Identification, Purification and Molecular Characterization of Chondrosin, a New Protein with Anti-tumoral Activity from the Marine Sponge Chondrosia Reniformis Nardo 1847

Bibliographic Details
Title: Identification, Purification and Molecular Characterization of Chondrosin, a New Protein with Anti-tumoral Activity from the Marine Sponge Chondrosia Reniformis Nardo 1847
Authors: Sonia Scarfì, Marina Pozzolini, Caterina Oliveri, Serena Mirata, Annalisa Salis, Gianluca Damonte, Daniela Fenoglio, Tiziana Altosole, Micha Ilan, Marco Bertolino, Marco Giovine
Source: Marine Drugs, Vol 18, Iss 8, p 409 (2020)
Publisher Information: MDPI AG, 2020.
Publication Year: 2020
Collection: LCC:Biology (General)
Subject Terms: Chondrosin, Chondrosia reniformis, marine toxin, cytotoxic protein, Porifera, Biology (General), QH301-705.5
More Details: Chondrosia reniformis is a common marine demosponge showing many peculiarities, lacking silica spicules and with a body entirely formed by a dense collagenous matrix. In this paper, we have described the identification of a new cytotoxic protein (chondrosin) with selective activity against specific tumor cell lines, from C. reniformis, collected from the Liguria Sea. Chondrosin was extracted and purified using a salting out approach and molecular weight size exclusion chromatography. The cytotoxic fractions were then characterized by two-dimensional gel electrophoresis and mass spectrometry analysis and matched the results with C. reniformis transcriptome database. The procedure allowed for identifying a full-length cDNA encoding for a 199-amino acids (aa) polypeptide, with a signal peptide of 21 amino acids. The mature protein has a theoretical molecular weight of 19611.12 and an IP of 5.11. Cell toxicity assays showed a selective action against some tumor cell lines (RAW 264.7 murine leukemia cells in particular). Cell death was determined by extracellular calcium intake, followed by cytoplasmic reactive oxygen species overproduction. The in silico modelling of chondrosin showed a high structural homology with the N-terminal region of the ryanodine receptor/channel and a short identity with defensin. The results are discussed suggesting a possible specific interaction of chondrosin with the Cav 1.3 ion voltage calcium channel expressed on the target cell membranes.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1660-3397
Relation: https://www.mdpi.com/1660-3397/18/8/409; https://doaj.org/toc/1660-3397
DOI: 10.3390/md18080409
Access URL: https://doaj.org/article/15cc061f2f2b4673a77c7ef3a533817f
Accession Number: edsdoj.15cc061f2f2b4673a77c7ef3a533817f
Database: Directory of Open Access Journals
More Details
ISSN:16603397
DOI:10.3390/md18080409
Published in:Marine Drugs
Language:English