Relevant bibliographies by topics / Insulin-like growth factor-II

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Insulin-like growth factor-II'

Author: Grafiati
Published: 4 June 2021
Last updated: 29 July 2024

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Journal articles on the topic "Insulin-like growth factor-II"

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TALLY, M., and K. HALL. "Insulin-Like Growth Factor II Effects Mediated through Insulin-Like Growth Factor II Receptors." Acta Paediatrica 79, s367 (April 1990): 67–73. http://dx.doi.org/10.1111/j.1651-2227.1990.tb11636.x.

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Choh Hao Li, Donald Yamashiro, R. Glenn Hammonds, and Manfred Westphal. "Synthetic insulin-like growth factor II." Biochemical and Biophysical Research Communications 127, no. 2 (March 1985): 420–24. http://dx.doi.org/10.1016/s0006-291x(85)80177-7.

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Giani, C., D. Campani, A. Rasmussen, P. Fierabracci, P. Miccoli, G. Bevilacqua, A. Pinchera, and K. J. Cullen. "Insulin-like growth factor II (IGF-II) immunohistochemistry." International Journal of Biological Markers 17, no. 2 (2002): 90–95. http://dx.doi.org/10.5301/jbm.2008.3917.

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Lamas, Eugenia, Frédérique Zindy, Danielle Seurin, Christiane Guguen-Guillouzo, and Christian Brechot. "Expression of insulin-like growth factor II and receptors for insulin-like growth factor II, insulin-like growth factor I and insulin in isolated and cultured rat hepatocytes." Hepatology 13, no. 5 (May 1991): 936–40. http://dx.doi.org/10.1002/hep.1840130522.

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Soares, Marcelo Bento, Arthur Turken, Douglas Ishii, Leslie Mills, Vasso Episkopou, Sean Cotter, Scott Zeitlin, and Argiris Efstratiadis. "Rat insulin-like growth factor II gene." Journal of Molecular Biology 192, no. 4 (December 1986): 737–52. http://dx.doi.org/10.1016/0022-2836(86)90025-2.

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ASAKAWA, KUMIKO, NAOMI HIZUKA, KAZUE TAKANO, IZUMI FUKUDA, IZUMI SUKEGAWA, HIROSHI DEMURA, and KAZUO SHIZUME. "Radioimmunoassay for Insulin-Like Growth Factor II(IGF-II)." Endocrinologia Japonica 37, no. 5 (1990): 607–14. http://dx.doi.org/10.1507/endocrj1954.37.607.

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Lee, P. D. K., D. Hodges, R. L. Hintz, J. H. Wyche, and R. G. Rosenfeld. "Identification of receptors for insulin-like growth factor II in two insulin-like growth factor II producing cell lines." Biochemical and Biophysical Research Communications 134, no. 2 (January 1986): 595–600. http://dx.doi.org/10.1016/s0006-291x(86)80461-2.

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Nolan, C. "Variable accumulation of insulin-like growth factor II in mouse tissues deficient in insulin-like growth factor II receptor." International Journal of Biochemistry & Cell Biology 31, no. 12 (December 1999): 1421–33. http://dx.doi.org/10.1016/s1357-2725(99)00103-x.

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GELATO, M. C., and J. VASSALOTTI. "Insulin-Like Growth Factor-II: Possible Local Growth Factor in Pheochromocytoma*." Journal of Clinical Endocrinology & Metabolism 71, no. 5 (November 1990): 1168–74. http://dx.doi.org/10.1210/jcem-71-5-1168.

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Tremollieres, Florence A., Donna D. Strong, David J. Baylink, and Subburaman Mohan. "Insulin-like growth factor II and transforming growth factor β1 regulate insulin-like growth factor I secretion in mouse bone cells." Acta Endocrinologica 125, no. 5 (November 1991): 538–46. http://dx.doi.org/10.1530/acta.0.1250538.

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Abstract. Bone cells in culture produce and respond to growth factors, suggesting that local as well as systemic factors regulate bone volume. Previous studies have shown that IGF-I is the major mitogen produced by mouse bone cells and that its production is regulated by systemic agents such as PTH and estrogen. Because IGF-II and transforming growth factor β1 have been shown, respectively, to increase and decrease MC3T3-E1 cell proliferation, we tested the hypothesis that these two growth factors modulate the production of IGF-I in this cell line. In order to eliminate artifacts owing to IGF binding proteins, conditioned media samples were pretreated with IGF-II before measurement of IGF-I by RIA. After 24 h treatment at a density of 2.5× 104 cells/cm2, IGF-II (10 μg/l) induced a 2.2-fold increase compared with untreated control (9.5±1.5 vs 4.2±0.44 pg/μg protein, p<0.001), whereas transforming growth factor β1 (1 μg/l) caused a 66% decrease in IGF-I production (1.5±0.3 vs 4.2±0.44 pg/μg protein, p<0.001). Both IGF-II and transforming growth factor β1 regulated IGF-I production in a dose-, time- and cell density-dependent manner. The lowest effective doses for IGF-II and transforming growth factor β1 were 1 and 0.01 μg/l, respectively. These results support a role for IGF-II and transforming growth factor β1 as potent modulators of IGF-I secretion in mouse bone cells. Furthermore, regulation of IGF-I production in bone cells by IGF-II and transforming growth factor β1 in an autocrine/paracrine manner could represent a component part of the mechanism whereby the skeleton locally adapts in reponse to external stimuli.
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Dissertations / Theses on the topic "Insulin-like growth factor-II"

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Burns, Jason Lee. "Growth control by insulin-like growth factor II." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270285.

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Mörth, Corinna. "Consequences of postnatal insulin-like growth factor II overexpression in insulin-like growth factor I deficient mice." Diss., lmu, 2005. http://nbn-resolving.de/urn:nbn:de:bvb:19-46307.

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Horn, Henrik von. "Regulation of insulin-like growth factor-II in human liver /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-880-0/.

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Zhang, Qimin. "Insulin-like growth factor II : cellular effects through different receptors /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-2754-5.

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Gadd, Stephanie Clare. "Insulin-like growth factor II in preovulatory follicles and ovarian cysts." Thesis, University of Southampton, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296517.

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Ohlsen, Susan M. "Cloning and characterization of ovine insulin, insulin-like growth factor-I and -II genes." Diss., This resource online, 1993. http://scholar.lib.vt.edu/theses/available/etd-06062008-165729/.

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Gustafsson, Sara. "The insulin-like growth factor system - effects of circulating proteases /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-436-8/.

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Olausson, Hanna. "Nutritional status before and during pregnancy in relation to the maternal insulin-like growth factor-system and health related variables in the offspring : studies in women, guinea pigs and rats /." Linköping : Univ, 2004. http://www.bibl.liu.se/liupubl/disp/disp2004/med860s.pdf.

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Elliss, Carolyn. "Studies of the role of IGF-II during mouse development." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.291034.

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Makins, Richard John. "Insulin-like growth factor-II in colitis and colitis-associated colorectal cancer." Thesis, Queen Mary, University of London, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.419706.

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Books on the topic "Insulin-like growth factor-II"

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

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K, Raizada Mohan, and LeRoith Derek 1945-, eds. The Role of insulin-like growth factors in the nervous system. New York, N.Y: New York Academy of Sciences, 1993.

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International Symposium on Molecular and Cellular Biology of Insulin and IGFs (3rd 1990 Gainesville, Fla.). Molecular biology and physiology of insulin and insulin-like growth factors. New York: Plenum Press, 1991.

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Le, Dai-Trang ELizabeth. The role of insulin, insulin-like growth factors I and II, insulin- like growth factor binding protein 3, and their receptors in the regulation of human fetal growth. [New Haven, Conn: s.n.], 1993.

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Lawlor, Margaret Ann. The role of the insulin-like growth factor-II/mannose-6-phosphate receptor in embryonic development. Dublin: University College Dublin, 1998.

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Tübingen, Universität, ed. Struktur und Funktion der Bindungsproteine für Insulin-like Growth Factor I und II im Humanserum. [S.l.]: [s.n.], 1987.

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Varela-Nieto, Isabel, and Julie Ann Chowen. Growth Hormone/Insulin-Like Growth Factor Axis During Development. Springer, 2005.

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Stenvert L.S. Drop (Editor) and Raymond L. Hintz (Editor), eds. Insulin-like Growth Factor Binding Proteins (International Congress). Elsevier, 1990.

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DeChiara, Thomas Michael. Expression and function of the insulin-like growth factor II gene. 1990.

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IGF and Nutrition in Health and Disease (Nutrition and Health). Humana Press, 2004.

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Book chapters on the topic "Insulin-like growth factor-II"

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Seth, John. "Insulin-Like Growth Factor-II." In The Immunoassay Kit Directory, 204–5. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-1414-1_30.

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Baxter, Robert C., and Carolyn D. Scott. "Insulin-Like Growth Factor-II Receptors." In Receptor Purification, 329–46. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0461-9_17.

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van Dijk, Erwin L., and P. Elly Holthuizen. "Site-Specific Cleavage of Insulin-Like Growth Factor II mRNAs." In Endocrine Updates, 239–54. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-6446-8_14.

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Nissley, Peter, Wieland Kiess, and Mark Sklar. "The Insulin-Like Growth Factor-II/Mannose 6-Phosphate Receptor." In Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors, 359–67. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5685-1_30.

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Polychronakos, Constantin. "The Insulin-Like Growth Factor-II/Mannose 6-Phosphate Receptor." In Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors, 369–80. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5685-1_31.

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Gammeltoft, Steen, Jan Christiansen, Finn C. Nielsen, and Sten Verland. "Insulin-Like Growth Factor II: Complexity of Biosynthesis and Receptor Binding." In Advances in Experimental Medicine and Biology, 31–44. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5949-4_4.

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Canalis, Ernesto, Michael Centrella, and Thomas L. McCarthy. "Role of Insulin-Like Growth Factor I And II on Skeletal Remodeling." In Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors, 459–66. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5685-1_38.

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Tan, E. M., J. Y. Zhang, and E. K. L. Chan. "Autoantibodies to insulin-like growth factor II mRNA-binding proteins in hepatocellular carcinoma." In Immunology and Liver, 8–15. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-011-4000-3_2.

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Zarrilli, Raffaele, Vittorio Colantuoni, Raffaella Faraonio, Stefano Casola, Elena Rossi, and Carmelo B. Bruni. "Extinction of Human Insulin-Like Growth Factor II Expression in Somatic Cell Hybrids." In Advances in Experimental Medicine and Biology, 77–83. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5949-4_7.

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Nishimoto, Ikuo, Etsuro Ogata, and Itaru Kojima. "Insulin-like Growth Factor II Stimulates Calcium Influx in Competent Balb/c 3T3 Cells Primed with Epidermal Growth Factor." In Cell Calcium Metabolism, 255–64. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5598-4_28.

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Conference papers on the topic "Insulin-like growth factor-II"

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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, and 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." In 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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Hsu, E., and CA Feghali-Bostwick. "Insulin-Like Growth Factor-II (IGF-II) Contributes to Fibrosis in Systemic Sclerosis-Related Pulmonary Fibrosis Via Insulin Receptor." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2703.

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Collins, LC, MS Rice, D. Shen, JL Connolly, SJ Schnitt, and RM Tamimi. "P4-11-02: Insulin-Like Growth Factor-1 (IGF-1), Insulin-Like Growth Factor Binding Protein-3 (IGFBP-3) and Lobule Type among Women in the Nurses' Health Study II (NHS II)." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p4-11-02.

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VV, Kocherova, and Shcherbak VA. "P195 Growth hormone and insulin-like growth factor ii in mothers and their newborn children with intrauterine growth retardation." In 8th Europaediatrics Congress jointly held with, The 13th National Congress of Romanian Pediatrics Society, 7–10 June 2017, Palace of Parliament, Romania, Paediatrics building bridges across Europe. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2017. http://dx.doi.org/10.1136/archdischild-2017-313273.283.

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Thomas, Justin M., and Carol Feghali-Bostwick. "Insulin-Like Growth Factor-II Receptor Activation And Downstream Effects In Scleroderma-Related Pulmonary Fibrosis." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1955.

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Hsu, Eileen, and Carol Feghali-Bostwick. "Insulin-like Growth Factor-II (IGF-II) Contributes To The Pathogenesis Of Systemic Sclerosis (SSc)-associated Pulmonary Fibrosis." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3512.

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Chen, Teng, Qin-Song Zuo, Ronghua Zhao, Dian-Xu Feng, Chao Chen, Yi-Min Jiang, Marcia Cruz-Correa, Alan G. Casson, and Feng Han. "Abstract 194: Loss of imprinting and abnormal expression of insulin-like growth factor II in gastric cancer." In 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.am10-194.

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Radhakrishnan, Vinodh Kumar, Qianwei Tan, Marino A. De León, and Daisy D. De León. "Abstract 536: Insulin-like growth factor II (IGF-II) is a potential target for the treatment of triple negative breast cancers (TNBC)." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-536.

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Zhao, Ronghua, Ron Geyer, John Decoteau, and Alan Casson. "Abstract A9: Expression of insulin-like growth factor II and of the type 1 receptor gene in esophageal adenocarcinoma." In Abstracts: Frontiers in Cancer Prevention Research 2008. American Association for Cancer Research, 2008. http://dx.doi.org/10.1158/1940-6207.prev-08-a9.

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Singh, Sharda Kalla, Qianwei Tan, Marino De Leon, and Daisy De Leon. "Abstract 281: Insulin-like growth factor II differential activation of the IGF-1 and insulin receptors in African-American and Caucasian breast cancer tissues." In 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.am10-281.

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Reports on the topic "Insulin-like growth factor-II"

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Jarrard, David F. Relaxation of Insulin-Like Growth Factor II Imprinting in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, January 2005. http://dx.doi.org/10.21236/ada433881.

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Jarrard, David F. Relaxation of Insulin-Like Growth Factor II Imprinting in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, January 2003. http://dx.doi.org/10.21236/ada414797.

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Jarrard, David F. Relaxation of Insulin-Like Growth Factor II Imprinting in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, January 2004. http://dx.doi.org/10.21236/ada423078.

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Kaup, Sahana S. Control of Expression of Insulin-Like Growth Factor II in Stromal Cells of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada397706.

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Ruttimann, Jacqueline. Control of Expression of Insulin-Like Growth Factor II in Stromal Cells of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, December 2002. http://dx.doi.org/10.21236/ada413130.

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

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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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Hansen, Peter J., and Amir Arav. Embryo transfer as a tool for improving fertility of heat-stressed dairy cattle. United States Department of Agriculture, September 2007. http://dx.doi.org/10.32747/2007.7587730.bard.

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The overall objective of the current proposal is to develop procedures to improve the pregnancy rate achieved following transfer of fresh or cryopreserved embryos produced in the laboratory into heat-stress recipients. The overall hypothesis is that pregnancy rate in heat-stressed lactating cows can be improved by use of embryo transfer and that additional gains in pregnancy rate can be achieved through development of procedures to cryopreserve embryos, select embryos most likely to establish and maintain pregnancy after transfer, and to enhance embryo competence for post-transfer survival through manipulation of culture conditions. The original specific objectives were to 1) optimize procedures for cryopreservation (Israel/US), 2) develop procedures for identifying embryos with the greatest potential for development and survival using the remote monitoring system called EmbryoGuard (Israel), 3) perform field trials to test the efficacy of cryopreservation and the EmbryoGuard selection system for improving pregnancy rates in heat-stressed, lactating cows (US/Israel), 4) test whether selection of fresh or frozen-thawed blastocysts based on measurement of group II caspase activity is an effective means of increasing survival after cryopreservation and post-transfer pregnancy rate (US), and 5) identify genes in blastocysts induced by insulin-like growth factor-1 (IGF-1) (US). In addition to these objectives, additional work was carried out to determine additional cellular determinants of embryonic resistance to heat shock. There were several major achievements. Results of one experiment indicated that survival of embryos to freezing could be improved by treating embryos with cytochalasin B to disrupt the cytoskeleton. An additional improvement in the efficacy of embryo transfer for achieving pregnancy in heat-stressed cows follows from the finding that IGF-1 can improve post-transfer survival of in vitro produced embryos in the summer but not winter. Expression of several genes in the blastocyst was regulated by IGF-1 including IGF binding protein-3, desmocollin II, Na/K ATPase, Bax, heat shock protein 70 and IGF-1 receptor. These genes are likely candidates 1) for developing assays for selection of embryos for transfer and 2) as marker genes for improving culture conditions for embryo production. The fact that IGF-1 improved survival of embryos in heat-stressed recipients only is consistent with the hypothesis that IGF-1 confers cellular thermotolerance to bovine embryos. Other experiments confirmed this action of IGF-1. One action of IGF-1, the ability to block heat-shock induced apoptosis, was shown to be mediated through activation of the phosphatidylinositol 3-kinase pathway. Other cellular determinants of resistance of embryos to elevated temperature were identified including redox status of the embryo and the ceramide signaling pathway. Developmental changes in embryonic apoptosis responses in response to heat shock were described and found to include alterations in the capacity of the embryo to undergo caspase-9 and caspase-3 activation as well as events downstream from caspase-3 activation. With the exception of IGF-1, other possible treatments to improve pregnancy rate to embryo transfer were not effective including selection of embryos for caspase activity, treatment of recipients with GnRH.and bilateral transfer of twin embryos. In conclusion, accomplishments achieved during the grant period have resulted in methods for improving post-transfer survival of in vitro produced embryos transferred into heat-stressed cows and have lead to additional avenues for research to increase embryo resistance to elevated temperature and improve survival to cryopreservation. In addition, embryo transfer of vitrified IVF embryos increased significantly the pregnancy rate in repeated breeder cows.
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