Molecular characterization and biochemical studies on a newly identified galectin-8 from P.lividus. (Abstract/Comunicazione in atti di convegno)

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  • Molecular characterization and biochemical studies on a newly identified galectin-8 from P.lividus. (Abstract/Comunicazione in atti di convegno) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Alternative label
  • K.Karakostis1,2, C.Costa1, F.Zitoa, H.C.Schröder2, W.E.G. Müller2, V.Matranga1 (2012)
    Molecular characterization and biochemical studies on a newly identified galectin-8 from P.lividus.
    in 14° Echinoderm Conference, Bruxelles, 20-24 agosto 2012
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • K.Karakostis1,2, C.Costa1, F.Zitoa, H.C.Schröder2, W.E.G. Müller2, V.Matranga1 (literal)
Note
  • Comunicazione (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1Consiglio Nazionale delle Ricerche, Istituto di Biomedicina e Immunologia Molecolare \"Alberto Monroy\", Via Ugo La Malfa 153, 90146 Palermo, Italy. 2Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Duesbergweg 6, D-55099 Mainz, Germany (literal)
Titolo
  • Molecular characterization and biochemical studies on a newly identified galectin-8 from P.lividus. (literal)
Abstract
  • Galectins are well conserved carbohydrate-binding proteins that interact with cell-surface glyco-conjugates and integrins to regulate diverse cellular events. In this study we identified and characterized galectin-8 in the Paracentrotus lividus sea urchin embryo. The cDNAsequence was isolated by EST data mining, RT-PCR and 3' RACE (Accession number: FR716469). The analysis of the protein (34.7 kDa) revealed Pl-galectin-8 as a novel member of the Galectin-8 family for the presence of two tandem carbohydrate-recognition domains (CRDs). A 3D structure model of the amino-terminal domain was created based on the solved structure of Human Galectin-8. The mRNA expression was highly regulated during development from blastula to pluteus stages, as monitored by comparative qPCR and spatially it was restricted to the gut, as observed by whole mount in situ hybridization. In view of future biomedical and biotechnological applications, we expressed the coding sequence of the Pl-galectin-8 after cloning in the expression vector pCOLD -TF. After purification the Pl-GALECTIN-8 recombinant protein was assayed for functional activity. In the haemmagglutination assay the protein showed an agglutination ability. Among sugars (lactose, mannose, maltose, sucrose and glucose) only lactose had an inhibitory effect on its activity, showing specificity in the interaction protein-carbohydrates. Furthermore, the biological role of Pl-GALECTIN-8 was demonstrated by a cell adhesion assay using human hepatoma (Hep-G2) cells, where cell adhesion was inhibited in presence of Pl-GALECTIN-8, probably as a result of its interaction with glycoproteins or glycoconjugates at cell surface. This work describes for the first time the molecular characterization and biological activity of galectin-8 in the sea urchin, paving the way for further studies on its role in embryonic development. This project has been funded by BIOMINTEC (EU 7FP Marie Curie ITN). The first author has been sponsored by the above mentioned grant. (literal)
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