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1.	Bouyoucef, S E, et al. (author) Poster Session 2 : Monday 4 May 2015, 08 2015 In: European Heart Journal Cardiovascular Imaging. - : Oxford University Press (OUP). - 2047-2404 .- 2047-2412. ; 16 Suppl 1 Journal article (peer-reviewed)
2.	Czerwiec, E, et al. (author) Novel gamma-carboxyglutamic acid-containing peptides from the venom of Conus textile 2006 In: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 273:12, s. 2779-2788 Journal article (peer-reviewed)abstract The cone snail is the only invertebrate system in which the vitamin K-dependent carboxylase (or gamma-carboxylase) and its product gamma-carboxyglutamic acid (Gla) have been identified. It remains the sole source of structural information of invertebrate gamma-carboxylase substrates. Four novel Gla-containing peptides were purified from the venom of Conus textile and characterized using biochemical methods and mass spectrometry. The peptides Gla(1)-TxVI, Gla(2)-TxVI/A, Gla(2)-TxVI/B and Gla(3)-TxVI each have six Cys residues and belong to the O-superfamily of conotoxins. All four conopeptides contain 4-trans-hydroxyproline and the unusual amino acid 6-L >-bromotryptophan. Gla(2)-TxVI/A and Gla(2)-TxVI/B are isoforms with an amidated C-terminus that differ at positions +1 and +13. Three isoforms of Gla(3)-TxVI were observed that differ at position +7: Gla(3)-TxVI, Glu7-Gla(3)-TxVI and Asp7-Gla(3)-TxVI. The cDNAs encoding the precursors of the four peptides were cloned. The predicted signal sequences (amino acids -46 to -27) were nearly identical and highly hydrophobic. The predicted propeptide region (-20 to -1) that contains the gamma-carboxylation recognition site (gamma-CRS) is very similar in Gla(2)-TxVI/A, Gla(2)-TxVI/B and Gla(3)-TxVI, but is more divergent for Gla(1)-TxVI. Kinetic studies utilizing the Conus gamma-carboxylase and synthetic peptide substrates localized the gamma-CRS of Gla(1)-TxVI to the region -14 to -1 of the polypeptide precursor: the K-m was reduced from 1.8 mM for Gla (1)-TxVI lacking a propeptide to 24 mu M when a 14-residue propeptide was attached to the substrate. Similarly, addition of an 18-residue propeptide to Gla(2)-TxVI/B reduced the K-m value tenfold.

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Type of publication: journal article (2)

Type of content: peer-reviewed (2)

Author/Editor: Costa, G. (1); Robinson, J. (1); Santos, J. (1); Smith, M. (1); Brünner, S. (1); Robinson, S. (1); show more...; Li, Q. (1); Soerensen, J. (1); Antoni, Gunnar (1); Sörensen, Jens (1); Reid, S. (1); Svensson, M. (1); Menendez, D. (1); Takahashi, K (1); Yousefi, B (1); Wikstrom, G. (1); Soares, J (1); Bottcher, M. (1); Fernandez, J. (1); Yla-Herttuala, S (1); Torres, M. (1); Martinez, C (1); Ferrari, C. (1); Reddy, P (1); Ramos, D (1); Lehner, S. (1); Cheng, B (1); Johnson, L (1); Akil, S (1); Hedeer, F (1); Engblom, H (1); Hindorf, C (1); Sayed, S (1); Soriano, E (1); Lubberink, Mark (1); Martin, W (1); Yoshida, H (1); Fukuda, H. (1); Westermark, P (1); Yokota, S. (1); Carlson, K (1); Rodriguez, L. (1); Kero, Tanja (1); Saraste, A. (1); Knuuti, J. (1); Morvan, M (1); Choqueux, C (1); Nicoletti, A (1); Cohen, M. (1); Rosales, S (1); show less...

University: Uppsala University (1); Lund University (1)

Language: English (2)

Research subject (UKÄ/SCB): Natural sciences (1)

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