerative disorders. These compounds have shown some antiamnesic effects in animal models. However, the mechanisms of these hypothesized actions are still far from clear. Moreover, the physiological role of POP has remained unknown, and a lack of basic studies, including its distribution, is obvious. The aim of this review is to gather information about POP and to propose some novel roles for this enzyme based on its distribution and its discordant spatial association with its best known substrates.

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“…Goldfish ODN (QATVGDVNTARPGMLDFT, deduced from the goldfish DBI sequence, ) and the metabotrophic endozepine receptor antagonist c d LOP were synthesised by solid‐phase methodology as described previously . The central‐type benzodiazepine receptor antagonist flumazenil (ethyl‐8‐fluoro‐5,6‐dihydro‐5‐methyl‐6‐oxo‐4 H ‐imidazo[1,5‐a][1,4]benzodiazepine‐3‐carboxylate) was purchased from Maruishi Pharmaceutical (Osaka, Japan).…”

Section: Methodsmentioning

confidence: 99%

“…Goldfish ODN (QATVGDVNTARPGMLDFT, deduced from the goldfish DBI sequence, AB618203) and the metabotrophic endozepine receptor antagonist cDLOP were synthesised by solid-phase methodology as described previously (12,29,35,48,49). The central-type benzodiazepine receptor antagonist flu-…”

Section: Pharmacological Reagentsmentioning

confidence: 99%

The Octadecaneuropeptide Stimulates Somatolactin Release from Cultured Goldfish Pituitary Cells

Azuma

Wada

Leprince

et al. 2013

J Neuroendocrinology

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The present study aimed to investigate the distribution of the octadecaneuropeptide (ODN) in the goldfish brain and to look for a possible effect of ODN on somatolactin (SL) release from pituitary cells. A discrete population of ODN‐immunoreactive neurones was localised in the lateral part of the nucleus lateralis tuberis. These neurones sent projections through the neurohypophyseal tract towards the neurohypophysis, and nerve fibres were seen in the close vicinity of SL‐producing cells in the pars intermedia. Incubation of cultured goldfish pituitary cells with graded concentrations of ODN (10−9–10−5 m) induced a dose‐dependent stimulation of SL‐β, but not SL‐α, release. ODN‐evoked SL release was blocked by the metabotrophic endozepine receptor antagonist cyclo1–8[DLeu5]OP but was not affected by the central‐type benzodiazepine receptor antagonist flumazenil. ODN‐induced SL release was suppressed by treatment with the phospholipase C (PLC) inhibitor U‐73122 but not with the protein kinase A (PKA) inhibitor H‐89. These results indicate that, in fish, ODN produced by hypothalamic neurones acts as a hypophysiotrophic neuropeptide stimulating SL release. The effect of ODN is mediated through a metabotrophic endozepine receptor positively coupled to the PLC/inositol 1,4,5‐trisphosphate/protein kinase C‐signalling pathway.

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Catabolism of the octadecaneuropeptide ODN by prolyl endopeptidase: Identification of an unusual cleavage site

Cited by 11 publications

References 48 publications

Identification of N‐glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

Identification of N‐glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity

The Octadecaneuropeptide Stimulates Somatolactin Release from Cultured Goldfish Pituitary Cells

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