Study on the binding of lactotransferrin (lactoferrin) to human PHA-activated lymphocytes and non-activated platelets. Localisation and description of the receptor-binding site
| Autor: | Mazurier, J., Legrand, D., Leveugle, B., Rochard, E., Montreuil, J., Spik, G. |
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| Přispěvatelé: | Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 1994 |
| Předmět: |
Blood Platelets
Models Molecular Platelet Aggregation Molecular Sequence Data MESH: Protein Structure Secondary MESH: Binding Competitive Receptors Cell Surface MESH: Amino Acid Sequence Lymphocyte Activation Binding Competitive MESH: Phytohemagglutinins Protein Structure Secondary Iodine Radioisotopes Humans MESH: Lysine [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Lymphocytes Phytohemagglutinins MESH: Peptide Fragments MESH: Lymphocyte Activation MESH: Blood Platelets MESH: Platelet Aggregation MESH: Receptors Cell Surface MESH: Molecular Sequence Data MESH: Humans MESH: Adenosine Diphosphate MESH: Kinetics Lysine Cell Membrane MESH: Iodine Radioisotopes MESH: Lactoferrin Peptide Fragments Adenosine Diphosphate Kinetics Lactoferrin MESH: Platelet Aggregation Inhibitors MESH: Lymphocytes MESH: Models Molecular Platelet Aggregation Inhibitors MESH: Cell Membrane |
| Zdroj: | Advances in Experimental Medicine and Biology Advances in Experimental Medicine and Biology, Kluwer, 1994, 357, pp.111-9 Advances in Experimental Medicine and Biology, 1994, 357, pp.111-9 |
| ISSN: | 0065-2598 |
| Popis: | International audience; Fluorescein isothiocyanate derivatization of human lactotransferrin on Lys-264 as well as covalent addition of sulfosuccinimidyl 2-(p-azidosalicylamido)ethyl-1,3'- dithiopropionate (SASD)* on Lys-74 inhibits the binding of the glycoprotein to both human PHA-activated lymphocytes and non-activated platelets. This suggests that the cell binding site of lactotransferrin is located in the vicinity of the lysine residues 74 & 264 and does not occur either through electrostatic or lectin interactions. In contrast, the derivatization of lactotransferrin using sulfosuccinimidyl 6-(4'-azido-2'-nitrophenyl-amino) hexanoate (sulfo-SANPAH), on Lys-281 does not modify the binding parameters of lactotransferrin to the cells. Molecular modeling showed the position of SASD, sulfo-SANPAH and fluorescein molecules at the surface of the protein and suggested that SASD and fluorescein could mask the two loop-containing regions of human lactotransferrin (residues 28-34 and 38-45). Elsewhere, a 6 kDa peptide covering the peptide chain from residues 4 to 52 was isolated and its inhibitory effect on the binding of lactotransferrin to both human PHA-activated lymphocytes and non-activated platelets was demonstrated. Inhibition of ADP-induced platelet aggregation by lactotransferrin (50% inhibition = 10 nM) was also found with the N-t fragment of lactotransferrin (residues 3-281; 50% inhibition = 2 microM) and with two synthetic peptides: KRDS tetrapeptide (50% inhibition = 350 microM) and CFQWQRNMRKVRGPPVSC octodecapeptide (50% inhibition = 20 microM) corresponding to the lactotransferrin amino acid sequence 39-42 and 20-37, respectively. |
| Databáze: | OpenAIRE |
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