Bis (monoacylglycero) phosphate interfacial properties and lipolysis by pancreatic lipase-related protein 2, an enzyme present in THP-1 human monocytes

Autor: Francine Ferrato, Guowei Jiang, Frédéric Carrière, Michel Record, Sawsan Amara, Caroline Subra, Glenn D. Prestwich

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1811:419-430

The interfacial physical properties of bis(monoacylglycero)phosphate (BMP) and its derivatives with three oleoyl chains (hemi-BDP) and four oleoyl chains (bis(diacylglycero)phosphate, BDP) were investigated using Langmuir monomolecular films. The mea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56e2629d59c90a411e9074c67f8f5c7d
https://doi.org/10.1016/j.bbalip.2011.04.008

Syntheses of an α-d-Gal-(1→6)-β-d-Gal diglyceride, as lipase substrate

Autor: Dominique Lafont, Paul Boullanger, Francine Ferrato, Frédéric Carrière

Publikováno v: Carbohydrate Research
Carbohydrate Research, Elsevier, 2006, 341 (6), pp.695-704. ⟨10.1016/j.carres.2006.01.021⟩
Carbohydrate Research, 2006, 341 (6), pp.695-704. ⟨10.1016/j.carres.2006.01.021⟩

Two different routes were explored to afford 3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol. In the first one, the key step was the glycosylation of the 3-O-(2,3,4-tri-O-benzyl-beta-D-galactopyranosyl)-1,2-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ea2593a078e003bf3665bfc62b9d0c0
https://doi.org/10.1016/j.carres.2006.01.021

Human Pancreatic Lipase: Colipase Dependence and Interfacial Binding of Lid Domain Mutants

Autor: Margarita G. Ivanova, Véronique Lopez, Sofiane Bezzine, Frédéric Carrière, Francine Ferrato, Robert Verger

Publikováno v: Biochemistry. 38:5499-5510

Five key amino acid residues from human pancreatic lipase (HPL) are mutated in some pancreatic lipase-related proteins 2 (PLRP2) that are not reactivated by colipase in the presence of bile salts. One of these residues (Y403) is involved in a direct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ffbf8df33cd2c3fdbde44e26478ffe8
https://doi.org/10.1021/bi982601x

Purification and molecular characterization of lamb pregastric lipase

Autor: Alain De Caro, Francine Ferrato, Robert Verger, Josiarte De Caro

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1252:321-329

Lamb pregastric lipase (LPGL) was purified from pharyngeal tissues. The purification procedure was based on an aqueous extract containing 0.7% Tween 80 which was chromatographed on DEAE-cellulose anion-exchanger and adsorbed on HA-Ultrogel followed b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daac2081c2d46f09cf35b9a3b8f5f2df
https://doi.org/10.1016/0167-4838(95)00134-g

A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase

Autor: Helle Fabricius Woldike, C. Cudrey, Frédéric Carrière, Lars Thim, Guy Dodson, Esper Boel, Christian Cambillau, Francine Ferrato, A. Hjorth, David M. R. Lawson

Publikováno v: Biochemistry. 32:4702-4707

Typically pancreatic lipases are characterized by the following properties: (1) they are activated by lipid/water interfaces (interfacial activation), (2) they are inhibited by bile salts but reactivated by colipase (a small activator protein), and (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ab1a5e6c1a9b0f8f9e95eb63ade264b
https://doi.org/10.1021/bi00069a003