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Titolo:
MOLECULAR-CLONING AND EXPRESSION OF RAT-BRAIN ENDOPEPTIDASE-3.4.24.16
Autore:
DAUCH P; VINCENT JP; CHECLER F;
Indirizzi:
INST PHARMACOL MOLEC & CELLULAIRE,660 ROUTE LUCIOLES F-06560 VALBONNEFRANCE INST PHARMACOL MOLEC & CELLULAIRE F-06560 VALBONNE FRANCE
Titolo Testata:
The Journal of biological chemistry
fascicolo: 45, volume: 270, anno: 1995,
pagine: 27266 - 27271
SICI:
0021-9258(1995)270:45<27266:MAEORE>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANGIOTENSIN-CONVERTING ENZYME; NEUROTENSIN-DEGRADING METALLOENDOPEPTIDASE; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; AMINO-ACID SEQUENCE; SOLUBLE METALLOENDOPEPTIDASE; MICROSOMAL ENDOPEPTIDASE; PROCESSING PROPROTEINS; SUBSTRATE-SPECIFICITY; SYNAPTIC-MEMBRANES; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
P. Dauch et al., "MOLECULAR-CLONING AND EXPRESSION OF RAT-BRAIN ENDOPEPTIDASE-3.4.24.16", The Journal of biological chemistry, 270(45), 1995, pp. 27266-27271

Abstract

We have isolated by immunological screening of a lambda ZAPII cDNA library constructed from rat brain mRNAs a cDNA clone encoding endopeptidase 3.4.24.16. The longest open reading frame encodes a 704-amino acid protein with a theoretical molecular mass of 80,202 daltons and bears the consensus sequence of the zinc metalloprotease family, The sequence exhibits a 60.2% homology with those of another zinc metallopeptidase, endopeptidase 3.4.24.15, Northern blot analysis reveals two mRNA species of about 3 and 5 kilobases in rat brain, ileum, kidney, and testis, We have transiently transfected COS-7 cells with pcDNA(3) containing the cloned cDNA and established the overexpression of a 70-75-kDaimmunoreactive protein. This protein hydrolyzes QFS, a quenched fluorimetric substrate of endopeptidase 3.4.24.16, and cleaves neurotensin at a single peptide bond, leading to the formation of neurotensin (1-10) and neurotensin (11-13), QFS and neurotensin hydrolysis are potently inhibited by the selective endopeptidase 3.4.24.16 dipeptide blockerpro-lie and by dithiothreitol, while the enzymatic activity remains unaffected by phosphoramidon and captopril, the specific inhibitors of endopeptidase 3.4.24.11 and angiotensin-converting enzyme, respectively, Altogether, these physicochemical, biochemical, and immunological properties unambiguously identify endopeptidase 3.4.24.16 as the protein encoded by the isolated cDNA clone.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 11:42:26