Yves Combarnous

Dr. Yves Combarnous

CNRS (emeritus)
orcid

Research Focus & Metrics

Academic Career Length

56Years (1971-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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27 March 2000 in Journal of Experimental Medicine
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Journal Article
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CLChristine Leteux
Christine Leteux
WCWengang Chai
Wengang Chai
RLR. Wendy Loveless
R. Wendy Loveless
CYChun-Ting Yuen
Chun-Ting Yuen
LULars Uhlin-Hansen
Lars Uhlin-Hansen
TFTen Feizi
Ten Feizi
The mannose receptor (MR) is an endocytic protein on macrophages and dendritic cells, as well as on hepatic endothelial, kidney mesangial, tracheal smooth muscle, and retinal pigment epithelial cells. The extracellular portion contains two types of carbohydrate-recognition domain (CRD): eight membrane-proximal C-type CRDs and a membrane-distal cysteine-rich domain (Cys-MR). The former bind mannose-, N-acetylglucosamine-, and fucose-terminating oligosaccharides, and may be important in innate immunity towards microbial pathogens, and in antigen trapping for processing and presentation in adaptive immunity. Cys-MR binds to the sulfated carbohydrate chains of pituitary hormones and may have a role in hormonal clearance. A second feature of Cys-MR is binding to macrophages in marginal zones of the spleen, and to B cell areas in germinal centers which may help direct MR-bearing cells toward germinal centers during the immune response. Here we describe two novel classes of carbohydrate ligand for Cys-MR: chondroitin-4 sulfate chains of the type found on proteoglycans produced by cells of the immune system, and sulfated blood group chains. We further demonstrate that Cys-MR interacts with cells in the spleen via the binding site for sulfated carbohydrates. Our data suggest that the three classes of sulfated carbohydrate ligands may variously regulate the trafficking and function of MR-bearing cells.

24 January 2019 in Toxics
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Yves CombarnousYves Combarnous
Yves Combarnous
TNThi Mong Diep Nguyen
Thi Mong Diep Nguyen
Endocrine Disruptor Compounds (EDCs) are synthetic or natural molecules in the environment that promote adverse modifications of endogenous hormone regulation in humans and/or in wildlife animals. In the present paper, we review the potential mechanisms of EDCs and point out the similarities and differences between EDCs and hormones. There was only one mechanism, out of nine identified, in which EDCs acted like hormones (i.e., binding and stimulated hormone receptor activity). In the other eight identified mechanisms of action, EDCs exerted their effects either by affecting endogenous hormone concentration, or its availability, or by modifying hormone receptor turn over. This overview is intended to classify the various EDC mechanisms of action in order to better appreciate when in vitro tests would be valid to assess their risks towards humans and wildlife.

18 August 2017 in Comptes Rendus. Biologies
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Journal Article
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Yves CombarnousYves Combarnous
Yves Combarnous
A number of pesticides are suspected or proved to act as endocrine disruptor compounds (EDCs). In the present survey of the literature, we try to define the main issues to be considered to classify individual pesticides as EDC or not.

26 February 2015 in Frontiers in Endocrinology
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CCClaire Cahoreau
Claire Cahoreau
DKDaniã¨lE Klett
Daniã¨lE Klett
Yves CombarnousYves Combarnous
Yves Combarnous
Glycoprotein hormones (GPHs) are the most complex molecules with hormonal activity. They exist only in vertebrates but the genes encoding their subunits ancestors are found in most vertebrate invertebrate species although their roles are still unknown. In the present report we review the available structural and functional data concerning GPHs and their subunits’ ancestors.

1 September 2010 in Aquatic Toxicology
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Journal Article
Closed access
MVMélanie Vosges
Mélanie Vosges
YPYann Le Page
Yann Le Page
BCBon-Chu Chung
Bon-Chu Chung
Yves CombarnousYves Combarnous
Yves Combarnous
JPJean-Marc Porcher
Jean-Marc Porcher
FBFrançois Brion
François Brion

2 November 1984 in Science
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Journal Article
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MBMartine Bégeot
Martine Bégeot
FHFiona J. Hemming
Fiona J. Hemming
PDPaul M. Dubois
Paul M. Dubois
Yves CombarnousYves Combarnous
Yves Combarnous
MDMaurice P. Dubois
Maurice P. Dubois
MAMichel L. Aubert
Michel L. Aubert
Addition of gonadotropin releasing hormone to cultures of fetal rat pituitary induced differentiation of lactotropes as revealed by immunocytochemistry. Antiserum to luteinizing hormone (LH) (recognizing native LH), but not antiserum to LH-β (recognizing both native LH and its β subunit), inhibited this induction. Further addition of highly purified LH-α subunit in culture medium also induced lactotrope differentiation. Thus, the α subunit may have a specific biological activity of its own with probable practical use in clinical investigations.