Zobrazeno 1 - 10
of 147
pro vyhledávání: '"Geneviève Spik"'
Publikováno v:
European Journal of Biochemistry. 114:169-178
Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration. The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc
Following the two meetings on Lactoferrin Structure and Function that were held in Honolulu, Hawaii, in 1993 and 1995, the Third International Conference on Lactoferrin Structure and Function was held in Le Touquet, France, and has successfully reinf
Publikováno v:
Arthritis & Rheumatism. 48:2197-2206
Objective To study cyclophilin B, a protein newly identified as a secretion product of cultured chondrocytes, in the context of chondrocyte pathobiology. Methods Cyclophilin B was purified by sequential chromatographic processing of the secretion med
Autor:
Marie-Christine Slomianny, Ikram El Yazidi-Belkoura, Patrick Van Berkel, Geneviève Spik, Jan H. Nuijens, Dominique Legrand
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1568:197-204
Although lactoferrins (Lfs) isolated from milk of various mammals exhibit a close structural relationship, they show species-specific binding to cells. To define the specificity of recognition of human (hLf), bovine (bLf) and murine (mLf) lactoferrin
Autor:
Norica Branza, Franc Pattus, Valérie Salmon, Geneviève Spik, Sophie Baveye-Descamps, Dominique Legrand, Frédéric R. Sallmann
Publikováno v:
Journal of Biological Chemistry. 274:16107-16114
The binding of lactoferrin, an iron-binding glycoprotein found in secretions and leukocytes, to the outer membrane of Gram-negative bacteria is a prerequisite to exert its bactericidal activity. It was proposed that porins, in addition to lipopolysac
Publikováno v:
Clinical Chemistry and Laboratory Medicine
Clinical Chemistry and Laboratory Medicine, 1999, 37 (3), pp.281-6
Clinical Chemistry and Laboratory Medicine, De Gruyter, 1999, 37 (3), pp.281-6
Clinical Chemistry and Laboratory Medicine, 1999, 37 (3), pp.281-6
Clinical Chemistry and Laboratory Medicine, De Gruyter, 1999, 37 (3), pp.281-6
Lactoferrin is an iron-binding glycoprotein found in exocrine secretions of mammals and released from neutrophilic granules during inflammation. This review describes the biological roles of lactoferrin in host defence. Secreted lactoferrin exerts an
Autor:
Geneviève Spik, Marie-Pierre Dehouck, Laurence Fenart, Carine Fillebeen, Monique Benaïssa, Laurence Descamps, Annick Pierce, Roméo Cecchelli
Publikováno v:
Journal of Biological Chemistry. 274:7011-7017
Lactoferrin (Lf) is an iron-binding protein involved in host defense against infection and severe inflammation; it accumulates in the brain during neurodegenerative disorders. Before determining Lf function in brain tissue, we investigated its origin
Publikováno v:
Biochemical Journal. 336:689-697
Cyclophilin B (CyPB) is a cyclosporin A (CsA)-binding protein, mainly associated with the secretory pathway, and is released in biological fluids. We recently reported that CyPB specifically binds to T-lymphocytes and promotes enhanced incorporation
Autor:
Philippe Bournat, Marie-Christine Slomianny, Veronique Gruber, Valérie Salmon, Dominique Legrand, Manfred Theisen, Ikram El Yazidi, Geneviève Spik, Dominique Mison, Béatrice Olagnier, Bertrand Merot
Publikováno v:
Protein Expression and Purification. 13:127-135
Production and characterization of human lactoferrin (hLf) in transgenic tobacco is reported. We have engineered two constructs containing either the native signal peptide from human lactoferrin or the signal peptide from sweet potato sporamin fused
Autor:
Yolande Boilly-Marer, Joël Mazurier, Maryse Masson, Eve Damiens, Isabelle Duthille, Ikram El Yazidi, Geneviève Spik
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1402:277-287
Lactoferrin is an iron-binding glycoprotein implicated in particular in the control of immune functions and cell proliferation. We have investigated its involvement, at inflammatory concentrations, in cancer progression. We report that lactoferrin ha