Characterization of metalloproteinase-like activities in barnacle (Balanus amphitrite) nauplii (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Characterization of metalloproteinase-like activities in barnacle (Balanus amphitrite) nauplii (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/S1096-4959(03)00049-6 (literal)

Alternative label

• Mannello, F; Canesi, L; Faimali, M; Piazza, V; Gallo, G; Geraci, S (2003)
  Characterization of metalloproteinase-like activities in barnacle (Balanus amphitrite) nauplii
  in Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Mannello, F; Canesi, L; Faimali, M; Piazza, V; Gallo, G; Geraci, S (literal)

Pagina inizio

• 17 (literal)

Pagina fine

• 24 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 135 (literal)

Rivista

• Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 8 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 1 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• University of Urbino; University of Urbino; University of Genoa (literal)

Titolo

• Characterization of metalloproteinase-like activities in barnacle (Balanus amphitrite) nauplii (literal)

Abstract

• The presence of extracellular matrix (ECM) degrading enzymes was investigated in naupliar stages of the barnacle Balanus aniphitrite Darwin. The results of substrate gel-zymography and quantitative assays demonstrated that naupliar extracts contain several protease activities that are specific towards gelatin substrates; some caseinolytic activity was also detected. Substrate specificity was observed in all naupliar stages (II-VI). The gelatinolytic activities showed dependence on both Ca2+ and Zn2+ and inhibition by EDTA, EGTA, and 1,10-phenanthroline. Also Mg2+ partially activated the enzymes, whereas Cd2+, Cu2+, Hg2+ and Pb2+ were inhibitory. The thermal denaturation profile was significantly different in the presence and absence of Ca2+ and Zn2+. Overall, the results indicate that the Ca2+/Zn2+-dependent gelatinase activities in barnacle nauplii belong to the subfamily of matrix metalloproteases. Barnacle larvae MMPs showed biochemical characteristics different from those of vertebrate MMPs but common to other gelatinases from marine invertebrates: they were unaffected by several protease inhibitors and insensitive to specific activators/inhibitors of vertebrate MMPs. The presence of NIMP-like activities in different naupliar stages suggests a constitutive role for these enzymes in ECM remodeling during barnacle larvae growth and development. (C) 2003 Elsevier Science Inc. All rights reserved. (literal)

Prodotto di

• Marine science institute (ISMAR) (Istituto)

Autore CNR

• MARCO FAIMALI (Unità di personale interno)
• SEBASTIANO GERACI (Unità di personale interno)
• VERONICA PIAZZA (Persona)

Insieme di parole chiave

• Parole chiave di "Characterization of metalloproteinase-like activities in barnacle (Balanus amphitrite) nauplii" (Insieme di parole chiave)

Incoming links:

Prodotto

• Marine science institute (ISMAR) (Istituto)

Autore CNR di

• SEBASTIANO GERACI (Unità di personale interno)
• MARCO FAIMALI (Unità di personale interno)
• VERONICA PIAZZA (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (Rivista)

Insieme di parole chiave di

• Parole chiave di "Characterization of metalloproteinase-like activities in barnacle (Balanus amphitrite) nauplii" (Insieme di parole chiave)