Background: Life scientists are often taught that proteins are comprised of a basic set of twenty amino acids. However, during the 1970's, it was discovered that a small subset of proteins contain selenocysteine, a 21st amino acid. Selenocysteine is structurally similar to cysteine, apart from it contains a selenium rather than a sulphur atom: this gives selenoproteins unique biochemical properties, particularly in terms of redox reactions. In this lecture, John Mackrill will review selenoprotein biology, particularly in terms of how selenium-containing proteins interact with lipids and calcium signalling mechanisms. He will also summarise some of the selenoprotein research that has been carried out in his laboratory.

Relevant Publications:

1. Hammoud Y, Rice T, Mackrill JJ. Oxysterols modulate calcium signalling in the A7r5 aortic smooth muscle cell-line. Biochimie. 2013 Mar;95(3):568-77.
2. Pierce WG, Zanette C, Caplice NM, Mackrill JJ. Calcium signalling in adult endothelial outgrowth cells. Biochem Biophys Res Commun. 2012 Jan 6;417(1):358-63.
3. Mackrill JJ. Oxysterols and calcium signal transduction. Chem Phys Lipids. 2011 Sep;164(6):488-95.
4. Jurynec MJ, Xia R, Mackrill JJ, Gunther D, Crawford T, Flanigan KM, Abramson JJ, Howard MT, Grunwald DJ. Selenoprotein N is required for ryanodine receptor calcium release channel activity in human and zebrafish muscle. Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12485-90.

Invitation: Gérard Lizard Equipe d'Accueil Bio-PeroxIL (EA7270

Le séminaire aura lieu à la Faculté de Médecine Dijon, Amphi Courtois à 11h00

Renseignements - omicheau@u-bourgogne.fr Tel: 03 80 39 34 68.