Characterization of human and bovine phosphatidylethanolamine-binding protein (PEBP/RKIP) interactions with morphine and morphine-glucuronides determined by noncovalent mass spectrometry

Cédric Atmanene (1) , Alexis Laux (2) , Elise Glattard (2) , Arnaud H. Muller (2) , Françoise Schoentgen (3) , Marie-Hélène Metz-Boutigue (2) , Dominique Aunis (2) , Alain van Dorsselaer (1) , George B. Stefano (4) , Sarah Sanglier-Cianférani (1) , Yannick Goumon (2)

1 DSA-IPHC - Département Sciences Analytiques et Interactions Ioniques et Biomoléculaires
2 Physiopathologie des Maladies du Système Nerveux Central
3 IMPMC - Institut de minéralogie et de physique des milieux condensés
4 SUNY - State University of New York

The phosphatidylethanolamine-binding protein (PEBP/RKIP), initially found to bind phosphatidylethanolamine (PE), has been shown to be associated with morphine derivatives. Our recent study on bovine primary chromaffi n cells showed that inside secretory granules, PEBP is noncovalently associated to endogenous morphine-6-glucuronide (M6G), a highly analgesic morphine metabolite. During stress, M6G-PEBP complexes may be released into circulation to target peripheral opioid receptors. We now report the investigation of PEBP binding properties towards morphine and morphine analogs. http://www.medscimonit.com/fulltxt.php

Mots clés: morphine-6-glucuronide; morphine-3-glucuronide; morphine; phosphatidylethanolaminebinding protein; Raf-1 kinase inhibitor protein; noncovalent mass spectrometry; proteinlig and interactions

Domaines: Biochimie, Biologie Moléculaire

Cédric Atmanene, Alexis Laux, Elise Glattard, Arnaud H. Muller, Françoise Schoentgen, et al.. Characterization of human and bovine phosphatidylethanolamine-binding protein (PEBP/RKIP) interactions with morphine and morphine-glucuronides determined by noncovalent mass spectrometry. Medical Science Monitor, 2009, 15, pp.178-187. ⟨hal-00490814⟩