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Transferrin is the main iron transport protein found in the circulation, and the level of transferrin saturation in the blood is an important indicator of iron status. The peptides amidated gastrin(17) (Gamide) and glycine-extended gastrin(17) (Ggly) are well known for their roles in controlling acid secretion and as growth factors in the gastrointestinal tract. | Definition of the residues required for the interaction between glycine-extended gastrin and transferrin in vitro Suzana Kovac1 Audrey Ferrand1 Jean-Pierre Esteve2 Anne B. Mason3 and Graham S. Baldwin1 1 Department of Surgery University of Melbourne Austin Health Victoria Australia 2 INSERM U.858 Plateforme d interaction moleculaire Institut Louis Bugnard Toulouse France 3 College of Medicine Department of Biochemistry University of Vermont Burlington VT USA Keywords ferric gastrin iron transferrin Correspondence G. S. Baldwin University of Melbourne Department of Surgery Austin Health Studley Road Heidelberg Victoria 3084 Australia Fax 61 3 9458 1650 Tel 61 3 9496 5592 E-mail grahamsb@unimelb.edu.au Received 2 March 2009 revised 27 May 2009 accepted 30 June 2009 doi 10.1111 j.1742-4658.2009.07186.x Transferrin is the main iron transport protein found in the circulation and the level of transferrin saturation in the blood is an important indicator of iron status. The peptides amidated gastrin 17 Gamide and glycine-extended gastrin 17 Ggly are well known for their roles in controlling acid secretion and as growth factors in the gastrointestinal tract. Several lines of evidence including the facts that transferrin binds gastrin that gastrins bind ferric ions and that the level of expression of gastrins positively correlates with transferrin saturation suggest the possible involvement of the transferrin-gastrin interaction in iron homeostasis. In the present work the interaction between gastrins and transferrin has been characterized by surface plasmon resonance and covalent crosslinking. First an interaction between iron-free apo-transferrin and Gamide or Ggly was observed. The fact that no interaction was observed in the presence of the chelator EDTA suggested that the gastrin-ferric ion complex was the interacting species. Moreover removal of ferric ions with EDTA reduced the stability of the complex between apo-transferrin and gastrins and no interaction was .
