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Relevant bibliographies by topics / Insulin-like growth factor binding protein

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Academic literature on the topic 'Insulin-like growth factor binding protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 September 2023

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Journal articles on the topic "Insulin-like growth factor binding protein"

1

Lee, Chang Hoon, Chin Saeng Cho, Kyung-You Park, Joon Woo Kim, Gwan Won Lee, Byung Kwon Lee, and 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, no. 1 (May 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, and 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, no. 1 (February 6, 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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Kostecká, Z., and J. Blahovec. "Animal insulin-like growth factor binding proteins and their biological functions." Veterinární Medicína 47, No. 2 - 3 (March 30, 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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Haugaard, Steen B., Ove Andersen, Birgitte R. Hansen, Hans Ørskov, Ulrik B. Andersen, Sten Madsbad, Johan Iversen, and Allan Flyvbjerg. "Insulin-like growth factors, insulin-like growth factor-binding proteins, insulin-like growth factor-binding protein-3 protease, and growth hormone-binding protein in lipodystrophic Human Immunodeficiency Virus-infected patients." Metabolism 53, no. 12 (December 2004): 1565–73. http://dx.doi.org/10.1016/j.metabol.2004.06.025.

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Rutanen, Eeva-Marja. "Insulin-Like Growth Factor Binding Protein-1." Seminars in Reproductive Medicine 10, no. 02 (May 1992): 154–63. http://dx.doi.org/10.1055/s-2007-1018871.

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Clay Bunn, R., and John L. Fowlkes. "Insulin-like growth factor binding protein proteolysis." Trends in Endocrinology & Metabolism 14, no. 4 (May 2003): 176–81. http://dx.doi.org/10.1016/s1043-2760(03)00049-3.

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Wang, Hsin-Shih, Jing-Der Lee, Bor-Jen Cheng, and Yung-Kuei Soong. "Insulin-like growth factor-binding protein 1 and insulin-like growth factor-binding protein 3 in pre-eclampsia." BJOG: An International Journal of Obstetrics and Gynaecology 103, no. 7 (July 1996): 654–59. http://dx.doi.org/10.1111/j.1471-0528.1996.tb09833.x.

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Kobayashi, S., D. R. Clemmons, and M. A. Venkatachalam. "Colocalization of insulin-like growth factor-binding protein with insulin-like growth factor I." American Journal of Physiology-Renal Physiology 261, no. 1 (July 1, 1991): F22—F28. http://dx.doi.org/10.1152/ajprenal.1991.261.1.f22.

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We report the localization of insulin-like growth factor I (IGF-I) and a 25-kDa form of insulin-like growth factor-binding protein (IGF-BP-1) in adult rat kidney. The antigens were localized using a rabbit anti-human IGF-I antibody, and a rabbit anti-human IGF-BP-1 antibody raised against human 25-kDa IGF-BP-1 purified from amniotic fluid. Immunohistochemistry by the avidin-biotin peroxidase conjugate technique showed that both peptides are located in the same nephron segments, in the same cell types. The most intense staining was in papillary collecting ducts. There was moderate staining also in cortical collecting ducts and medullary thick ascending limbs of Henle's loop. In collecting ducts the antigens were shown to be present in principal cells but not in intercalated cells. In distal convoluted tubules, cortical thick ascending limbs, and in structures presumptively identified as thin limbs of Henle's loops there was only modest staining. The macula densa, however, lacked immunoreactivity. Colocalization of IGF-I and IGF-BP-1 in the same cells supports the notion, derived from studies on cultured cells, that the actions of IGF-I may be modified by IGF-BPs that are present in the same location.

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Ryu, Hye-Young, Hye-Jung Hwang, In-Hye Kim, Hong-Soo Ryu, and Taek-Jeong Nam. "Effects of Glucose on Insulin-like Growth Factor Binding-5 Expression in Human Fibroblasts." Journal of Life Science 17, no. 9 (September 30, 2007): 1224–31. http://dx.doi.org/10.5352/jls.2007.17.9.1224.

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Conover, C. A., J. T. Clarkson, and L. K. Bale. "Factors regulating insulin-like growth factor-binding protein-3 binding, processing, and potentiation of insulin-like growth factor action." Endocrinology 137, no. 6 (June 1996): 2286–92. http://dx.doi.org/10.1210/endo.137.6.8641177.

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Dissertations / Theses on the topic "Insulin-like growth factor binding protein"

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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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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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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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Wang, Jing. "Novel insulin-like growth factor-binding protein proteases: detection and characterization /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-942-4/.

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Ahlsén, Maria. "Insulin-like growth factor binding protein-3 : structure and function /." Stockholm : Karolinska institutet, 2007. http://diss.kib.ki.se/2007/978-91-7357-350-4/.

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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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Alsabban, Abdulrahman Essam. "Establishing methods to screen novel small molecules targeting insulin-like growth factor/insulin-like growth factor binding protein interaction." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/45046.

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Insulin-like growth factors (IGFs) are important systemic mediators of growth and survival that suppress apoptosis and promote cell cycle progression, angiogenesis and metastatic activities in various cancers by activating IGF-IR tyrosine kinase-mediated signaling. These effects depend on the bioavailability of IGFs, which is regulated by IGF binding proteins (IGFBPs). Increased IGFBP-2 and IGFBP-5 expression observed in castration-resistant prostate cancer is thought to promote tumor progression by enhancing IGF-mediated signaling. IGFBPs have cooperative carboxy-terminal and amino-terminal low and a high affinity IGF binding sites. I hypothesize that blocking the high affinity IGF binding site can affect the bioavailability of IGFs to target tissues and thus be used for treatment of various IGF-responsive diseases including prostate cancer. I initially characterized immunologic reagents capable of being used in sandwich ELISA formats to detect IGF-I and IGFBP-5 and attempted several configurations to establish an IGF-I/IGFBP-5 “bridged” sandwich ELISA platform to measure association and dissociation of IGF-I/IGFBP-5 complex formation. The inability of all bridged ELISA formats tested to measure IGF-I/IGFBP-5 binding, lead me to developed a Bio-Layer Interferometry-based assay that measures IGF-I/ IGFBP-5 binding kinetics that will allow for screening of factors that can affect this intermolecular interaction. I demonstrated that biotinylated IGF-I bound to streptavidin-coated biosensors can be used to measure binding of recombinant IGFBP-5 [2.24 nm shift in optical density (Response)]. I also demonstrated that IGF-I could efficiently disrupt this interaction (0.21 nm shift), while the amino-terminal IGF-I mutant, E3R, exhibits an intermediate competitive activity (1.47 nm shift) and insulin exhibits a low competitive activity (1.83 nm shift). In addition, I demonstrated that IGF-I can competitively disrupted this interaction, resulting in a dissociation rate constant (Kdis 1.5-³ 1/s), In contrast, the amino terminal IGF-I mutant, E3R binds with an intermediate affinity (Kdis 5.6-⁴ 1/s), and buffer free sample results in a (Kdis) of 1.5-⁴ (1/s). These results demonstrate the capacity of this BLI-based assay to differentiate relative competitive activity of compounds that target the high affinity IGF-I binding site of IGFBPs and establish a platform to screen for factors that might be developed as rationale therapeutics to disrupt sequestration of IGF-I by IGFBPs.

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Watanabe, Shin. "Insulin-like growth factor axis (insulin-like growth factor-I/insulin-like growth factor-binding protein-3) as a prognostic predictor of heart failure: association with adiponectin." Kyoto University, 2011. http://hdl.handle.net/2433/142074.

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Balderson, Stephanie D. "Investigations of Insulin-Like Growth Factor I Cell Surface Binding: Regulation by Insulin-Like Growth Factor Binding Protein-3 and Heparan Sulfate Proteoglycan." Thesis, Virginia Tech, 1997. http://hdl.handle.net/10919/30494.

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The primary aim of this text is to gain insight on how cellular activation by a insulin-like growth factor (IGF-I), in the presence of insulin-like growth factor binding protein-3 (IGFBP-3), is influenced by heparan sulfate proteoglycans (HSPG). Initial research will be presented, assumptions and hypotheses that were included in the development of mathematical models will be discussed, and the future enhancements of the models will be explored. There are many potential scenarios for how each component might influence the others. Mathematical modeling techniques will highlight the contributions made by numerous extracellular parameters on IGF-I cell surface binding. Tentative assumptions can be applied to modeling techniques and predictions may aid in the direction of future experiments. Experimentally, it was found that IGFBP-3 inhibited IGF-I Bovine Aortic Endothelial (BAE) cell surface binding while p9 HS slightly increased IGF-I BAE cell surface binding. IGFBP-3 has a higher binding affinity for IGF-I (3 x 10-9 M) than p9 HS has for IGF-I (1.5 x 10-8 M) as determined with cell-free binding assays. The presence of p9 HS countered the inhibiting effect of IGFBP-3 on IGF-I BAE cell surface binding. Although preliminary experiments with labeled p9 HS and IGFBP-3 indicated little to no cell surface binding, later experiments indicated that both IGFBP-3 and p9 HS do bind to the BAE cell surface. Pre-incubation of BAE cells with either IGFBP-3 or p9 HS resulted in an increase of IGF-I BAE cell surface binding . There was a more substantial increase of IGF-I surface binding when cells were pre-incubated with IGFBP- 3 than p9 HS. There was a larger increase of IGF-I BAE cell surface binding when cells were pre-incubated with p9 HS than when p9 HS and IGF-I were added simultaneously. This suggests that IGFBP-3 and p9 HS surface binding plays key role in IGF-I surface binding, however, p9 HS surface binding does not alter IGF-I surface binding as much as IGFBP-3 surface binding seems to. Experimental work helps further the understanding of IGF-I cellular activation as regulated by IGFBP-3 and p9 HS. Developing mathematical models allows the researcher to focus on individual elements in a complex systems and gain insight on how the real system will respond to individual changes. Discrepancies between the model results and the experimental data presented indicate that soluble receptor inhibition is not sufficient to account for experimental results. The alliance of engineering analysis and molecular biology helps to clarify significant principles relevant to the conveyance of growth factors into tissue. Awareness of the effects of individual parameters in the delivery system, made possible with mathematical models, will provide guidance and save time in the design of future therapeutics involving growth factors.
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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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Books on the topic "Insulin-like growth factor binding protein"

1

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

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

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

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4

S, Drop Stenvert L., and Hintz Raymond L, eds. 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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Colloque médecine et recherche (8th : 2008 Paris, France). IGFs: Local repair and survival factors throughout life span. Heidelberg: Springer, 2010.

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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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1945-, LeRoith Derek, Raizada Mohan K, and International Symposium on Insulin, IGFs, and their Receptors (4th : 1993 : Woods Hole, Mass.), eds. Current directions in insulin-like growth factor research. New York: Plenum, 1993.

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8

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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9

E, Müller E., ed. IGFs in the nervous system. Berlin: Springer, 1998.

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

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Book chapters on the topic "Insulin-like growth factor binding protein"

1

Seth, John. "Insulin-Like Growth Factor Binding Protein-1." In 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." In 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." In 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." In 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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Holly, Jeff M. P., and Janet K. Fernihough. "The Insulin-Like Growth Factor (IGF) Binding Proteins (IGFBPS)." In 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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Wilczak, Nadine, and Jacques de Keyser. "Insulin-Like Growth Factor System in Amyotrophic Lateral Sclerosis." In IGF-I and IGF Binding Proteins, 160–69. Basel: KARGER, 2005. http://dx.doi.org/10.1159/000085764.

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Baxter, R. C. "Insulin-like Growth Factor Binding Proteins: Biochemical Characterization." In 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." In 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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Conover, Cheryl A., Jay T. Clarkson, Susan K. Durham, and Laurie K. Bale. "Cellular Actions of Insulin-Like Growth Factor Binding Protein-3." In Advances in Experimental Medicine and Biology, 255–66. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2988-0_25.

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Jeschke, M. G., R. E. Barrow, R. Vita, K. W. Jauch, and D. N. Herndon. "Insulin-Like Growth Factor-I in Kombination mit Insulin-Like Growth Factor Binding Protein-3 wirkt antiapoptotisch auf Hepatozyten." In Deutsche Gesellschaft für Chirurgie, 577–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-57295-1_120.

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Conference papers on the topic "Insulin-like growth factor binding protein"

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Bruns, Alexander-Francisco, Jessica Smith, Pooja Shah, Nadira Yuldasheva, Mark T. Kearney, and Stephen Wheatcroft. "145 Insulin-like growth factor binding protein 2 (igfbp2) positively regulates angiogenesis." In 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, 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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Angeles, Christina V., Markus Hafner, Nicholas D. Socci, Penelope DeCarolis, Thomas Tuschl, and Samuel Singer. "Abstract 3100: The RNA-binding protein insulin-like growth factor 2 mRNA-binding protein 3 is oncogenic in liposarcoma." 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.am10-3100.

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Silvers, Amy L., Lin Lin, David G. Beer, and Andrew C. Chang. "Abstract 830: Insulin-like growth factor binding protein-2 and chemosensitivity in esophageal adenocarcinoma." In 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." 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.am10-5004.

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Contois, Liangru W., Jennifer M. Caron, Eric Tweedie, Leonard Liebes, Robert Friesel, Calvin Vary, and Peter C. Brooks. "Abstract 3485: Insulin-like growth factor binding protein-4 (IGFBP-4) differentially inhibits growth factor induced angiogenesis in vivo." In 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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Aditya Prayudi, Pande Kadek, I. Nyoman Gede Budiana, and Ketut Suwiyoga. "54 Diagnostic accuracy of serum insulin-like growth factor binding protein 2 for ovarian cancer." In ESGO SoA 2020 Conference Abstracts. BMJ Publishing Group Ltd, 2020. http://dx.doi.org/10.1136/ijgc-2020-esgo.97.

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Scully, Tiffany, Carolyn D. Scott, Hasanthi C. de Silva, Sue M. Firth, Stephen M. Twigg, John E. Pintar, and Robert C. Baxter. "Abstract 741: Insulin-like growth factor binding protein-3 (IGFBP-3) enhances obesity-related breast tumorigenesis." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-741.

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Veraldi, Kristen L., Katelynn J. Thiel, and Carol A. Feghali-Bostwick. "Insulin-Like Growth Factor Binding Protein-5 Promotes Fibrosis Through Modulation Of The Heat Shock Response." In 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.a3488.

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Ibrahim, YH, J. Hartel, K. La Parra, and 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." In 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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Reports on the topic "Insulin-like growth factor binding protein"

1

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, July 2003. http://dx.doi.org/10.21236/ada420347.

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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, February 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, February 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, February 2002. http://dx.doi.org/10.21236/ada406049.

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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, October 2008. http://dx.doi.org/10.21236/ada519976.

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Harbeson, Caroline E., and 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, July 2003. http://dx.doi.org/10.21236/ada420331.

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Harbeson, Caroline E., and 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, July 2002. http://dx.doi.org/10.21236/ada409808.

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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, March 1995. http://dx.doi.org/10.21236/ad1011459.

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Barg, Rivka, Erich Grotewold, and Yechiam Salts. Regulation of Tomato Fruit Development by Interacting MYB Proteins. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7592647.bard.

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Background to the topic: Early tomato fruit development is executed via extensive cell divisions followed by cell expansion concomitantly with endoreduplication. The signals involved in activating the different modes of growth during fruit development are still inadequately understood. Addressing this developmental process, we identified SlFSM1 as a gene expressed specifically during the cell-division dependent stages of fruit development. SlFSM1 is the founder of a class of small plant specific proteins containing a divergent SANT/MYB domain (Barg et al 2005). Before initiating this project, we found that low ectopic over-expression (OEX) of SlFSM1 leads to a significant decrease in the final size of the cells in mature leaves and fruits, and the outer pericarp is substantially narrower, suggesting a role in determining cell size and shape. We also found the interacting partners of the Arabidopsis homologs of FSM1 (two, belonging to the same family), and cloned their tomato single homolog, which we named SlFSB1 (Fruit SANT/MYB–Binding1). SlFSB1 is a novel plant specific single MYB-like protein, which function was unknown. The present project aimed at elucidating the function and mode of action of these two single MYB proteins in regulating tomato fruit development. The specific objectives were: 1. Functional analysis of SlFSM1 and its interacting protein SlFSB1 in relation to fruit development. 2. Identification of the SlFSM1 and/or SlFSB1 cellular targets. The plan of work included: 1) Detailed phenotypic, histological and cellular analyses of plants ectopically expressing FSM1, and plants either ectopically over-expressing or silenced for FSB1. 2) Extensive SELEX analysis, which did not reveal any specific DNA target of SlFSM1 binding, hence the originally offered ChIP analysis was omitted. 3) Genome-wide transcriptional impact of gain- and loss- of SlFSM1 and SlFSB1 function by Affymetrix microarray analyses. This part is still in progress and therefore results are not reported, 4) Search for additional candidate partners of SlFSB1 revealed SlMYBI to be an alternative partner of FSB1, and 5) Study of the physical basis of the interaction between SlFSM1 and SlFSB1 and between FSB1 and MYBI. Major conclusions, solutions, achievements: We established that FSM1 negatively affects cell expansion, particularly of those cells with the highest potential to expand, such as the ones residing inner to the vascular bundles in the fruit pericarp. On the other hand, FSB1 which is expressed throughout fruit development acts as a positive regulator of cell expansion. It was also established that besides interacting with FSM1, FSB1 interacts also with the transcription factor MYBI, and that the formation of the FSB1-MYBI complex is competed by FSM1, which recognizes in FSB1 the same region as MYBI does. Based on these findings a model was developed explaining the role of this novel network of the three different MYB containing proteins FSM1/FSB1/MYBI in the control of tomato cell expansion, particularly during fruit development. In short, during early stages of fruit development (Phase II), the formation of the FSM1-FSB1 complex serves to restrict the expansion of the cells with the greatest expansion potential, those non-dividing cells residing in the inner mesocarp layers of the pericarp. Alternatively, during growth phase III, after transcription of FSM1 sharply declines, FSB1, possibly through complexing with the transcription factor MYBI serves as a positive regulator of the differential cell expansion which drives fruit enlargement during this phase. Additionally, a novel mechanism was revealed by which competing MYB-MYB interactions could participate in the control of gene expression. Implications, both scientific and agricultural: The demonstrated role of the FSM1/FSB1/MYBI complex in controlling differential cell growth in the developing tomato fruit highlights potential exploitations of these genes for improving fruit quality characteristics. Modulation of expression of these genes or their paralogs in other organs could serve to modify leaf and canopy architecture in various crops.

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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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