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Littérature scientifique sur le sujet « Insulin-like growth factor-binding proteins »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 26 juillet 2024

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Articles de revues sur le sujet "Insulin-like growth factor-binding proteins"

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Kostecká, Z., et J. Blahovec. « Animal insulin-like growth factor binding proteins and their biological functions ». Veterinární Medicína 47, No. 2 - 3 (30 mars 2012) : 75–84. http://dx.doi.org/10.17221/5807-vetmed.

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Insulin-like growth factor (IGF-I, IGF-II) action is influenced by until today known eight forms of insulin-like growth factor binding proteins (IGFBPs). They have been obtained not only from some human and animal tissues and body fluids but also from conditioned medium of cell cultures. An important biological property of the IGFBPs is their ability to increase the circulating half-life of the IGFs. They are able to act as potentiators of cell proliferation. As IGFBPs bind to cell surfaces, they may act either to deliver the IGFs to those surfaces for activation of specific receptors or to activate cell responses independently of receptor activation. Phosphorylation, glycosylation and proteolysis of IGFBPs influence their affinity to IGFs. The IGFBPs in the role of inhibitors may block the activity of the IGFs and be used for antimitogenic therapy. In the last time measuring of IGFBPs levels can be used for diagnosis determination of some endocrine diseases or in differential diagnostics.

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Lee, Chang Hoon, Chin Saeng Cho, Kyung-You Park, Joon Woo Kim, Gwan Won Lee, Byung Kwon Lee et Jae Soo Lee. « The Role of Insulin-Like Growth Factor I and Binding Protein in Cholesteatoma Fibroblasts ». Journal of Clinical Otolaryngology Head and Neck Surgery 14, n^o 1 (mai 2003) : 113–17. http://dx.doi.org/10.35420/jcohns.2003.14.1.113.

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Purwana, Arie, Budiono Budiono, Jose RL Batubara et Muhammad Faizi. « Association of Growth Velocity with Insulin-Like Growth Factor-1 and Insulin-Like Growth Factor Binding Protein-3 Levels in Children with a Vegan Diet ». Journal of Biomedicine and Translational Research 6, n^o 1 (6 février 2020) : 6–10. http://dx.doi.org/10.14710/jbtr.v6i1.5474.

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Background: The vegan diet in children provides the benefit of reducing the risk of being overweight and improving the fat profile. The risk that can occur in the provision of a vegan diet in children is anthropometric size below reference and low caloric intake. Growth hormone (GH) and Insulin like Growth Factors (IGFs) are powerful stimulators for longitudinal growth of bone and require insulin-like growth factor binding protein (IGFBPs) which acts as a transport protein for IGF-1. A vegan diet with lower calorie intake in children has lower IGF-I levels than children with an omnivorous diet.Objective: Examining the effect of vegan diets on IGF-1 levels, IGFBP-3 levels, and growth velocity.Methods: This study was done with a prospective cohort design. The study subjects were divided into two groups, namely the vegan group and the omnivorous group, then matched based on age and sex. During the study, anthropometric data collection, IGF-1 and IGFBP-3 levels measurements were done in both vegan children and omnivorous children.Results: During 6 months of observation, 22 subjects were divided into two groups, namely children with a vegan diet and children with an omnivorous diet. IGF-1 (ng / mL) in vegan children was 105.5 ± 47.3 compared to 102.7 ± 42.3 in omnivorous children with a value of p = 0.89. IGFBP-3 (ng / mL) in vegan children was 2146.4 ± 595.1 compared to 2142 ± 609.1 in omnivorous children with value of p = 0.99 and Growth Velocity (cm / 6 months) was 3.0 in vegan children (1.0-5.30), and 3.2 (2.6-6.5) in omnivorous children with value of p = 0.41.Conclusion:Children with vegan diet had IGF-1 level, IGFBP-3 level, and growth velocity that were the same as children with an omnivorous diet.

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Leroith, Derek. « Insulin-like growth factor receptors and binding proteins ». Baillière's Clinical Endocrinology and Metabolism 10, n^o 1 (janvier 1996) : 49–73. http://dx.doi.org/10.1016/s0950-351x(96)80298-9.

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Coverley, J. A., et R. C. Baxter. « Phosphorylation of insulin-like growth factor binding proteins ». Molecular and Cellular Endocrinology 128, n^o 1-2 (avril 1997) : 1–5. http://dx.doi.org/10.1016/s0303-7207(97)04032-x.

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Collet, Chris, et Judith Candy. « How many insulin-like growth factor binding proteins ? » Molecular and Cellular Endocrinology 139, n^o 1-2 (avril 1998) : 1–6. http://dx.doi.org/10.1016/s0303-7207(98)00078-1.

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Baxter, Robert C. « Insulin-like growth factor binding proteins as glucoregulators ». Metabolism 44 (octobre 1995) : 12–17. http://dx.doi.org/10.1016/0026-0495(95)90215-5.

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Bach, Leon A. « Insulin-like growth factor binding proteins 4-6 ». Best Practice & ; Research Clinical Endocrinology & ; Metabolism 29, n^o 5 (octobre 2015) : 713–22. http://dx.doi.org/10.1016/j.beem.2015.06.002.

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Ferry Jr., Robert J., Ruben W. Cerri et Pinchas Cohen. « Insulin-Like Growth Factor Binding Proteins : New Proteins, New Functions ». Hormone Research in Paediatrics 51, n^o 2 (1999) : 53–67. http://dx.doi.org/10.1159/000023315.

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Feld, Stella M., et Raimund Hirschberg. « Insulin-like growth factor-I and insulin-like growth factor-binding proteins in the nephrotic syndrome ». Pediatric Nephrology 10, n^o 3 (1 mai 1996) : 355–58. http://dx.doi.org/10.1007/s004670050124.

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Thèses sur le sujet "Insulin-like growth factor-binding proteins"

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Robertson, James Gray. « Insulin-like growth factors and insulin-like growth factor binding proteins in wounds / ». Title page, contents and abstract only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phr6509.pdf.

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Hopkins, Nicholas John. « Insulin-like growth factor-I and its binding proteins ». Thesis, University of Reading, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240702.

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Clark, Sarah Jane. « The growth hormone, insulin-like growth factor, insulin-like growth factor binding proteins and insulin axis in acute liver failure ». Thesis, King's College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.397943.

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Jones, Tiffany Celeste. « Syndecan-4 binds insulin-like growth factor binding protein-4 ». Birmingham, Ala. : University of Alabama at Birmingham, 2009. https://www.mhsl.uab.edu/dt/2010r/jones.pdf.

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Mireuta, Matei. « Aspects of insulin-like growth factor binding proteins in cancer ». Thesis, McGill University, 2013. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=114128.

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The insulin-like growth factor (IGF) system is composed of two ligands (IGF-1 and IGF-2), two receptors (IGF-1R and IGF-2R) and six binding proteins (IGFBP-1 to -6). IGFs act as endocrine, paracrine and autocrine growth factors and stimulate cell growth, proliferation and metabolism. There is extensive evidence, both from in vitro and in vivo models as well as population studies, that IGF physiology is relevant to neoplasia. IGF-1R is the physiologic receptor for both ligands and its activation elicits a plethora of changes at the cellular level, such as activation of PI3K/AKT/mTOR and Ras/Raf/MAP kinase pathways. Given its role in the maintenance and promotion of neoplasia, the IGF system represents a potential target in the context of cancer therapy.Classically, IGFBPs have been described as carrier proteins for IGFs in the blood and other fluids. They can regulate IGF bioavailability both positively through increases in ligand half-life as well as negatively through competition with the IGF-1R for ligand binding. In addition to their classical roles, there is evidence suggesting that IGFBPs can act independently of IGFs by poorly characterized mechanisms. Additionally, epidemiologic studies have correlated overexpression of certain IGFBPs, in particular IGFBP-2, with poor prognosis in various cancers.Although the role of IGFBPs has been extensively studied in the context of both normal and malignant growth, this thesis describes several new aspects of IGFBPs in neoplasia. In the second chapter, we study the effect of the PI3K/AKT/mTOR cascade on IGFBP-2 gene expression in a breast cancer cell line in vitro. We demonstrate that activation of this pathway essentially leads to an Sp1-dependent increase in IGFBP-2 gene transcription. We further show that Sp-1 is phosphorylated upon PI3K/AKT/mTOR pathway activation and accumulates in the nucleus. In the third chapter, we study the effects of 2-deoxyglucose (2-DG) on IGF-1:IGFBP-3 complex formation. A recent publication suggested that 2-DG unexpectedly disrupted IGF-1:IGFBP-3 binding leading to increases in IGF-1R and AKT signaling in various cell lines. We show by three different techniques that neither 2-DG nor glucose affect IGF-1:IGFBP-3 complex formation. We additionally show that the 2-DG effects observed are not consistent between cell lines and likely the result of changes in intracellular signaling. In the fourth chapter, we study the effects of a novel therapeutic antibody (BI836845) with high affinity for both IGF-1 and IGF-2. In mouse serum samples ex vivo, we show that the addition of BI836845 leads to a shift of IGF-1 from the IGFBPs to the antibody. In vivo, we demonstrate that BI836845 binds the vast majority of IGF-1. Finally, we demonstrate that BI836845 induces a decrease in IGFBP-3 and an increase in growth hormone levels in C57 BL/6 mice.
L'ensemble du système de facteurs de croissance insulinomimétique (IGF) est composé de deux ligands (IGF-1 et IGF-2), de deux récepteurs (IGF- 1R et IGF-2R) et de six protéines de liaison (IGFBP-1 à 6). Les IGFs sont des hormones endocrines, paracrines et autocrines qui stimulent la croissance cellulaire, la prolifération et le métabolisme. Il existe un grand nombre d'études utilisant des approches épidémiologiques ou des modèles in vivo et in vitro qui démontrent l'importance des IGFs dans le contexte du cancer. Le IGF-1R est le récepteur physiologique des deux ligands et son activation mène à d'importants changements cellulaires tels que l'activation des voies de signalisation PI3K/AKT/mTOR et Ras/Raf/MAPK. Étant donné son rôle dans la promotion et dans la progression du cancer, le système des IGFs représente une cible potentielle pour le traitement du cancer. De façon classique, les protéines de liaison IGFBP ont été décrites comme de simples porteurs d'IGFs dans le sang et autres fluides. Les IGFBPs peuvent modifier la biodisponibilité des IGFs de façon positive en augmentant leur demi-vie ou de façon négative due à leur compétition avec le IGF-1R pour la liaison. En plus de leur rôle classique, il est de plus en plus évident que ces protéines peuvent agir de manière indépendante, mais les mécanismes impliqués restent flous. Également, il existe des études épidémiologiques qui ont corrélé la surexpression de IGFBPs, en particulier IGFBP-2, avec un pronostic défavorable dans plusieurs formes de cancer. Bien que le rôle des IGFBPs ait été largement étudié dans le contexte de la croissance normale et en néoplasie, la présente thèse révèle quelques nouveaux aspects de la physiologie des IGFBPs dans le contexte du cancer. En première partie, nous étudions l'effet de la voie de signalisation PI3K/AKT/mTOR sur l'expression du gène IGFBP-2 dans une lignée cellulaire de cancer du sein. Nous démontrons que l'activation de cette voie mène essentiellement à une augmentation de la transcription de ce gène de manière dépendante au facteur de transcription Sp-1. De plus, nous établissons que Sp-1 est phosphorylé par l'activation de la voie PI3K/AKT/mTOR et s'accumule dans le noyau. En deuxième partie, nous étudions les effets de la molécule 2-deoxyglucose (2-DG) sur la liaison entre IGF-1 et IGFBP-3. Un récent article avait suggéré un effet inhibitoire de cette molécule sur la formation de complexes IGF -1 :IGFBP-3. Nous démontrons par trois méthodes différentes que 2-DG ou la molécule apparentée glucose n'ont aucun effet sur la liaison entre IGF-1 et IGFBP-3. De plus, nous démontrons que les effets cellulaires de 2-DG sur l'activation de la voie PI3K/AKT/mTOR observées par les auteurs de l'article en question ne sont pas universels et sont probablement le résultat de signaux intracellulaires. Finalement, en dernière partie, nous étudions les effets d'un nouvel anticorps thérapeutique nommé BI836845 qui possède une grande affinité pour IGF-1 et IGF-2. Dans des échantillons de sérum de souris ex vivo, nous démontrons que l'ajout de BI836845 déplace IGF-1 des complexes naturels contenant les IGFBPs vers des complexes contenant l'anticorps. In vivo, nous démontrons que BI836845 lie la grande majorité d'IGF-1. Nous démontrons aussi que l'anticorps mène à une baisse de la concentration de IGFBP-3 et à une hausse de la concentration de l'hormone de croissance chez des souris C57 BL/6.

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Twigg, Stephen Morris. « Insulin-like growth factor binding protein-5 and its complexes ». Thesis, The University of Sydney, 1998. https://hdl.handle.net/2123/27686.

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The insulin-like growth factors, IGF-I and IGF-H, are multifunctional proteins. They are anabolic and they regulate glycaemia, and at tissue and cellular level, IGFs are mitogenic and anti—apoptotic and they may modify differentiated cell function. In serum and tissues IGF bioactivity is modified by six well characterised insulin-like growth factor binding proteins (IGFBPs), that have high affinity for IGF-I and IGF-II.

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Milner, Steven John. « The oxidative folding of insulin-like growth factor-I analogues / ». Title page, table of contents and summary only, 1996. http://web4.library.adelaide.edu.au/theses/09PH/09phm65945.pdf.

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Nickerson, Tara. « A role for insulin-like growth factor binding proteins in apoptosis ». Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0022/NQ50229.pdf.

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Lucic, Melinda Robin. « Characterisation of the molecular interactions between insulin-like growth factors and their binding proteins ». Title page, contents and abstract only, 2001. http://web4.library.adelaide.edu.au/theses/09PH/09phl9375.pdf.

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Addenda inserted in back. Includes bibliographical references (leaves 139-160) Assesses the importance of amino acids 221 to 236 of bIGFBP-2 for IGF binding activity, by creating amino acid substitutions.

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de, los Rios Patricia. « Insulin-like growth factor binding proteins (IGFBPs) in ovine fetal growth plate chondrocytes ». Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0011/MQ28557.pdf.

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Livres sur le sujet "Insulin-like growth factor-binding proteins"

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S, Drop Stenvert L., et Hintz Raymond L, dir. Insulin-like growth factor binding proteins : Proceedings of a workshop on insulin-like growth factor binding proteins, Vancouver BC, Canada, June 17-19, 1989. Amsterdam : Excerpta Medica, 1989.

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1945-, LeRoith Derek, Zumkeller Walter et Baxter R. C, dir. Insulin-like growth factors. Georgetown, Tex : Eurekah.com, Landes Bioscience, 2003.

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1945-, LeRoith Derek, Zumkeller Walter et Baxter R. C, dir. Insulin-like growth factors. Georgetown, Tex : Landes Bioscience/Eurekah.com, 2003.

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Colloque médecine et recherche (8th : 2008 Paris, France). IGFs : Local repair and survival factors throughout life span. Heidelberg : Springer, 2010.

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Jr, Roberts Charles T., et Rosenfeld Ron G, dir. The IGF system : Molecular biology, physiology, and clinical applications. Totowa, N.J : Humana Press, 1999.

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1945-, LeRoith Derek, dir. Insulin-like growth factors : Molecular and cellular aspects. Boca Raton : CRC Press, 1991.

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Leyck, Dieken Markus, Federwisch Matthias, De Meyts Pierre et Wollmer Axel 1935-, dir. Insulin & related proteins : Structure to function and pharmacology. Dordrecht : Kluwer Academic Publishers, 2002.

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Westwood, Melissa. Biochemical characterisation of insulin-like growth factor binding protein-1. Manchester : University of Manchester, 1994.

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White, Darren Andrew. An analytical study of insulin-like growth factor binding proteins in human serum. Birmingham : University of Birmingham, 1995.

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Sue, Houston M., Holly Jeffrey M. P et Feldman Eva L, dir. IGF and nutrition in health and disease. Totowa, N.J : Humana Press, 2005.

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Chapitres de livres sur le sujet "Insulin-like growth factor-binding proteins"

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Holly, Jeff M. P., et Janet K. Fernihough. « The Insulin-Like Growth Factor (IGF) Binding Proteins (IGFBPS) ». Dans Growth Hormone, 77–96. Boston, MA : Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-5163-8_5.

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Baxter, R. C. « Insulin-like Growth Factor Binding Proteins : Biochemical Characterization ». Dans Growth Hormone and Somatomedins during Lifespan, 100–108. Berlin, Heidelberg : Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78217-6_9.

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Clemmons, D. R. « Role of Insulin-like Growth Factor Binding Proteins in Modulating Insulin-like Growth Factor Action ». Dans Growth Hormone and Somatomedins during Lifespan, 109–16. Berlin, Heidelberg : Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78217-6_10.

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Seth, John. « Insulin-Like Growth Factor Binding Protein-1 ». Dans The Immunoassay Kit Directory, 206. Dordrecht : Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-1414-1_31.

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Seth, John. « Insulin-Like Growth Factor Binding Protein-3 ». Dans The Immunoassay Kit Directory, 207–9. Dordrecht : Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-1414-1_32.

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Bidlingmaier, M. « Insulin-like growth factor binding protein-3 ». Dans Lexikon der Medizinischen Laboratoriumsdiagnostik, 1–2. Berlin, Heidelberg : Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_1585-1.

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Bidlingmaier, M. « Insulin-like growth factor binding protein-3 ». Dans Springer Reference Medizin, 1257–58. Berlin, Heidelberg : Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_1585.

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Wilczak, Nadine, et Jacques de Keyser. « Insulin-Like Growth Factor System in Amyotrophic Lateral Sclerosis ». Dans IGF-I and IGF Binding Proteins, 160–69. Basel : KARGER, 2005. http://dx.doi.org/10.1159/000085764.

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Minniti, Giuseppe, et Youngman Oh. « Insulin-Like Growth Factor Binding Proteins in Endocrine-Related Neoplasia ». Dans Endocrine Oncology, 215–35. Totowa, NJ : Humana Press, 2000. http://dx.doi.org/10.1007/978-1-59259-223-4_11.

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Ocrant, Ian. « Insulin-Like Growth Factor Binding Proteins in the Nervous System ». Dans Advances in Experimental Medicine and Biology, 471–82. Boston, MA : Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5949-4_42.

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Actes de conférences sur le sujet "Insulin-like growth factor-binding proteins"

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Bruns, Alexander-Francisco, Jessica Smith, Pooja Shah, Nadira Yuldasheva, Mark T. Kearney et Stephen Wheatcroft. « 145 Insulin-like growth factor binding protein 2 (igfbp2) positively regulates angiogenesis ». Dans British Cardiovascular Society Annual Conference ‘High Performing Teams’, 4–6 June 2018, Manchester, UK. BMJ Publishing Group Ltd and British Cardiovascular Society, 2018. http://dx.doi.org/10.1136/heartjnl-2018-bcs.141.

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Rice, Megan S., Rulla M. Tamimi, James L. Connolly, Laura C. Collins, Dejun Shen, Michael N. Pollak, Bernard Rosner, Susan E. Hankinson et Shelley S. Tworoger. « Abstract A68 : Insulin-like growth factor-1, insulin-like growth factor binding protein-3, and lobule type in the Nurses' Health Study II ». Dans Abstracts : AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011 ; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-a68.

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Park, Jae-Hyun, Morten Grønbech Rasch, Jing Qiu, Ida Katrine Lund, Zena Werb et Mikala Egeblad. « Abstract 2465 : Matrix metalloproteinase 9 promotes breast cancer through regulation of insulin-like growth factor-binding proteins ». Dans Proceedings : AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012 ; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2465.

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Silvers, Amy L., Lin Lin, David G. Beer et Andrew C. Chang. « Abstract 830 : Insulin-like growth factor binding protein-2 and chemosensitivity in esophageal adenocarcinoma ». Dans Proceedings : AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012 ; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-830.

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Dar, Altaf A. « Abstract 5004 : Functional modulation of insulin-like growth factor binding protein-3 in melanoma ». Dans Proceedings : AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010 ; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5004.

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Contois, Liangru W., Jennifer M. Caron, Eric Tweedie, Leonard Liebes, Robert Friesel, Calvin Vary et Peter C. Brooks. « Abstract 3485 : Insulin-like growth factor binding protein-4 (IGFBP-4) differentially inhibits growth factor induced angiogenesis in vivo ». Dans Proceedings : AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011 ; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3485.

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Angeles, Christina V., Markus Hafner, Nicholas D. Socci, Penelope DeCarolis, Thomas Tuschl et Samuel Singer. « Abstract 3100 : The RNA-binding protein insulin-like growth factor 2 mRNA-binding protein 3 is oncogenic in liposarcoma ». Dans Proceedings : AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010 ; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3100.

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Aditya Prayudi, Pande Kadek, I. Nyoman Gede Budiana et Ketut Suwiyoga. « 54 Diagnostic accuracy of serum insulin-like growth factor binding protein 2 for ovarian cancer ». Dans ESGO SoA 2020 Conference Abstracts. BMJ Publishing Group Ltd, 2020. http://dx.doi.org/10.1136/ijgc-2020-esgo.97.

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Ibrahim, YH, J. Hartel, K. La Parra et D. Yee. « Insulin-like growth factor binding protein-1 (IGFBP-1) targets both the insulin-like growth factor (IGF) and integrin pathways for the inhibition of breast cancer cell motility. » Dans CTRC-AACR San Antonio Breast Cancer Symposium : 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-402.

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Ahasic, Amy M., Rihong Zhai, Li Su, Konstantinos Aronis, Christos S. Mantzoros, B. T. Thompson et David C. Christiani. « IGFBP3 Polymorphism Is Associated With Plasma Insulin-Like Growth Factor (IGF)-1 And Insulin-Like Growth Factor Binding Protein (IGFBP-3) In An Intensive Care Unit (ICU) Cohort ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3545.

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Rapports d'organisations sur le sujet "Insulin-like growth factor-binding proteins"

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Gross, Jennifer M. Insulin-Like Growth Factor Binding Protein-1 Interacts with Integrins to Inhibit Insulin-Like Growth Factor-Induced Breast Cancer Growth and Migration. Fort Belvoir, VA : Defense Technical Information Center, juillet 2003. http://dx.doi.org/10.21236/ada420347.

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Harbeson, Caroline E., et Steven A. Rosenzweig. The Role of Insulin-Like Growth Factor (IGF) Binding Proteins (IGFBPs) in IGF-Mediated Tumorigenicity. Fort Belvoir, VA : Defense Technical Information Center, juillet 2003. http://dx.doi.org/10.21236/ada420331.

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Harbeson, Caroline E., et Steven A. Rosenzweig. The Role of the Insulin-Like Growth Factor (IGF) Binding Proteins (IGFBPs) in IGF-Mediated Tumorigenicity. Fort Belvoir, VA : Defense Technical Information Center, juillet 2002. http://dx.doi.org/10.21236/ada409808.

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4

Rosenfeld, Ron G. A Novel Member of the Insulin-Like Growth Factor Binding Protein Superfamily in Prostate Cancer. Fort Belvoir, VA : Defense Technical Information Center, février 2004. http://dx.doi.org/10.21236/ada438221.

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Rosenfeld, Ron G. A Novel Member of the Insulin-Like Growth Factor Binding Protein Superfamily in Prostate Cancer. Fort Belvoir, VA : Defense Technical Information Center, février 2001. http://dx.doi.org/10.21236/ada393860.

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Rosenfeld, Ron G. A Novel Member of the Insulin-Like Growth Factor Binding Protein Superfamily in Prostate Cancer. Fort Belvoir, VA : Defense Technical Information Center, février 2002. http://dx.doi.org/10.21236/ada406049.

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7

Schoen, Timothy J. Expression and Characterization of Insulin-Like Growth Factor Binding Proteins (IGFBPs) and IGFBP-2 mRNA in the Developing Chicken Eye. Fort Belvoir, VA : Defense Technical Information Center, mars 1995. http://dx.doi.org/10.21236/ad1011459.

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8

Dodd, Janice G. In Vivo Activity of Insulin-Like Growth Factor Binding Protein-3 in Prevention of Prostate Cancer Progression. Fort Belvoir, VA : Defense Technical Information Center, octobre 2008. http://dx.doi.org/10.21236/ada519976.

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9

Erickson, Keesha E., Oleksii S. Rukhlenko, Md Shahinuzzaman, Kalina P. Slavkova, Yen Ting Lin, Edward C. Stites, Marian Anghel et al. Modeling cell line-specific recruitment of signaling proteins to the insulin-like growth factor 1 receptor. Office of Scientific and Technical Information (OSTI), septembre 2018. http://dx.doi.org/10.2172/1473773.

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10

Funkenstein, Bruria, et Shaojun (Jim) Du. Interactions Between the GH-IGF axis and Myostatin in Regulating Muscle Growth in Sparus aurata. United States Department of Agriculture, mars 2009. http://dx.doi.org/10.32747/2009.7696530.bard.

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Résumé :

Growth rate of cultured fish from hatching to commercial size is a major factor in the success of aquaculture. The normal stimulus for muscle growth in growing fish is not well understood and understanding the regulation of muscle growth in fish is of particular importance for aquaculture. Fish meat constitutes mostly of skeletal muscles and provides high value proteins in most people's diet. Unlike mammals, fish continue to grow throughout their lives, although the size fish attain, as adults, is species specific. Evidence indicates that muscle growth is regulated positively and negatively by a variety of growth and transcription factors that control both muscle cell proliferation and differentiation. In particular, growth hormone (GH), fibroblast growth factors (FGFs), insulin-like growth factors (IGFs) and transforming growth factor-13 (TGF-13) play critical roles in myogenesis during animal growth. An important advance in our understanding of muscle growth was provided by the recent discovery of the crucial functions of myostatin (MSTN) in controlling muscle growth. MSTN is a member of the TGF-13 superfamily and functions as a negative regulator of skeletal muscle growth in mammals. Studies in mammals also provided evidence for possible interactions between GH, IGFs, MSTN and the musclespecific transcription factor My oD with regards to muscle development and growth. The goal of our project was to try to clarify the role of MSTNs in Sparus aurata muscle growth and in particular determine the possible interaction between the GH-IGFaxis and MSTN in regulating muscle growth in fish. The steps to achieve this goal included: i) Determining possible relationship between changes in the expression of growth-related genes, MSTN and MyoD in muscle from slow and fast growing sea bream progeny of full-sib families and that of growth rate; ii) Testing the possible effect of over-expressing GH, IGF-I and IGF-Il on the expression of MSTN and MyoD in skeletal muscle both in vivo and in vitro; iii) Studying the regulation of the two S. aurata MSTN promoters and investigating the possible role of MyoD in this regulation. The major findings of our research can be summarized as follows: 1) Two MSTN promoters (saMSTN-1 and saMSTN-2) were isolated and characterized from S. aurata and were found to direct reporter gene activity in A204 cells. Studies were initiated to decipher the regulation of fish MSTN expression in vitro using the cloned promoters; 2) The gene coding for saMSTN-2 was cloned. Both the promoter and the first intron were found to be polymorphic. The first intron zygosity appears to be associated with growth rate; 3) Full length cDNA coding for S. aurata growth differentiation factor-l I (GDF-II), a closely related growth factor to MSTN, was cloned from S. aurata brain, and the mature peptide (C-terminal) was found to be highly conserved throughout evolution. GDF-II transcript was detected by RT -PCR analysis throughout development in S. aurata embryos and larvae, suggesting that this mRNA is the product of the embryonic genome. Transcripts for GDF-Il were detected by RT-PCR in brain, eye and spleen with highest level found in brain; 4) A novel member of the TGF-Bsuperfamily was partially cloned from S. aurata. It is highly homologous to an unidentified protein (TGF-B-like) from Tetraodon nigroviridisand is expressed in various tissues, including muscle; 5) Recombinant S. aurata GH was produced in bacteria, refolded and purified and was used in in vitro and in vivo experiments. Generally, the results of gene expression in response to GH administration in vivo depended on the nutritional state (starvation or feeding) and the time at which the fish were sacrificed after GH administration. In vitro, recombinantsaGH activated signal transduction in two fish cell lines: RTHI49 and SAFI; 6) A fibroblastic-like cell line from S. aurata (SAF-I) was characterized for its gene expression and was found to be a suitable experimental system for studies on GH-IGF and MSTN interactions; 7) The gene of the muscle-specific transcription factor Myogenin was cloned from S. aurata, its expression and promoter activity were characterized; 8) Three genes important to myofibrillogenesis were cloned from zebrafish: SmyDl, Hsp90al and skNAC. Our data suggests the existence of an interaction between the GH-IGFaxis and MSTN. This project yielded a great number of experimental tools, both DNA constructs and in vitro systems that will enable further studies on the regulation of MSTN expression and on the interactions between members of the GHIGFaxis and MSTN in regulating muscle growth in S. aurata.

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