Cancer du sein et micro-environnement tumoral: rôle de la protéase ...

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42. Zurhove, K., Nakajima, C., Herz, J., Bock, H. H., and May, P. Gammasecretaselimits the inflammatory response through the processing of LRP1.Sci Signal, 1: ra15, 2008.43. von Arnim, C. A., Kinoshita, A., Peltan, I. D., Tangredi, M. M., Herl, L., Lee, B.M., Spoelgen, R., Hshieh, T. T., Ranganathan, S., Battey, F. D., Liu, C. X.,Bacskai, B. J., Sever, S., Irizarry, M. C., Strickland, D. K., and Hyman, B. T.The low density lipoprotein receptor-related protein (LRP) is a novel betasecretase(BACE1) substrate. J Biol Chem, 280: 17777-17785, 2005.44. Kinoshita, A., Shah, T., Tangredi, M. M., Strickland, D. K., and Hyman, B. T.The intracellular domain of the low density lipoprotein receptor-related proteinmodulates transactivation mediated by amyloid precursor protein and Fe65. JBiol Chem, 278: 41182-41188, 2003.23
A abNH2Beaujouin, Figure 14K 14K 34KAsp33Asp231-44 13481 QIDRGVTHLN ISGLKMPRGI AIDWVAGNVY WTDSGRDVIE VAQMKGENRK51 TLISGMIDEP HAIVVDPLRG TMYWSDWGNH PKIETAAMDG TLRETLVQDN101 IQWPTGLAVD YHNERLYWAD AKLSVIGSIR LNGTDPIVAA DSKRGLSHPF151 SIDVFEDYIY GVTYINNRVF KIHKFGHSPL VNLTGGLSHA SDVVLYHQHK201 QPEVTNPCDR KKCEWLCLLS PSGPVCTCPN GKRLDNGTCV PVPSPTPPPD251 APRPGTCNLQ CFNGGSCFLN ARRQPKCRCQ PRYTGDKCEL DQCWEHCRNG301 GTCAASPSGM PTCRCPTGFT GPKCTQQVCA GYCANNSTCT VNQGNQPQCR351 CLPGFLG DRC QYRQCSGYCE NFGTCQMAAD GSRQCRCTAY FEGSRCEVNK401 CSRCLEGACV VNKQSGDVTC NCTDGRVAPS CLTCVGHCSN GGSCTMNSKM451 MPECQCPPHM TGPRCEEHVF SQQQPGHIAS ILIPLLLLLL LVLVAGVVFW501 YKRRVQGAKG FQHQRMTNGA MNVEIGNPTY KMYEGGE PDD VGGLLDADFA551 LDPDKPTNFT NPVYATLYMG GHGSRHSLAS TDEKRELLGR GPEDEIGDPL601 ACOOHCoomassieAutoradiographyBab79K -27K -LRP1b [1-476]cd61K -27K -LRP1b [1-476]e66K -fLRP1b [1-476]27K -Cab43K -27K -52K pro-cath-Dcd43K -27K -APP
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Université Montpellier I UFR Méd
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Un grand merci à tous mes collabor
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TitleBreast cancer and tumoral micr
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Cancer du sein et micro-environneme
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C. PRESENTATION DU TRAVAIL DE THESE
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But de la thèseLa cathepsine-D (ca
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I. Le tissu adipeux1) Généralité
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(Adenosine triphosphate). Cette pro
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Cette synthèse de novo a lieu dans
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ABFigure 6 : Schéma de la oxydati
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d. Ladipocyte : une cellule sécré
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3) Ladipogenèsea. Les différentes
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. Les facteurs de transcriptionLa d
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Lexpression de C/EBP est quant à e
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adipeux. Les analyses histologiques
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adipocyteFigure 10 : Schéma repré
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II. La cathepsine-D1) Synthèse, ma
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les cath-B et L, en une forme matur
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Il existe deux RM6P : le RM6P/IGFII
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2) Fonctions de la cath-Da. Dans la
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. Dans les pathologiesEn plus de se
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c. Rôles et mécanismes daction da
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carcinome de prostate serait respon
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La cath-D joue donc un rôle import
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Une fois le marquage des peptides e
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Afin de réaliser ce projet, nous a
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III. Le récepteur LRP11) Organisat
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2) Trafic intra-cellulaireComme le
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LRP1αLRP1Membrane associatedprotea
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Tableau 3 : Ligands connus du LRP1(
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I. Etude du rôle de la cathepsine
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Cathepsin-D, a key protease in brea
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IntroductionConsumption of meals ri
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(Fig. 1A, panel a). This differenti
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differentiated adipocyte (Fig. 4B).
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DiscussionOur results demonstrate t
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from normal and peri-al breast adip
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mouse RS9 (sens 5CGGCCCGGGAGCTGTTGA
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agreement of local ethic committee.
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Statistical analysis. Results are e
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Loncarek J, Freiss G, Vignon F and
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Aa3000 *b4000*B8000**cath-D mRNA(ar
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ABcath-D mRNA(ratio RS9)PPARg mRNA(
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A D3 D7 D14D0BaD0 D3 D7 D14D0 D3 D7
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AshLucshcath-DF442A C34 C37 A4 D10c
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AF442-AC34C37A4D10BF442-AC34C37A4D1
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II. Etude du rôle du LRP1 dans les
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2) Article 2:LRP1 receptor controls
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LRP1, Adipogenesis, Obesityrelative
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LRP1, Adipogenesis, ObesityFigure 3
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LRP1, Adipogenesis, ObesityFigure 5
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LRP1, Adipogenesis, ObesitySome ins
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LRP1, Adipogenesis, ObesityLipolysi
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CONCLUSIONLa cathepsine D (cath-D)
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la souris obèses. Enfin, linhibiti
Page 112 and 113: carcinogénique sont encore mal con
Page 114 and 115: Ce travail de thèse a étudié, po
Page 116 and 117: REFERENCESAhima, R. S. (2006). Adip
Page 118 and 119: implicates them as antigen presenti
Page 120 and 121: Cataldo, A. M., Barnett, J. L., Ber
Page 122 and 123: Folkman, J. (2003). Fundamental con
Page 124 and 125: Hofmann, S. M., Zhou, L., Perez-Til
Page 126 and 127: Langin, D. (2006a). Adipose tissue
Page 128 and 129: Ludwig, T., Ovitt, C. E., Bauer, U.
Page 130 and 131: Nirde, P., Derocq, D., Maynadier, M
Page 132 and 133: Rozanov, D. V., Hahn-Dantona, E., S
Page 134 and 135: Taleb, S., Cancello, R., Clement, K
Page 136 and 137: Xiao, Y., Junfeng, H., Tianhong, L.
Page 138 and 139: F. ANNEXE98
Page 140 and 141: Cathepsin D is a new ligand for ext
Page 142 and 143: INTRODUCTIONLysosomal aspartic prot
Page 144 and 145: pcDNA3.1(+)Myc-tagged LRP1b into pc
Page 146 and 147: (Protein refolding kit, Novagen) fo
Page 148 and 149: anti-mouse-gold (Aurion). Sections
Page 150 and 151: not secrete detectable levels of pr
Page 152 and 153: using cath-D-/- MEF transfected wit
Page 154 and 155: co-culture outgrowth assays with ca
Page 156 and 157: REFERENCES1. Vignon, F., Capony, F.
Page 158 and 159: steps in vivo: proliferation, angio
Page 160 and 161: 28. Laurent-Matha, V., Lucas, A., H
Page 164 and 165: Figure 1. Cath-D interacts with the
Page 166 and 167: Figure 2. Cath-D binds to residues
Page 168 and 169: Figure 3. Cath-D interacts with LRP
Page 170 and 171: Figure 5. Silencing LRP1 in cath-D
Page 172 and 173: Figure 1. Cath-D interacts with the
Page 174 and 175: Figure 6. LRP1 is the receptor medi
Page 176 and 177: Beaujouin, Figure Sup. 2cath-D-/-ME
Page 178: RésuméLaspartyl protéase catheps
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