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J Biol Chem, Vol. 273, Issue 33, 20886-20893, August 14, 1998

The Mannose 6-Phosphate/Insulin-like Growth Factor II Receptor Is a Nanomolar Affinity Receptor for Glycosylated Human Leukemia Inhibitory Factor

Frédéric BlanchardDagger , Sylvie RaherDagger , Laurence DuplombDagger , Patricia Vusio, Vincent Pitardparallel , Jean-Luc Taupinparallel , Jean-François Moreauparallel , Bernard Hoflack**, Stéphane MinvielleDagger , Yannick JacquesDagger , and Anne GodardDagger

From the Dagger  Groupe de Recherche Cytokines/Récepteurs/Transduction, Unité INSERM 463 and  IFR26, Institut de Biologie, 9 Quai Moncousu, 44035 Nantes Cedex 01, parallel  CNRS-UMR 5540, Fédération de Recherche 60, Université Bordeaux 2, 146, rue Léo Saignat, 33076 Bordeaux Cedex, and ** Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, BP 447, 1 rue Professeur Calmette, 59021 Lille Cedex, France

Comparison of the binding properties of non-glycosylated, glycosylated human leukemia inhibitory factor (LIF) and monoclonal antibodies (mAbs) directed at gp190/LIF-receptor beta  subunit showed that most of the low affinity (nanomolar) receptors expressed by a variety of cell lines are not due to gp190. These receptors bind glycosylated LIF produced in Chinese hamster ovary cells (CHO LIF) (Kd = 6.9 nM) but not Escherichia coli-derived LIF or CHO LIF treated with endoglycosidase F. CHO LIF binding to these receptors is neither affected by anti-gp190 mAbs nor by anti-gp130 mAbs and is specifically inhibited by low concentrations of mannose 6-phosphate (Man-6-P) (IC50 = 40 µM), suggesting that they could be related to Man-6-P receptors. The identity of this LIF binding component with the Man-6-P/insulin-like growth factor-II receptor (Man-6-P/IGFII-R) was supported by several findings. (i) It has a molecular mass very similar to that of the Man-6-P/IGFII-R (270 kDa); (ii) the complex of LIF cross-linked to this receptor is immunoprecipitated by a polyclonal anti-Man-6-P/IGFII-R antibody; (iii) this antibody inhibits LIF and IGFII binding to the receptor with comparable efficiencies; (iv) soluble Man-6-P/IGFII-R purified from serum binds glycosylated LIF (Kd = 4.3 nM) but not E. coli LIF. The potential role of Man-6-P/IGFII-R in LIF processing and biological activity is discussed.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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