@article{brasse-lagnel_intestinal_2011,

title = {Intestinal DMT1 cotransporter is down-regulated by hepcidin via proteasome internalization and degradation},

author = {Brasse-Lagnel, Carole and Karim, Zoubida and Letteron, Philippe and Bekri, Soumeya and Bado, André and Beaumont, Carole},

doi = {10.1053/j.gastro.2010.12.037},

issn = {1528-0012},

year  = {2011},

date = {2011-04-01},

journal = {Gastroenterology},

volume = {140},

number = {4},

pages = {1261--1271.e1},

abstract = {BACKGROUNDS & AIMS: The mechanism by which hepcidin regulates iron export from macrophages has been well established and is believed to involve degradation of ferroportin. However, in the small intestine, hepcidin's mechanisms of action are not known. We studied human polarized intestinal (Caco-2/TC7) cells and mouse duodenal segments, ex vivo, to investigate the molecular mechanisms by which hepcidin down-regulates intestinal transepithelial iron transport. 

METHODS: Iron transport was analyzed using ⁵⁵FeNTA. Expression of Divalent Metal Transporter 1 (DMT1) and ferroportin was evaluated by reverse-transcription quantitative polymerase chain reaction and immunoblotting. Videomicroscopy analysis was performed on live cells that expressed either DMT1 or ferroportin fused to green fluorescent protein. 

RESULTS: In Caco-2/TC7 cells, physiologic doses of hepcidin (50-1000 nmol/L) inhibited transport of ⁵⁵Fe in a dose-dependent manner; a half-maximum effect was observed at 75-100 nmol/L. However, 200 nmol/L hepcidin induced a significant decrease in DMT1 protein expression but no change in ferroportin protein levels, unlike macrophages. This result was confirmed ex vivo in isolated duodenal segments: 200 nmol/L hepcidin induced a significant reduction in iron transport and DMT1 protein levels but no change in ferroportin levels. In Caco-2/TC7 cells, the effect of hepcidin on the DMT1 protein level was completely abolished in the presence of a proteasome inhibitor (MG-132); DMT1 ubiquitination was induced by the addition of hepcidin. 

CONCLUSIONS: An acute increase in hepcidin concentration reduces intestinal iron absorption through ubiquitin-dependent proteasome degradation of DMT1.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Leclerc2011,

title = {The ubiquitous dermokine delta activates Rab5 function in the early endocytic pathway.},

author = {Leclerc, Emilie A and Gazeilles, Leila and Serre, Guy and Guerrin, Marina and Jonca, Nathalie},

doi = {10.1371/journal.pone.0017816},

issn = {1932-6203 (Electronic)},

year  = {2011},

date = {2011-03-01},

journal = {PloS one},

volume = {6},

number = {3},

pages = {e17816},

abstract = {The expression of the recently identified dermokine (Dmkn) gene leads to four families of proteins with as yet unknown functions. The secreted $alpha$, $beta$ and $gamma$ isoforms share an epidermis-restricted expression pattern, whereas the $delta$ isoform is intracellular and ubiquitous. To get an insight into Dmkn$delta$ function, we performed yeast two-hybrid screening and identified the small GTPases Rab5 as partners for Dmkn$delta$. The Rab5 proteins are known to regulate membrane docking and fusion in the early endocytic pathway. GST pull-down assays confirmed the direct interaction between Rab5 and Dmkn$delta$. Transient expression of Dmkn$delta$ in HeLa cells led to the formation of punctate structures colocalized with endogenous Rab5 and clathrin, indicating Dmkn$delta$ involvement in the early steps of endocytosis. Dmkn$delta$ indeed colocalized with transferrin at early stages of endocytosis, but did not modulate its endocytosis or recycling kinetics. We also showed that Dmkn$delta$ was able to bind both inactive (GDP-bound) and active (GTP-bound) forms of Rab5 in vitro but preferentially targeted GDP-bound form in HeLa cells. Interestingly, Dmkn$delta$ expression rescued the Rab5S34N-mediated inhibition of endosome fusion. Moreover, Dmkn$delta$ caused the enlargement of vesicles positive for Rab5 by promoting GTP loading onto the small GTPase. Together our data reveal that Dmkn$delta$ activates Rab5 function and thus is involved in the early endosomal trafficking.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Mattiuzzo2011,

title = {A large-scale multi-technique approach identifies forty-nine new players of keratinocyte terminal differentiation in human epidermis.},

author = {Mattiuzzo, Nicolas R and Toulza, Eve and Jonca, Nathalie and Serre, Guy and Guerrin, Marina},

doi = {10.1111/j.1600-0625.2010.01188.x},

issn = {1600-0625 (Electronic)},

year  = {2011},

date = {2011-02-01},

journal = {Experimental dermatology},

volume = {20},

number = {2},

pages = {113--118},

abstract = {At the latest stage of terminal differentiation in the epidermis, granular keratinocytes (GKs) undergo cornification, a programmed cell death required for the establishment of a functional skin barrier. A complex genetic regulatory network orchestrates the underlying biochemical modifications, but very few transcription factors specific to this programme have been identified to date. Here, we describe a large-scale, multi-technique approach performed on cells purified from normal human epidermis, primarily focusing on the identification of regulators. We combined data from microarray analysis of cell fractions enriched in GKs or basal keratinocytes, from an expressed sequence tag (EST) library built from GKs and from an in silico promoter analysis of 52 differentiation-associated genes. Among 3576 genes potentially expressed in GK, 298 candidates were selected, and half were directly profiled for the first time in the different layers of the epidermis by quantitative real-time PCR. Forty-nine genes upregulated during terminal differentiation, associated with numerous function of GK including lipid synthesis and secretion, were identified. Of 94 transcription factors detected, 37 were found to be either positively or negatively regulated, suggesting their involvement as regulators of gene expression in the GKs. These results largely extend the number of genes known as involved in the latest step of the terminal differentiation of human epidermis as well as the number of transcription factors known to control the expression of these genes.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Vasilopoulos2011,

title = {The 3'-UTR AACCins5874 in the stratum corneum chymotryptic enzyme gene (SCCE/KLK7), associated with atopic dermatitis; causes an increased mRNA expression without altering its stability.},

author = {Vasilopoulos, Yiannis and Sharaf, Nazar and di Giovine, Franco and Simon, Michel and Cork, Michael J and Duff, Gordon W and Tazi-Ahnini, Rachid},

doi = {10.1016/j.jdermsci.2010.11.013},

issn = {1873-569X (Electronic)},

year  = {2011},

date = {2011-02-01},

booktitle = {Journal of dermatological science},

journal = {Journal of dermatological science},

volume = {61},

number = {2},

pages = {131--133},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Viret2011b,

title = {Thymus-specific serine protease contributes to the diversification of the functional endogenous CD4 T cell receptor repertoire. },

author = {Viret, C. and Lamare, C. and Guiraud, M. and Fazilleau, N. and Bour, A. and Malissen, B. and Carrier, A. and Guerder, S. },

url = {https://www.ncbi.nlm.nih.gov/pubmed/21173102},

doi = {10.1084/jem.20100027},

year  = {2011},

date = {2011-01-17},

journal = {J Exp Med.},

volume = {208},

pages = {3-11},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN21b,

title = {Absence of the lysophosphatidic acid receptor LPA1 results in abnormal bone development and decreased bone mass},

author = {Gennero, I. and Laurencin-Dalicieux, S. and Conte-Auriol, F. and Briand-Mesange, F. and Laurencin, D. and Rue, J. and Beton, N. and Malet, N. and Mus, M. and Tokumura, A. and Bourin, P. and Vico, L. and Brunel, G. and Oreffo, R. O. and Chun, J. and Salles, J. P.},

url = {https://www.ncbi.nlm.nih.gov/pubmed/21569876},

doi = {10.1016/j.bone.2011.04.018},

issn = {1873-2763 (Electronic) 

1873-2763 (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {Bone},

volume = {49},

number = {3},

pages = {395-403},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN27,

title = {Traditional cardiovascular risk factors in rheumatoid arthritis: a meta-analysis},

author = {Boyer, J. F. and Gourraud, P. A. and Cantagrel, A. and Davignon, J. L. and Constantin, A.},

url = {https://www.ncbi.nlm.nih.gov/pubmed/20851020},

doi = {10.1016/j.jbspin.2010.07.016},

issn = {1778-7254 (Electronic) 

1297-319X (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {Joint Bone Spine},

volume = {78},

number = {2},

pages = {179-83},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN13b,

title = {Cytosolic phospholipase A2alpha gene silencing in the myeloid lineage alters development of Th1 responses and reduces disease severity in collagen-induced arthritis},

author = {Courties, G. and Baron, M. and Presumey, J. and Escriou, V. and van Lent, P. and Scherman, D. and Cantagrel, A. and van den Berg, W. B. and Jorgensen, C. and Apparailly, F. and Davignon, J. L.},

url = {https://www.ncbi.nlm.nih.gov/pubmed/21360497},

doi = {10.1002/art.30174},

issn = {1529-0131 (Electronic) 

0004-3591 (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {Arthritis Rheum},

volume = {63},

number = {3},

pages = {681-90},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN34,

title = {A Phosphorus-Based Dendrimer Targets Inflammation 

and Osteoclastogenesis in Experimental Arthritis},

author = {Myriam Hayder and Mary Poupot and Michel Baron and Delphine Nigon and Cédric-Olivier Turrin and Anne-Marie Caminade and Jean-Pierre Majoral and Robert A. Eisenberg and Jean-Jacques Fournié and Alain Cantagrel and Rémy Poupot and Davignon, Jean-Luc},

year  = {2011},

date = {2011-01-01},

journal = {‎Sci. Transl. Med},

volume = {3},

number = {81 81ra35},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN34b,

title = {A Phosphorus-Based Dendrimer Targets Inflammation 

and Osteoclastogenesis in Experimental Arthritis},

author = {Myriam Hayder and Mary Poupot and Michel Baron and Delphine Nigon and Cédric-Olivier Turrin and Anne-Marie Caminade and Jean-Pierre Majoral and Robert A. Eisenberg and Jean-Jacques Fournié and Alain Cantagrel and Rémy Poupot and Davignon, Jean-Luc},

year  = {2011},

date = {2011-01-01},

journal = {‎Sci. Transl. Med},

volume = {3},

number = {81 81ra35},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN163,

title = {Hematopoietic chimerism and transplantation tolerance: a role for regulatory T cells},

author = {Pasquet, Lise and Joffre, Olivier and Santolaria, Thibault and van Meerwijk, Joost},

url = {http://www.frontiersin.org/Journal/Abstract.aspx?s=1180&name=immunological_tolerance&ART_DOI=10.3389/fimmu.2011.00080},

doi = {10.3389/fimmu.2011.00080},

issn = {1664-3224},

year  = {2011},

date = {2011-01-01},

journal = {Frontiers in Immunology},

volume = {2},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN162,

title = {AIRE-deficient CD8+CD28low regulatory T lymphocytes fail to control experimental colitis},

author = {Pomie, C. and Vicente, R. and Vuddamalay, Y. and Ardesjö Lundgren, B. and van der Hoek, M. and Enault, G. and Kagan, J. and Fazilleau, N and Scott, H. S. and Romagnoli, P. and van Meerwijk, J.P.M.},

year  = {2011},

date = {2011-01-01},

journal = {Proceedings of the National Academy of Sciences of the U.S.A.},

volume = {108},

number = {30},

pages = {12437-12442},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN14b,

title = {The p.Arg63Trp polymorphism controls Vav1 functions and Foxp3 regulatory T cell development},

author = {Colacios, C. and Casemayou, A. and Dejean, A. S. and Gaits-Iacovoni, F. and Pedros, C. and Bernard, I. and Lagrange, D. and Deckert, M. and Lamouroux, L. and Jagodic, M. and Olsson, T. and Liblau, R. S. and Fournie, G. J. and Saoudi, A.},

url = {http://www.ncbi.nlm.nih.gov/pubmed/21948080},

doi = {10.1084/jem.20102191},

issn = {1540-9538 (Electronic) 

0022-1007 (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {J Exp Med},

volume = {208},

number = {11},

pages = {2183-91},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN8b,

title = {Tyrosine kinase 2 variant influences T lymphocyte polarization and multiple sclerosis susceptibility},

author = {Couturier, N. and Bucciarelli, F. and Nurtdinov, R. N. and Debouverie, M. and Lebrun-Frenay, C. and Defer, G. and Moreau, T. and Confavreux, C. and Vukusic, S. and Cournu-Rebeix, I. and Goertsches, R. H. and Zettl, U. K. and Comabella, M. and Montalban, X. and Rieckmann, P. and Weber, F. and Muller-Myhsok, B. and Edan, G. and Fontaine, B. and Mars, L. T. and Saoudi, A. and Oksenberg, J. R. and Clanet, M. and Liblau, R. S. and Brassat, D.},

url = {http://www.ncbi.nlm.nih.gov/pubmed/21354972},

doi = {10.1093/brain/awr010},

issn = {1460-2156 (Electronic) 

0006-8950 (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {Brain},

volume = {134},

number = {Pt 3},

pages = {693-703},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN18b,

title = {Highly specialized role of Forkhead box O transcription factors in the immune system},

author = {Dejean, A. S. and Hedrick, S. M. and Kerdiles, Y. M.},

url = {http://www.ncbi.nlm.nih.gov/pubmed/20673126},

doi = {10.1089/ars.2010.3414},

issn = {1557-7716 (Electronic) 

1523-0864 (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {Antioxid Redox Signal},

volume = {14},

number = {4},

pages = {663-74},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{RN7b,

title = {Genetic risk and a primary role for cell-mediated immune mechanisms in multiple sclerosis},

author = {International Multiple Sclerosis Genetics, Consortium and Wellcome Trust Case Control, Consortium and Sawcer, S. and Hellenthal, G. and Pirinen, M. and Spencer, C. C. and Patsopoulos, N. A. and Moutsianas, L. and Dilthey, A. and Su, Z. and Freeman, C. and Hunt, S. E. and Edkins, S. and Gray, E. and Booth, D. R. and Potter, S. C. and Goris, A. and Band, G. and Oturai, A. B. and Strange, A. and Saarela, J. and Bellenguez, C. and Fontaine, B. and Gillman, M. and Hemmer, B. and Gwilliam, R. and Zipp, F. and Jayakumar, A. and Martin, R. and Leslie, S. and Hawkins, S. and Giannoulatou, E. and D'Alfonso, S. and Blackburn, H. and Martinelli Boneschi, F. and Liddle, J. and Harbo, H. F. and Perez, M. L. and Spurkland, A. and Waller, M. J. and Mycko, M. P. and Ricketts, M. and Comabella, M. and Hammond, N. and Kockum, I. and McCann, O. T. and Ban, M. and Whittaker, P. and Kemppinen, A. and Weston, P. and Hawkins, C. and Widaa, S. and Zajicek, J. and Dronov, S. and Robertson, N. and Bumpstead, S. J. and Barcellos, L. F. and Ravindrarajah, R. and Abraham, R. and Alfredsson, L. and Ardlie, K. and Aubin, C. and Baker, A. and Baker, K. and Baranzini, S. E. and Bergamaschi, L. and Bergamaschi, R. and Bernstein, A. and Berthele, A. and Boggild, M. and Bradfield, J. P. and Brassat, D. and Broadley, S. A. and Buck, D. and Butzkueven, H. and Capra, R. and Carroll, W. M. and Cavalla, P. and Celius, E. G. and Cepok, S. and Chiavacci, R. and Clerget-Darpoux, F. and Clysters, K. and Comi, G. and Cossburn, M. and Cournu-Rebeix, I. and Cox, M. B. and Cozen, W. and Cree, B. A. and Cross, A. H. and Cusi, D. and Daly, M. J. and Davis, E. and de Bakker, P. I. and Debouverie, M. and D'Hooghe M, B. and Dixon, K. and Dobosi, R. and Dubois, B. and Ellinghaus, D. and others},

url = {http://www.ncbi.nlm.nih.gov/pubmed/21833088},

doi = {10.1038/nature10251},

issn = {1476-4687 (Electronic) 

0028-0836 (Linking)},

year  = {2011},

date = {2011-01-01},

journal = {Nature},

volume = {476},

number = {7359},

pages = {214-9},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{b,

title = {Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells},

author = {Cebrian, I. and Visentin, G. and Blanchard, N. and Jouve, M. and Bobard, A. and Moita, C. and Enninga, J. and Moita, L. F. and Amigorena, S. and Savina, A.},

year  = {2011},

date = {2011-01-01},

journal = {Cell},

volume = {147},

number = {6},

pages = {1355-68},

abstract = {Antigen (Ag) crosspresentation by dendritic cells (DCs) involves the presentation of internalized Ags on MHC class I molecules to initiate CD8+ T cell-mediated immunity in response to certain pathogens and tumor cells. Here, we identify the SNARE Sec22b as a specific regulator of Ag crosspresentation. Sec22b localizes to the ER-Golgi intermediate compartment (ERGIC) and pairs to the plasma membrane SNARE syntaxin 4, which is present in phagosomes (Phgs). Depletion of Sec22b inhibits the recruitment of ER-resident proteins to Phgs and to the vacuole containing the Toxoplasma gondii parasite. In Sec22b-deficient DCs, crosspresentation is compromised after Ag phagocytosis or endocytosis and after invasion by T. gondii. Sec22b silencing inhibited Ag export to the cytosol and increased phagosomal degradation by accelerating lysosomal recruitment. Our findings provide insight into an intracellular traffic pathway required for crosspresentation and show that Sec22b-dependent recruitment of ER proteins to Phgs critically influences phagosomal functions in DCs.},

note = {Cebrian, Ignacio 

Visentin, Geraldine 

Blanchard, Nicolas 

Jouve, Mabel 

Bobard, Alexandre 

Moita, Catarina 

Enninga, Jost 

Moita, Luis F 

Amigorena, Sebastian 

Savina, Ariel 

Cell. 2011 Dec 9;147(6):1355-68.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{b,

title = {Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells},

author = {Cebrian, I. and Visentin, G. and Blanchard, N. and Jouve, M. and Bobard, A. and Moita, C. and Enninga, J. and Moita, L. F. and Amigorena, S. and Savina, A.},

year  = {2011},

date = {2011-01-01},

journal = {Cell},

volume = {147},

number = {6},

pages = {1355-68},

abstract = {Antigen (Ag) crosspresentation by dendritic cells (DCs) involves the presentation of internalized Ags on MHC class I molecules to initiate CD8+ T cell-mediated immunity in response to certain pathogens and tumor cells. Here, we identify the SNARE Sec22b as a specific regulator of Ag crosspresentation. Sec22b localizes to the ER-Golgi intermediate compartment (ERGIC) and pairs to the plasma membrane SNARE syntaxin 4, which is present in phagosomes (Phgs). Depletion of Sec22b inhibits the recruitment of ER-resident proteins to Phgs and to the vacuole containing the Toxoplasma gondii parasite. In Sec22b-deficient DCs, crosspresentation is compromised after Ag phagocytosis or endocytosis and after invasion by T. gondii. Sec22b silencing inhibited Ag export to the cytosol and increased phagosomal degradation by accelerating lysosomal recruitment. Our findings provide insight into an intracellular traffic pathway required for crosspresentation and show that Sec22b-dependent recruitment of ER proteins to Phgs critically influences phagosomal functions in DCs.},

note = {Dec 9;147(6):1355-68.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Coudane2011,

title = {Deimination and expression of peptidylarginine deiminases during cutaneous wound healing in mice.},

author = {Coudane, Fanny and Méchin, Marie-Claire and Huchenq, Anne and Henry, Julie and Nachat, Rachida and Ishigami, Akihito and Adoue, Véronique and Sebbag, Mireille and Serre, Guy and Simon, Michel},

doi = {10.1684/ejd.2011.1394},

issn = {1167-1122 (Print)},

year  = {2011},

date = {2011-01-01},

journal = {European journal of dermatology : EJD},

volume = {21},

number = {3},

pages = {376--384},

abstract = {Deimination, the conversion of protein-bound arginines into citrullines, is a post-translational modification catalyzed by a peptidylarginine deiminase (Pad). In the epidermis, three Pads are expressed, namely Pad1, 2 and 3, and the major deiminated protein is filaggrin. Deimination of fibrin has been observed in various pathological inflammatory conditions. Here, we analyzed the expression of Pads and citrullination of proteins during cutaneous wound healing, i.e. in a physiological inflammatory condition. Full-thickness punches were performed on adult mouse back skin, and wound recovery was analyzed over 10 days by immunohistology and western blotting. Pad1 was immunodetected in all the neo-epidermis. Pad3, normally expressed in the stratum granulosum, was not detected in the hyperproliferative tongue of the neo-epidermis, but was shown to be co-localized with (pro)filaggrin in a large number of keratinocyte layers in its differentiating part. Deiminated proteins were detected in the stratum corneum of the neo-epidermis in the late phase of re-epithelialization, and in the clot and the clot-derived scab. In the clot where we only detected Pad4, one of the deiminated proteins was shown to be fibrin. Deimination of the clot proteins, and more generally wound healing and keratinocyte differentiation, seemed to be Pad2-independent, as shown using Padi2(-/-) mice.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}