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  Crystal Structure of Crataeva tapia Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines

Ferreira, R. d. S., Zhou, D., Ferreira, J. G., Cabral Silva, M. C., Silva-Lucca, R. A., Mentele, R., et al. (2013). Crystal Structure of Crataeva tapia Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines. PLOS ONE, 8(6): e64426. doi:10.1371/journal.pone.0064426.

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 Urheber:
Ferreira, Rodrigo da Silva1, Autor
Zhou, Dongwen1, Autor
Ferreira, Joana Gasperazzo1, Autor
Cabral Silva, Mariana Cristina1, Autor
Silva-Lucca, Rosemeire Aparecida1, Autor
Mentele, Reinhard2, Autor           
Paredes-Gamero, Edgar Julian1, Autor
Bertolin, Thiago Carlos1, Autor
dos Santos Correia, Maria Tereza1, Autor
Guedes Paiva, Patricia Maria1, Autor
Gustchina, Alla1, Autor
Wlodawer, Alexander1, Autor
Vilela Oliva, Maria Luiza1, Autor
Affiliations:
1external, ou_persistent22              
2Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              

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Schlagwörter: TRYPSIN-INHIBITOR; SERINE RESIDUE; REACTIVE SITE; BINDING; LECTIN; APOPTOSIS; MECHANISM; SEEDS; DU145; GLYCOSAMINOGLYCANS
 Zusammenfassung: A protein isolated from the bark of Crataeva tapia (CrataBL) is both a Kunitz-type plant protease inhibitor and a lectin. We have determined the amino acid sequence and three-dimensional structure of CrataBL, as well as characterized its selected biochemical and biological properties. We found two different isoforms of CrataBL isolated from the original source, differing in positions 31 (Pro/Leu); 92 (Ser/Leu); 93 (Ile/Thr); 95 (Arg/Gly) and 97 (Leu/Ser). CrataBL showed relatively weak inhibitory activity against trypsin (K-iapp = 43 mu M) and was more potent against Factor Xa (K-iapp = 8.6 mu M), but was not active against a number of other proteases. We have confirmed that CrataBL contains two glycosylation sites and forms a dimer at high concentration. The high-resolution crystal structures of two different crystal forms of isoform II verified the beta-trefoil fold of CrataBL and have shown the presence of dimers consisting of two almost identical molecules making extensive contacts (similar to 645 angstrom(2)). The structure differs from those of the most closely related proteins by the lack of the N-terminal beta-hairpin. In experiments aimed at investigating the biological properties of CrataBL, we have shown that addition of 40 mM of the protein for 48 h caused maximum growth inhibition in MTT assay (47% of DU145 cells and 43% of PC3 cells). The apoptosis of DU145 and PC3 cell lines was confirmed by flow cytometry using Annexin V/FITC and propidium iodide staining. Treatment with CrataBL resulted in the release of mitochondrial cytochrome c and in the activation of caspase-3 in DU145 and PC3 cells.

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Sprache(n): eng - English
 Datum: 2013
 Publikationsstatus: Online veröffentlicht
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
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 Identifikatoren: ISI: 000320576400001
DOI: 10.1371/journal.pone.0064426
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Titel: PLOS ONE
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA : PUBLIC LIBRARY SCIENCE
Seiten: - Band / Heft: 8 (6) Artikelnummer: e64426 Start- / Endseite: - Identifikator: ISSN: 1932-6203