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Titolo:
DISTINCT PROPERTIES OF NEURONAL AND ASTROCYTIC ENDOPEPTIDASE-3.4.24.16 - A STUDY ON DIFFERENTIATION, SUBCELLULAR-DISTRIBUTION, AND SECRETION PROCESSES
Autore:
VINCENT B; BEAUDET A; DAUCH P; VINCENT JP; CHECLER F;
Indirizzi:
CNRS UPR 411,INST PHARMACOL MOL & CELLULAIRE,660 ROUTE LUCIOLES F-06560 VALBONNE FRANCE CNRS UPR 411,INST PHARMACOL MOL & CELLULAIRE F-06560 VALBONNE FRANCE MCGILL UNIV,MONTREAL NEUROL INST,LAB NEUROANAT MONTREAL PQ H3A 2B4 CANADA
Titolo Testata:
The Journal of neuroscience
fascicolo: 16, volume: 16, anno: 1996,
pagine: 5049 - 5059
SICI:
0270-6474(1996)16:16<5049:DPONAA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUROTENSIN-DEGRADING METALLOENDOPEPTIDASE; PRIMARY CULTURED NEURONS; CARBOXYPEPTIDASE-E; DOG ILEUM; IN-VIVO; RAT; PROTEINS; PURIFICATION; BRAIN; CELLS;
Keywords:
NEURONS; ASTROCYTES; ENDOPEPTIDASE 3.4.24.16; DEGRADATION; SECRETION; NEUROPEPTIDES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
B. Vincent et al., "DISTINCT PROPERTIES OF NEURONAL AND ASTROCYTIC ENDOPEPTIDASE-3.4.24.16 - A STUDY ON DIFFERENTIATION, SUBCELLULAR-DISTRIBUTION, AND SECRETION PROCESSES", The Journal of neuroscience, 16(16), 1996, pp. 5049-5059

Abstract

Endopeptidase 3.4.24.16 belongs to the zinc-containing metalloprotease family and likely participates in the physiological inactivation of neurotensin. The peptidase displays distinct features in pure primary cultured neurons and astrocytes. Neuronal maturation leads to a decrease in the proportion of endopeptidase 3.4.24.16-bearing neurons and toa concomitant increase in endopeptidase 3.4.24.16 activity and mRNA content. By contrast, there is no change with time in endopeptidase 3.4.24.16 activity or content in astrocytes. Primary cultured neurons exhibit both soluble and membrane-associated endopeptidase 3.4.24.16 activity. The latter behaves as an ectopeptidase on intact plated neurons and resists treatments with 0.2% digitonin and Na2CO3. Further evidence for an association of the enzyme with plasma membranes was provided by cryoprotection experiments and electron microscopic analysis. The membrane-associated form of endopeptidase 3.4.24.16 increased during neuronal differentiation and appears to be mainly responsible for the overall augmentation of endopeptidase 3.4.24.16 activity observed duringneuronal maturation. Unlike neurons, astrocytes only contain soluble endopeptidase 3.4.24.16. Astrocytes secrete the enzyme through monensin, brefeldin A, and forskolin-independent mechanisms. This indicates that endopeptidase 3.4.24.16 is not released by classical regulated or constitutive secreting processes. However, secretion is blocked at 4 degrees C and by 8 bromo cAMP and is enhanced at 42 degrees C, two properties reminiscent of that of other secreted proteins lacking a classical signal peptide. By contrast, neurons appear unable to secrete endopeptidase 3.4.24.16.

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Documento generato il 31/03/20 alle ore 10:24:58