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9. Lactoferrin

Author

Zimecki, M., primary, Kapp, J., additional, Machnicki, M., additional, Zagulski, T., additional, Wlaszczyk, A., additional, Kübler, A., additional, Mazurier, J., additional, and Spik, G., additional

Published
1998
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13. Involvement of Gags in the Activity of Pro-Inflammatory Factors

Author

Agnès Denys, Fabrice Allain, Joël Mazurier, Rachel Pakula, Christophe Vanpouille, and Mathieu Carpentier

Subjects
Peptidylprolyl isomerase, Basement membrane, Endothelium, biology, Chemistry, Cell, Integrin, Inflammation, Cell biology, Membrane glycoproteins, medicine.anatomical_structure, medicine, biology.protein, Hepatocyte growth factor, medicine.symptom, medicine.drug
Abstract

During inflammation, the recruitment of leukocytes is regulated by a cascade of molecular events resulting in adhesion to the endothelium followed by migration into tissue. Initially, selectin-mediated interactions cause leukocytes to roll along the endothelium where they contact factors that trigger strong binding by activating cell integrins. The final step in the exit of leukocytes out of the bloodstream requires cell penetration through the underlying basement membrane (Ebnet and Vestweber, 1999).

Published
2003

14. Lactoferrin Stimulates the Mitogen-Activated Protein Kinase in the Human Lymphoblastic T Jurkat Cell Line

Author

Isabelle Duthille, Geneviève Spik, Maryse Masson, and Joël Mazurier

Subjects
biology, Lactoferrin, Chemistry, Monocyte, media_common.quotation_subject, food and beverages, Granulocyte, Jurkat cells, Cell biology, stomatognathic diseases, Transduction (genetics), fluids and secretions, medicine.anatomical_structure, medicine, biology.protein, Signal transduction, Internalization, Intracellular, media_common
Abstract

Lactoferrin11 (also called lactotransferrin) has been shown to be involved in numerous inflammatory and immune response functions such as regulation of granulocyte monocyte colony stimulating factor6,7,12,17 and of interleukin9 synthesis, activation of NK cell activity13, inhibition of metastasis2 and maturation of T- and B-cells15,16. Recently, it has also been demonstrated the activation of a nuclear reporter gene harbouring the spe-ci fic DNA sequence that lactoferrin recognizes8. Therefore, lactoferrin could be considered as a transcriptional factor1. It requires that lactoferrin is internalized and imported into the nucleus of target cells where it acts as a transcriptional factor1. However, there is no evidence that cell-surface lactoferrin receptors can transport lactoferrin either directly or via a new trafficking pathway to the nucleus. In order to investigate how lactoferrin affects the immune system, we have developed an experimental model using the human lymphoblastic T Jurkat cell line which upon lactoferrin treatment slowly undergoes a maturation process5. Jurkat cells express the lactoferrin receptor10 at the cell surface in coated-pit like domains, associated into clusters, and in different subsets of intracellular vesicles3 . Therefore, we have investigated the first intracellular events following the binding of lactoferrin to lymphocytes: internalization process of lactoferrin and activation of a transduction pathway.

Published
1998

15. Lactoferrin

Author

M. Zimecki, J. Kapp, M. Machnicki, T. Zagulski, A. Wlaszczyk, A. Kübler, J. Mazurier, and G. Spik

Published
1998

16. Molecular Biology of the Various Types of von Willebrand Disease

Author

C. Mazurier

Subjects
chemistry.chemical_classification, congenital, hereditary, and neonatal diseases and abnormalities, Pathology, medicine.medical_specialty, biology, business.industry, Platelet adhesion, medicine.disease, Most common inherited bleeding disorder, Dual role, Von Willebrand factor, Von willebrand, chemistry, hemic and lymphatic diseases, biology.protein, medicine, Von Willebrand disease, Platelet, Glycoprotein, business, circulatory and respiratory physiology
Abstract

Historically discovered in 1926 by Erik von Willebrand studying bleeding patients living on an island of the Aland archipelago, von Willebrand disease (vWD) is now recognised as the most common inherited bleeding disorder. It defines a heterogeneous group of patients with quantitative or qualitative defects of the von Willebrand factor (vWF) [1] which is a large glycoprotein present in plasma, subendothelium and the alpha granules of platelets. Synthesized exclusively by both endothelial cells and megakaryocytes, vWF plays a dual role in haemostasis. It mediates platelet adhesion to the subendothelium at the site of vessel injury and its circulating form carries and stabilizes factor VIII (FVIII), [2].

Published
1995

17. Study on the Binding of Lactotransferrin (Lactoferrin) to Human Pha-Activated Lymphocytes and Non-Activated Platelets

Author

Dominique Legrand, Joël Mazurier, B. Leveugle, Geneviève Spik, Elisabeth Rochard, and Jean Montreuil

Subjects
chemistry.chemical_classification, biology, Tetrapeptide, Chemistry, Lactoferrin, Lectin, Peptide, Lactotransferrin, chemistry.chemical_compound, Biochemistry, biology.protein, Platelet activation, Fluorescein isothiocyanate, Peptide sequence
Abstract

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.

Published
1994

18. Primary and Three-Dimensional Structure of Lactotransferrin (Lactoferrin) Glycans

Author

Yves Bourne, Christian Cambillaut, Joël Mazurier, Geneviève Spik, Bernadette Coddeville, and Jean Montreuil

Subjects
chemistry.chemical_classification, 0303 health sciences, Glycan, biology, Chemistry, Lactoferrin, 030302 biochemistry & molecular biology, Protein primary structure, Peptide, carbohydrates (lipids), Lactotransferrin, 03 medical and health sciences, Biochemistry, Serotransferrin, Transferrin, biology.protein, Carbohydrate conformation, 030304 developmental biology
Abstract

In order to establish relationships between glycan structure and biological activity, the authors undertook a comparative study of the glycan primary structure of different transferons from several species. By associating permethylation-mass spectrometry and 1H-NMR spectroscopy, the primary structure of the human, bovine, caprine, murine and porcine lactotransferrin glycans were determined. Using the same methods, the glycan structure of 9 serotransferrins was determined. The results obtained led to the conclusion that glycans are specific for each transferrin and, for a given transferrin, specific to the species. No relationship could be established between primary structure and function of transferrin glycans. Glycan molecular modelling, molecular dynamics simulations and X-ray diffraction studies of free glycans confirm the mobility in space of antennae. In contrast, the glycan associated with a protein is immobilized into only one conformation, as in the case of glycan-lectin associations or of “internal” glycan-protein interactions, like in rabbit serotransferrin, in which the glycan forms a bridge between the two lobes of the peptide chain, and maintains the protein in a biologically active conformation. In the case of human sero- and lactotransferrins, the glycans are in an external position on the molecules and could play a role of recognition signals.

Published
1994

19. Characterization of Two Kinds of Lactotransferrin (Lactoferrin) Receptors on Different Target Cells

Author

B. Leveugle, Takashi Mikogami, Annick Pierce, Elisabeth Rochard, Joël Mazurier, Dominique Legrand, Geneviève Spik, and Jean Montreuil

Subjects
chemistry.chemical_classification, 0303 health sciences, Growth factor, medicine.medical_treatment, Cell, Lactoferrin receptors, Immune receptor, Biology, 3. Good health, Cell biology, Lactotransferrin, 03 medical and health sciences, 0302 clinical medicine, medicine.anatomical_structure, chemistry, Biochemistry, medicine, Glycoprotein, High affinity receptor, Receptor, 030304 developmental biology, 030215 immunology
Abstract

Lactotransferrin (Lf), an iron-binding glycoprotein present as a major component in the specific granules of human neutrophilic granulocytes is released in the blood during the acute phase of infection and participates in the regulation of the host-defence mechanisms. Our previous observations (Mazurier et al., 1989) showing i) that the activation by PHA of T-lymphocytes induces the appearance at the cell surface of Lf-receptors which are absent from the membrane of resting lymphocytes and ii) that Lf becomes a growth factor for the activated lymphocytes, led us to undertake a series of researches on the presence of Lf receptors at the surface of different blood cells.

Published
1994

22. Summary

Author

Lönnerdal, Bo, Spik, Geneviève, editor, Legrand, Dominique, editor, Mazurier, Joël, editor, Pierce, Annick, editor, and Perraudin, Jean-Paul, editor

Published
1998
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27. Structural and Immunochemical Studies on Bovine Lactoferrin Fragments

Author

Shimazaki, Kei-ichi, Kamio, Makoto, Nam, Myong Soo, Harakawa, Shinji, Tanaka, Tetsuya, Omata, Yoshitaka, Saito, Atsushi, Kumura, Haruto, Mikawa, Katsuhiko, Igarashi, Ikuo, Suzuki, Naoyoshi, Spik, Geneviève, editor, Legrand, Dominique, editor, Mazurier, Joël, editor, Pierce, Annick, editor, and Perraudin, Jean-Paul, editor

Published
1998
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35. Inhibition of Azoxymethane Initiated Colon Tumor and Aberrant Crypt Foci Development by Bovine Lactoferrin Administration in F344 Rats

Author

Tsuda, Hiroyuki, Sekine, Kazunori, Nakamura, Joe, Ushida, Yoshihiko, Kuhara, Tetsuya, Takasuka, Nobuo, Kim, Dae Joong, Asamoto, Makoto, Baba-Toriyama, Hiroyasu, Moore, Malcolm A., Nishino, Hoyoku, Kakizoe, Tadao, Spik, Geneviève, editor, Legrand, Dominique, editor, Mazurier, Joël, editor, Pierce, Annick, editor, and Perraudin, Jean-Paul, editor

Published
1998
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41. The Mechanism of in Vivo Bacteriostasis of Bovine Lactoferrin

Author

Ogata, Tomohiro, Teraguchi, Susumu, Shin, Kouichirou, Kingaku, Michiko, Fukuwatari, Yasuo, Kawase, Kouzou, Hayasawa, Hirotoshi, Tomita, Mamoru, Spik, Geneviève, editor, Legrand, Dominique, editor, Mazurier, Joël, editor, Pierce, Annick, editor, and Perraudin, Jean-Paul, editor

Published
1998
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47. Lactoferrin : Antiviral Activity of Lactoferrin

Author

Swart, Pieter J., Kuipers, E. Mirjam, Smit, Catharina, Van Der Strate, Barry W. A., Harmsen, Martin C., Meijer, Dirk K. F., Spik, Geneviève, editor, Legrand, Dominique, editor, Mazurier, Joël, editor, Pierce, Annick, editor, and Perraudin, Jean-Paul, editor

Published
1998
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49. Antiviral Activity of Lactoferrin

Author

Valenti, Piera, Marchetti, Magda, Superti, Fabiana, Amendolia, Maria Grazia, Puddu, Patrizia, Gessani, Sandra, Borghi, Paola, Belardelli, Filippo, Antonini, Giovanni, Seganti, Lucilla, Spik, Geneviève, editor, Legrand, Dominique, editor, Mazurier, Joël, editor, Pierce, Annick, editor, and Perraudin, Jean-Paul, editor

Published
1998
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