A novel aspartyl-proteinase from apocrine epithelia and breast tumors. (Articolo in rivista)

Type

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

Label

• A novel aspartyl-proteinase from apocrine epithelia and breast tumors. (Articolo in rivista) (literal)

Anno

• 2000-01-01T00:00:00+01:00 (literal)

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

• 10.1074/jbc.275.11.7935 (literal)

Alternative label

• Caputo E, Manco G, Mandrich L, Guardiola J. (2000)
  A novel aspartyl-proteinase from apocrine epithelia and breast tumors.
  in The Journal of biological chemistry (Print)
  (literal)

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

• Caputo E, Manco G, Mandrich L, Guardiola J. (literal)

Pagina inizio

• 7935 (literal)

Pagina fine

• 7941 (literal)

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

• 275 (literal)

Rivista

• ?The ?Journal of biological chemistry (Rivista)

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

• 7 (literal)

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

• 11 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• IGB, IBP (literal)

Titolo

• A novel aspartyl-proteinase from apocrine epithelia and breast tumors. (literal)

Abstract

• GCDFP-15 (gross cystic disease fluid protein, 15 kDa) is a secretory marker of apocrine differentiation in breast carcinoma. In human breast cancer cell lines, gene expression is regulated by hormones, including androgens and prolactin. The protein is also known under different names in different body fluids such as gp17 in seminal plasma. GCDFP-15/gp17 is a ligand of CD4 and is a potent inhibitor of T-cell apoptosis induced by sequential CD4/T-cell receptor triggering. We now report that GCDFP-15/gp17 is a protease exhibiting structural properties relating it to the aspartyl proteinase superfamily. Unexpectedly, GCDFP-15/gp17 appears to be related to the retroviral members rather than to the known cellular members of this class. Site-specific mutagenesis of Asp22 (predicted to be catalytically important for the active site) and pepstatin A inhibition confirmed that the protein is an aspartic-type protease. We also show that, among the substrates tested, GCDFP-15/ gp17 is specific for fibronectin. The study of GCDFP-15/ gp17-mediated proteolysis may provide a handle to understand phenomena as diverse as mammary tumor progression and fertilization. (literal)

Prodotto di

• Institute of protein biochemistry (IBP) (Istituto)
• Istituto di genetica e biofisica \"Adriano Buzzati Traverso\" (IGB) (Istituto)
• Analisi cellulare e molecolare della risposta immunitaria indotta da vaccini sintetici (SV.P15.009.002) (Modulo)

Autore CNR

• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale esterno)
• EMILIA CAPUTO (Persona)
• JOHN GUARDIOLA (Persona)

Insieme di parole chiave

• Keywords of "A novel aspartyl-proteinase from apocrine epithelia and breast tumors." (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale esterno)
• JOHN GUARDIOLA (Persona)
• EMILIA CAPUTO (Persona)

Prodotto

• Istituto di genetica e biofisica \"Adriano Buzzati Traverso\" (IGB) (Istituto)
• Institute of protein biochemistry (IBP) (Istituto)
• Analisi cellulare e molecolare della risposta immunitaria indotta da vaccini sintetici (SV.P15.009.002) (Modulo)

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

• ?The ?Journal of biological chemistry (Rivista)

Insieme di parole chiave di

• Keywords of "A novel aspartyl-proteinase from apocrine epithelia and breast tumors." (Insieme di parole chiave)