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Titolo:
DIFFERENTIAL CATABOLIC FATE OF NEUROMEDIN-N AND NEUROTENSIN IN THE CANINE INTESTINAL-MUCOSA
Autore:
BARELLI H; MAO YK; VINCENT B; DANIEL EE; VINCENT JP; CHECLER F;
Indirizzi:
UNIV NICE,INST PHARMACOL MOLEC CELLULAIRE,CNRS,UPR 411,660 ROUTE LUCIOLES F-06560 VALBONNE FRANCE UNIV NICE,INST PHARMACOL MOLEC CELLULAIRE,CNRS,UPR 411,660 ROUTE LUCIOLES F-06560 VALBONNE FRANCE FAC HLTH SCI HAMILTON,DEPT NEUROSCI HAMILTON L8N 3Z5 ON CANADA
Titolo Testata:
Peptides
fascicolo: 3, volume: 14, anno: 1993,
pagine: 457 - 463
SICI:
0196-9781(1993)14:3<457:DCFONA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
VENTRAL TEGMENTAL AREA; DEGRADING METALLOENDOPEPTIDASE; NUCLEUS-ACCUMBENS; BRAIN; RAT; ENDOPEPTIDASE; PRECURSOR; INACTIVATION; PURIFICATION; POTENTIATION;
Keywords:
NEUROTENSIN; NEUROMEDIN-N; DEGRADATION; INTESTINE; MUCOSA; PEPTIDASES; AMINOPEPTIDASE-M; ENDOPEPTIDASE-24.11;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
H. Barelli et al., "DIFFERENTIAL CATABOLIC FATE OF NEUROMEDIN-N AND NEUROTENSIN IN THE CANINE INTESTINAL-MUCOSA", Peptides, 14(3), 1993, pp. 457-463

Abstract

We have established the peptidase content of a P2 fraction (enriched in synaptosomes) and plasma membranes prepared from canine intestinal mucosa. Fourteen exo- and endopeptidases were assayed with fluorimetric or chromogenic substrates and identified by means of specific peptidase inhibitors. Post-proline dipeptidyl aminopeptidase IV, aminopeptidase M, and carboxypeptidase A were the most abundant exopeptidases, while aminopeptidases A and B, dipeptidyl aminopeptidase, pyroglutamyl peptide hydrolase I, and carboxypeptidase B displayed little, if any, activity. Endopeptidase 24.11 was the only endopeptidase that was detected in high amount. By contrast, proline endopeptidase exhibited a lowactivity, while angiotensin-converting enzyme, endopeptidase 24.15, endopeptidase 24.16, and cathepsin B and D-like activities were not detected. The catabolic rates of the two related neuropeptides, neurotensin (NT) and neuromedin N (NN), established that NN was inactivated 16 to 24 times faster than NT by plasma membrane and P2 fractions, respectively. Furthermore, the two peptides underwent qualitatively distinctmechanisms of degradation. A phosphoramidon-sensitive formation of NT(1-10) was detected as the major NT catabolite, indicating that NT wassusceptible to an endoproteolytic cleavage elicited by endopeptidase 24.11. By contrast, NN was inactivated by the action of an exopeptidase at its N-terminus, leading to the formation of [des-Lys1]NN. The occurrence of this NN metabolite was prevented by bestatin and actinonin,but not by the aminopeptidase B inhibitor, arphamenine B, indicating that the release of the N-terminal residue of NN was likely due to aminopeptidase M. The drastically different catabolic rates of NT and NN could support the possibility that inactivating mechanisms directly influence the fate of the two peptides in the intestine and, therefore, modulate their putative paracrine/endocrine function in the periphery.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 12:54:35