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Artigos de revistas sobre o tema "Insulin-like growth factor binding protein"

Autor: Grafiati

Publicado: 4 de junho de 2021

Última modificação: 7 de setembro de 2023

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1

Lee, Chang Hoon, Chin Saeng Cho, Kyung-You Park, Joon Woo Kim, Gwan Won Lee, Byung Kwon Lee e 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 (maio de 2003): 113–17. http://dx.doi.org/10.35420/jcohns.2003.14.1.113.

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2

Purwana, Arie, Budiono Budiono, Jose RL Batubara e 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 de fevereiro de 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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3

Kostecká, Z., e J. Blahovec. "Animal insulin-like growth factor binding proteins and their biological functions". Veterinární Medicína 47, No. 2 - 3 (30 de março de 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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4

Haugaard, Steen B., Ove Andersen, Birgitte R. Hansen, Hans Ørskov, Ulrik B. Andersen, Sten Madsbad, Johan Iversen e 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, n.º 12 (dezembro de 2004): 1565–73. http://dx.doi.org/10.1016/j.metabol.2004.06.025.

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5

Rutanen, Eeva-Marja. "Insulin-Like Growth Factor Binding Protein-1". Seminars in Reproductive Medicine 10, n.º 02 (maio de 1992): 154–63. http://dx.doi.org/10.1055/s-2007-1018871.

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6

Clay Bunn, R., e John L. Fowlkes. "Insulin-like growth factor binding protein proteolysis". Trends in Endocrinology & Metabolism 14, n.º 4 (maio de 2003): 176–81. http://dx.doi.org/10.1016/s1043-2760(03)00049-3.

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7

Wang, Hsin-Shih, Jing-Der Lee, Bor-Jen Cheng e 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, n.º 7 (julho de 1996): 654–59. http://dx.doi.org/10.1111/j.1471-0528.1996.tb09833.x.

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8

Kobayashi, S., D. R. Clemmons e M. A. Venkatachalam. "Colocalization of insulin-like growth factor-binding protein with insulin-like growth factor I". American Journal of Physiology-Renal Physiology 261, n.º 1 (1 de julho de 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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9

Ryu, Hye-Young, Hye-Jung Hwang, In-Hye Kim, Hong-Soo Ryu e Taek-Jeong Nam. "Effects of Glucose on Insulin-like Growth Factor Binding-5 Expression in Human Fibroblasts." Journal of Life Science 17, n.º 9 (30 de setembro de 2007): 1224–31. http://dx.doi.org/10.5352/jls.2007.17.9.1224.

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10

Conover, C. A., J. T. Clarkson e L. K. Bale. "Factors regulating insulin-like growth factor-binding protein-3 binding, processing, and potentiation of insulin-like growth factor action." Endocrinology 137, n.º 6 (junho de 1996): 2286–92. http://dx.doi.org/10.1210/endo.137.6.8641177.

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11

Zumkeller, Walter, e Kerstin Hall. "Immunoreactive insulin-like growth factor II in urine". Acta Endocrinologica 123, n.º 5 (novembro de 1990): 499–503. http://dx.doi.org/10.1530/acta.0.1230499.

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Abstract. Insulin-like growth factor II and insulin-like growth factor binding protein-1 were identified and quantified in the urine of 23 healthy subjects between 17 and 76 years of age. IGF-II was measured after separation by gel chromatography at low pH and compared with IGF-I levels in the same samples, whereas IGF binding protein-1 was measured in dialysed urine. Urinary IGF-II was found at much higher concentrations than IGF-I (mean ±sem: 717±69 vs 110±5 ng/mmol creatinine). The chromatographic profile indicates that pro-IGF-II may also be present. The concentrations of IGF-II appear to be less variable than the other reported parameters. The mean IGF binding protein-1 concentrations in these urine samples was 414±83 ng/mmol creatinine. IGFs in the urine are in part bound to binding proteins.

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12

Cohen, Pinchas. "Insulin-Like Growth Factor Binding Protein-3: Insulin-Like Growth Factor Independence Comes of Age". Endocrinology 147, n.º 5 (1 de maio de 2006): 2109–11. http://dx.doi.org/10.1210/en.2006-0195.

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13

Hasegawa, Yukihiro. "Relationship between Insulin-like Growth Factor-I and Insulin-like Growth Factor Binding Protein-3". Clinical Pediatric Endocrinology 5, Supple8 (1996): 89–93. http://dx.doi.org/10.1297/cpe.5.supple8_89.

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14

Bach, L. "Insulin-Like Growth Factor Binding Protein-6: The “Forgotten” Binding Protein?" Hormone and Metabolic Research 31, n.º 02/03 (janeiro de 1999): 226–34. http://dx.doi.org/10.1055/s-2007-978723.

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15

Bereket, Abdullah, Yasar Cesur, Behzat Ozkan, Erdal Adal, Serap Turan, Sertac Hanedan Onan, Hakan Döneray Doneray, Teoman Akcay e Goncagul Haklar. "Circulating Insulin-like Growth Factor Binding Protein-4". Journal of Clinical Research in Pediatric Endocrinology 2, n.º 1 (12 de março de 2010): 17–20. http://dx.doi.org/10.4274/jcrpe.v2i1.17.

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16

Rosenfeld, Ron G., Vivian Hwa, Elizabeth Wilson, Stephen R. Plymate e Youngman Oh. "The insulin-like growth factor-binding protein superfamily". Growth Hormone & IGF Research 10 (janeiro de 2000): S16—S17. http://dx.doi.org/10.1016/s1096-6374(00)90007-8.

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17

Ricort, Jean-Marc. "Insulin-like growth factor binding protein (IGFBP) signalling". Growth Hormone & IGF Research 14, n.º 4 (agosto de 2004): 277–86. http://dx.doi.org/10.1016/j.ghir.2004.02.002.

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18

Gabbitas, Bari, e Ernesto Canalis. "Insulin-like growth factors sustain insulin-like growth factor-binding protein-5 expression in osteoblasts". American Journal of Physiology-Endocrinology and Metabolism 275, n.º 2 (1 de agosto de 1998): E222—E228. http://dx.doi.org/10.1152/ajpendo.1998.275.2.e222.

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Insulin-like growth factors (IGFs) I and II are considered to be autocrine regulators of bone cell function. Recently, we demonstrated that IGF-I induces IGF-binding protein-5 (IGFBP-5) expression in cultures of osteoblast-enriched cells from 22-day fetal rat calvariae (Ob cells). In the present study, we postulated that IGFs play an autocrine role in the maintenance of IGFBP-5 basal expression in Ob cells. IGFBP-2 and -3, at concentrations that bind endogenous IGFs, decreased IGFBP-5 mRNA levels, as determined by Northern blot analysis, and protein levels, as determined by Western immunoblots of extracellular matrix extracts of Ob cells. IGFBP-2 and -3 in excess inhibited IGFBP-5 heterogeneous nuclear RNA levels, as determined by RT-PCR, and did not alter the half-life of IGFBP-5 mRNA in transcriptionally arrested Ob cells. In conclusion, blocking endogenous IGFs in Ob cells represses IGFBP-5 expression, suggesting that IGFs are autocrine inducers of IGFBP-5 synthesis in osteoblasts.

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19

Janssen, J. A. M. J. L., R. P. Stolk, H. A. P. Pols, D. E. Grobbee e S. W. J. Lamberts. "Serum Free and Total Insulin-Like Growth Factor-I, Insulin-Like Growth Factor Binding Protein-1 and Insulin-Like Growth Factor Binding Protein-3Levels in Healthy Elderly Individuals". Gerontology 44, n.º 5 (1998): 277–80. http://dx.doi.org/10.1159/000022026.

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20

Iglesias, P., C. Bayón, J. Méndez, P. González Gancedo, C. Grande e J. J. Díez. "Serum Insulin-Like Growth Factor Type 1, Insulin-Like Growth Factor-Binding Protein-1, and Insulin-Like Growth Factor-Binding Protein-3 Concentrations in Patients with Thyroid Dysfunction". Thyroid 11, n.º 11 (novembro de 2001): 1043–48. http://dx.doi.org/10.1089/105072501753271734.

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21

Pirazzoli, P., E. Cacciari, R. De Iasio, M. C. Pittalis, P. Dallacasa, S. Zucchini, S. Gualandi, S. Salardi, C. David e S. Boschi. "Developmental pattern of fetal growth hormone, insulin-like growth factor I, growth hormone binding protein and insulin-like growth factor binding protein-3". Archives of Disease in Childhood - Fetal and Neonatal Edition 77, n.º 2 (1 de setembro de 1997): F100—F104. http://dx.doi.org/10.1136/fn.77.2.f100.

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22

Zimmermann, E. M., L. Li, Y. T. Hou, N. K. Mohapatra e J. B. Pucilowska. "Insulin-like growth factor I and insulin-like growth factor binding protein 5 in Crohn's disease". American Journal of Physiology-Gastrointestinal and Liver Physiology 280, n.º 5 (1 de maio de 2001): G1022—G1029. http://dx.doi.org/10.1152/ajpgi.2001.280.5.g1022.

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Insulin-like growth factor (IGF)-I and its binding protein IGF binding protein 5 (IGFBP-5) were highly expressed in inflamed and fibrotic intestine in experimental Crohn's disease. IGF-I induced proliferation and increased collagen synthesis by smooth muscle cells and fibroblasts/myofibroblasts in vitro. Here we studied IGF-I and IGFBP-5 in Crohn's disease tissue. Tissue was collected from patients undergoing intestinal resection for Crohn's disease. IGF-I and IGFBP-5 mRNAs were quantitated by RNase protection assay and Northern blot analysis, respectively. In situ hybridization was performed to localize mRNA expression, and Western immunoblot was performed to quantitate protein expression. IGF-I and IGFBP-5 mRNAs were increased in inflamed/fibrotic intestine compared with normal-appearing intestine. IGF-I mRNA was expressed in multiple cell types in the lamina propria and fibroblast-like cells of the submucosa and muscularis externa. IGFBP-5 mRNA was highly expressed in smooth muscle of the muscularis mucosae and muscularis externa as well as fibroblast-like cells throughout the bowel wall. Tissue IGFBP-5 protein correlated with collagen type I ( r = 0.82). These findings are consistent with a mechanism whereby IGF-I acts on smooth muscle and fibroblasts/myofibroblasts to increase collagen synthesis and cellular proliferation; its effects may be modulated by locally expressed IGFBP-5.

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23

Storch, Stephan, Bernd Kübler, Stefan Höning, Michael Ackmann, Jürgen Zapf, Werner Blum e Thomas Braulke. "Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3". FEBS Letters 509, n.º 3 (29 de novembro de 2001): 395–98. http://dx.doi.org/10.1016/s0014-5793(01)03204-5.

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24

Morimoto, L. M. "Variation in Plasma Insulin-Like Growth Factor-1 and Insulin-Like Growth Factor Binding Protein-3: Genetic Factors". Cancer Epidemiology Biomarkers & Prevention 14, n.º 6 (1 de junho de 2005): 1394–401. http://dx.doi.org/10.1158/1055-9965.epi-04-0694.

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25

Weinzimer, Stuart A., Tara Beers Gibson, Paulo F. Collett-Solberg, Aruna Khare, Bingrong Liu e Pinchas Cohen. "Transferrin Is an Insulin-Like Growth Factor-Binding Protein-3 Binding Protein1". Journal of Clinical Endocrinology & Metabolism 86, n.º 4 (1 de abril de 2001): 1806–13. http://dx.doi.org/10.1210/jcem.86.4.7380.

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Insulin-like growth factor (IGF)-binding protein-3 (IGFBP-3) possesses both growth-inhibitory and -potentiating effects on cells that are independent of IGF action and are mediated through specific IGFBP-3 binding proteins/receptors located at the cell membrane, cytosol, or nuclear compartments and in the extracellular matrix. We have here characterized transferrin (Tf) as one of these IGFBP-3 binding proteins. Human serum was fractionated over an IGFBP-3 affinity column, and a 70-kDa protein was eluted, sequenced, and identified (through database searching and Western immunoblot) as human Tf. Tf bound IGFBP-3 but had negligible affinity to the other five IGFBPs, and iron-saturated holo-Tf bound IGFBP-3 more avidly than unsaturated Tf. Biosensor interaction analysis confirmed that this interaction is specific and sensitive, with a high association rate similar to IGF-I, and suggested that binding occurs in the vicinity of the IGFBP-3 nuclear localization site. As an independent confirmation of this interaction, using a yeast two-hybrid system, we cloned Tf from a human liver complementary DNA library as an IGFBP-3 protein partner. Tf treatment blocked IGFBP-3-induced cell proliferation in bladder smooth muscle cells, and IGFBP-3-induced apoptosis in prostate cancer cells. In summary, we have employed a combination of techniques to demonstrate that Tf specifically binds IGFBP-3, and we showed that this interaction has important physiological effects on cellular events.

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26

Platz, Elizabeth A., Michael N. Pollak, Walter C. Willett e Edward Giovannucci. "Vertex balding, plasma insulin-like growth factor 1, and insulin-like growth factor binding protein 3". Journal of the American Academy of Dermatology 42, n.º 6 (junho de 2000): 1003–7. http://dx.doi.org/10.1067/mjd.2000.103987.

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27

Duron, Emmanuelle, Benoît Funalot, Nadège Brunel, Joel Coste, Laurent Quinquis, Cécile Viollet, Joel Belmin et al. "Insulin-Like Growth Factor-I and Insulin-Like Growth Factor Binding Protein-3 in Alzheimer's Disease". Journal of Clinical Endocrinology & Metabolism 97, n.º 12 (1 de dezembro de 2012): 4673–81. http://dx.doi.org/10.1210/jc.2012-2063.

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28

Akmal, Sharifah Noor, Kankatsu Yun, Janet MacLay, Yoshikazu Higami e Takayoshi Ikeda. "Insulin-like growth factor 2 and insulin-like growth factor binding protein 2 expression in hepatoblastoma". Human Pathology 26, n.º 8 (agosto de 1995): 846–51. http://dx.doi.org/10.1016/0046-8177(95)90005-5.

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29

Zhang, Jing, Fanghui Ding, Dan Jiao, Qiaozhi Li e Hong Ma. "The Aberrant Expression of MicroRNA-125a-5p/IGF2BP3 Axis in Advanced Gastric Cancer and Its Clinical Relevance". Technology in Cancer Research & Treatment 19 (1 de janeiro de 2020): 153303382091733. http://dx.doi.org/10.1177/1533033820917332.

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RNA-binding proteins have been associated with cancer development. The overexpression of a well-known RNA-binding protein, insulin-like growth factor 2 messenger RNA–binding protein 3, has been identified as an indicator of poor prognosis in patients with various types of cancer. Although gastric cancer is a relatively frequent and potentially fatal malignancy, the mechanism by which insulin-like growth factor 2 messenger RNA–binding protein 3 regulates the development of this cancer remains unclear. This study aimed to investigate the role and regulatory mechanism of insulin-like growth factor 2 messenger RNA–binding protein 3 in gastric cancer. An analysis of IGF2BP3 expression patterns reported in 4 public gastric cancer–related microarray data sets from the Gene Expression Omnibus and The Cancer Genome Atlas-Stomach Adenocarcinoma revealed strong expression of this gene in gastric cancer tissues. Insulin-like growth factor 2 messenger RNA–binding protein 3 expression in gastric cancer was further confirmed via quantitative reverse transcription polymerase chain reaction and immunohistochemistry, respectively, in an in-house gastric cancer cohort (n = 30), and the association of insulin-like growth factor 2 messenger RNA–binding protein 3 expression with clinical parameters and prognosis was analyzed. Notably, stronger IGF2BP3 expression significantly correlated with poor prognosis, and significant changes in insulin-like growth factor 2 messenger RNA–binding protein 3 expression were only confirmed in patients with advanced-stage gastric cancer in an independent cohort. The effects of insulin-like growth factor 2 messenger RNA–binding protein 3 on cell proliferation were confirmed through in vitro experiments involving the HGC-27 gastric cancer cell line. MicroR-125a-5p, a candidate microRNA that target on insulin-like growth factor 2 messenger RNA–binding protein 3, decreased in advanced-stage gastric cancer. Upregulation of microR-125a-5p inhibited insulin-like growth factor 2 messenger RNA–binding protein 3, and dual-luciferase report assay indicated that microR-125a-5p inhibited the translation of IGF2BP3 by directly targeting the 3′ untranslated region. These results indicate that the microR-125a-5p/insulin-like growth factor 2 messenger RNA–binding protein 3 axis contributes to the oncogenesis of advanced gastric cancer.

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30

Radulović, Ž. M., L. M. Porter, T. K. Kim, M. Bakshi e A. Mulenga. "Amblyomma americanumtick saliva insulin-like growth factor binding protein-related protein 1 binds insulin but not insulin-like growth factors". Insect Molecular Biology 24, n.º 5 (25 de junho de 2015): 539–50. http://dx.doi.org/10.1111/imb.12180.

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31

Weinzimer, S. A. "Transferrin Is an Insulin-Like Growth Factor-Binding Protein-3 Binding Protein". Journal of Clinical Endocrinology & Metabolism 86, n.º 4 (1 de abril de 2001): 1806–13. http://dx.doi.org/10.1210/jc.86.4.1806.

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32

McCusker, R. H. "Controlling Insulin-Like Growth Factor Activity and the Modulation of Insulin-Like Growth Factor Binding Protein and Receptor Binding". Journal of Dairy Science 81, n.º 6 (junho de 1998): 1790–800. http://dx.doi.org/10.3168/jds.s0022-0302(98)75748-0.

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Thomas, A. G., J. M. Holly, F. Taylor e V. Miller. "Insulin like growth factor-I, insulin like growth factor binding protein-1, and insulin in childhood Crohn's disease." Gut 34, n.º 7 (1 de julho de 1993): 944–47. http://dx.doi.org/10.1136/gut.34.7.944.

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Chen, DongFeng, Yingqian Li e Eric Zhao. "Emerging roles for insulin-like growth factor binding protein like protein 1". Neural Regeneration Research 14, n.º 2 (2019): 258. http://dx.doi.org/10.4103/1673-5374.244787.

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35

Ryu, Hye-Young, Hye-Jung Hwang, In-Hye Kim, Hong-Soo Ryu e Taek-Jeong Nam. "Effects of glucose on metabolism and Insulin-like growth factor binding-3 expression in human fibroblasts." Journal of Life Science 17, n.º 5 (25 de maio de 2007): 687–93. http://dx.doi.org/10.5352/jls.2007.17.5.687.

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36

HIZUKA, Naomi. "Serum Growth Hormone Binding Protein (GHBP)and Insulin-like Growth Factor Binding Protein (IGFBP)". Folia Endocrinologica Japonica 68, n.º 10 (1992): 1073–81. http://dx.doi.org/10.1507/endocrine1927.68.10_1073.

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Barrios, V., J. Argente, J. Pozo, F. Hervás, M. T. Muñoz, J. I. Sánchez e M. Hernández. "Insulin-Like Growth Factor I, Insulin-Like Growth Factor Binding Proteins, and Growth Hormone Binding Protein in Spanish Premature and Full-Term Newborns". Hormone Research 46, n.º 3 (1996): 130–37. http://dx.doi.org/10.1159/000185009.

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38

Khosravi, M. Javad, Anastasia Diamandi e Jehangir Mistry. "Immunoassay of insulin-like growth factor binding protein-1". Clinical Chemistry 43, n.º 3 (1 de março de 1997): 523–32. http://dx.doi.org/10.1093/clinchem/43.3.523.

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Abstract Accurate measurement of insulin-like growth factor (IGF) binding protein-1 (IGFBP-1) is important for precise definition of its physiological roles and potential diagnostic values. Because altered phosphorylation results in altered IGFBP-1 immunoreactivity, current assays may significantly underestimate or fail to detect physiological changes in the IGFBP-1 concentrations. We developed three ELISAs (ELISA 1–3) using a common capture but three different detection antibodies. IGFBP-1 in serum, synovial fluid (SF), cerebrospinal fluid (CSF), and amniotic fluid (AF) were measured before and after treatment with alkaline phosphatase (ALP). Among the methods, only ELISA-1 was unaffected by IGFBP-1 phosphorylation and generated identical results before and after ALP treatment. The serum and SF values by ELISA-2 and -3 were lower by ∼4- to 10-fold, but increased after ALP treatment to within 66–98% of those by ELISA-1. The medians in AF, and to a lesser extent in CSF, by all methods were similar and did not change significantly after dephosphorylation. ELISA-1 showed excellent correlation with ELISA-2, ELISA-3, and a commercial IGFBP-1 IRMA only after ALP-treated samples were analyzed by the comparative methods. ELISA-1 is highly specific for IGFBP-1 and demonstrated acceptable analytical performance characteristics.

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Hwa, V. "The Insulin-Like Growth Factor-Binding Protein (IGFBP) Superfamily". Endocrine Reviews 20, n.º 6 (1 de dezembro de 1999): 761–87. http://dx.doi.org/10.1210/er.20.6.761.

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Bach, Leon A., Ping Fu e Zhiyong Yang. "Insulin-like growth factor-binding protein-6 and cancer". Clinical Science 124, n.º 4 (31 de outubro de 2012): 215–29. http://dx.doi.org/10.1042/cs20120343.

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The IGF (insulin-like growth factor) system is essential for physiological growth and it is also implicated in a number of diseases including cancer. IGF activity is modulated by a family of high-affinity IGF-binding proteins, and IGFBP-6 is distinctive because of its marked binding preference for IGF-II over IGF-I. A principal role for IGFBP-6 is inhibition of IGF-II actions, but recent studies have indicated that IGFBP-6 also has IGF-independent effects, including inhibition of angiogenesis and promotion of cancer cell migration. The present review briefly summarizes the IGF system in physiology and disease before focusing on recent studies on the regulation and actions of IGFBP-6, and its potential roles in cancer cells. Given the widespread interest in IGF inhibition in cancer therapeutics, increasing our understanding of the mechanisms underlying the actions of the IGF ligands, receptors and binding proteins, including IGFBP-6, will enhance our ability to develop optimal treatments that can be targeted to the most appropriate patients.

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Hwa, Vivian, Youngman Oh e Ron G. Rosenfeld. "The Insulin-Like Growth Factor-Binding Protein (IGFBP) Superfamily*". Endocrine Reviews 20, n.º 6 (1 de dezembro de 1999): 761–87. http://dx.doi.org/10.1210/edrv.20.6.0382.

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Fowlkes, John L., Kathryn M. Thrailkill, Delila M. Serra e Hideaki Nagase. "Insulin-like growth factor binding protein (IGFBP) substrate zymography". Endocrine 7, n.º 1 (agosto de 1997): 33–36. http://dx.doi.org/10.1007/bf02778059.

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Ranke, Michael B. "Insulin-like growth factor binding-protein-3 (IGFBP–3)". Best Practice & Research Clinical Endocrinology & Metabolism 29, n.º 5 (outubro de 2015): 701–11. http://dx.doi.org/10.1016/j.beem.2015.06.003.

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Marinaro, Joe A., Gary P. Jamieson, P. Mark Hogarth e Leon A. Bach. "Differential dissociation kinetics explain the binding preference of insulin-like growth factor binding protein-6 for insulin-like growth factor-II over insulin-like growth factor-I". FEBS Letters 450, n.º 3 (7 de maio de 1999): 240–44. http://dx.doi.org/10.1016/s0014-5793(99)00499-8.

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Aziz, Kamran Mahmood Ahmed. "Growth Hormone and Growth Retardation in Autoimmune Type-1 Diabetes. Insulin an Important Endocrine Growth Factor". Diabetes & Obesity International Journal 8, n.º 1 (2023): 1–7. http://dx.doi.org/10.23880/doij-16000267.

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Growth hormone (GH) secretory alterations and dysregulations with insulin-like growth factor-I (IGF-1) axis among type-1 diabetic children and adolescents is well established. In this poorly controlled abnormal metabolic state, GH hypersecretion is observed with decreased levels of Insulin-like Growth Factors (IGFs), IGF binding proteins-3 (IGFBP-3), and growth hormone binding protein (GHBP). These all factors results in decreased growth velocity and growth retardation in type-1 diabetic children and adolescents. Insulin is the most important metabolic regulator of this system. Absolute insulin deficiency, as observed in type-1 diabetics, is the primary cause of this dysregulation and alterations. Several published studies have shown that elevated HbA1c and poor glycaemic control are the main factors of this abnormal metabolic state. Conversely, studies have also demonstrated that good glycaemic control with basal bolus insulin regimens or insulin pump can improve diabetic state with restoration of normal growth. Hence this perspective review focuses on these important aspects of growth abnormalities in type-1 diabetic patients and concludes that health care policy makers should develop a close monitoring program and system with multi-disciplinary team approach to prevent further diabetes related growth complications.

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SNYDER, DAVID K., e DAVID R. CLEMMONS. "Insulin-Dependent Regulation of Insulin-Like Growth Factor-Binding Protein-1*". Journal of Clinical Endocrinology & Metabolism 71, n.º 6 (dezembro de 1990): 1632–36. http://dx.doi.org/10.1210/jcem-71-6-1632.

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Cara, José F. "Insulin-Like Growth Factors, Insulin-Like Growth Factor Binding Proteins and Ovarian Androgen Production". Hormone Research 42, n.º 1-2 (1994): 49–54. http://dx.doi.org/10.1159/000184145.

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Rosen, Clifford J. "Serum Insulin-like Growth Factors and Insulin-like Growth Factor-binding Proteins: Clinical Implications". Clinical Chemistry 45, n.º 8 (1 de agosto de 1999): 1384–90. http://dx.doi.org/10.1093/clinchem/45.8.1384.

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Abstract The last decade has been characterized by a major investigative thrust into the physiology of two unique but ubiquitous peptides, insulin-like growth factor (IGF)-I and IGF-II. The regulatory systems that control the tissue bioactivity of the IGFs have been delineated, and subcellular signaling mechanisms have been clarified. Clearly, both tissue and circulating growth factor concentrations are important in defining the relationship between IGF-I and cell activity. Bone, liver, and circulatory IGF-I have received the most attention by investigators, in part because of the ease of measurement and the interaction with disease states such as osteoporosis. More recently, attention has focused on the role IGF-I plays in neoplastic transformation and growth. Two large prospective observational studies have demonstrated greater risk for prostate and breast cancer associated with high circulating concentrations of IGF-I. Animal models and in vitro studies confirm that there is a close, albeit complex, interaction between IGF-I signaling and bone turnover. This report will focus on: (a) IGF physiology, including IGF ligands, binding proteins, and proteases; (b) the relationship between IGF-I and bone mass in respect to risk for osteoporosis; (c) the heritable regulation of the IGF-I phenotype; and (d) the association between serum IGF-I and cancer risk. The IGFs remain a major area for basic and clinical investigations; future studies may define both diagnostic and therapeutic roles for these peptides or their related proteins in several disease states.

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Roelen, Corné A., Hans P. Koppeschaar, Wouter R. de Vries, Pierre M. Zelissen, Yvonne E. Snel, Manorath E. Doerga, Jos H. Thijssen e Rien A. Blankenstein. "High-affinity growth hormone binding protein, insulin-like growth factor I and insulin-like growth factor binding protein 3 in adults with growth hormone deficiency". European Journal of Endocrinology 135, n.º 1 (julho de 1996): 82–86. http://dx.doi.org/10.1530/eje.0.1350082.

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Roelen CA, Koppeschaar HP, de Vries WR, Zelissen PM, Snel YE, Doerga ME, Thijssen JH, Blankenstein RA. High-affinity growth hormone binding protein, insulin-like growth factor I and insulin-like growth factor binding protein 3 in adults with growth hormone deficiency. Eur J Endocrinol 1996;135:82–6. ISSN 0804–4643 The high-affinity growth hormone binding protein (GHBP) circulates in human blood and represents the extracellular domain of the growth hormone (GH) receptor. The effects of GH deficiency on GHBP in adults are not clear. The aim of this study was to evaluate serum GHBP levels in adults with GH deficiency and to assess whether GHBP measurement may contribute to the diagnosis of adult GH deficiency, based on a two-step model. We measured insulin-like growth factor I (IGF-I), IGF binding protein 3 (IGFBP-3) and GHBP levels in serum samples of 36 patients with adult-onset GH deficiency. The GHBP levels were measured by FPLC size-exclusion chromatography; IGF-I and IGFBP-3 levels were measured by RIA. Serum GHBP levels were elevated above the upper limit of the 95% confidence interval in 26 patients, whereas IGF-I and IGFBP-3 levels were low in 10 patients and in 16 patients, respectively. The combination of low serum IGF-I and low IGFBP-3 levels was found in 10 patients. In nine patients, serum IGF-I levels were low, with elevated GHBP levels. Low serum IGF-I, low IGFBP-3 and elevated GHBP levels were found in five patients. Only four out of 36 patients had serum IGF-I, IGFBP-3 and GHBP levels that were within the 95% confidence interval of the control values. We conclude that adults with acquired GH deficiency have elevated GHBP levels in comparison to healthy subjects. We suggest that measurement of GHBP levels might contribute to the diagnosis of adult GH deficiency, though further research is required to study the additional value of GHBP measurements. HPF Koppeschaar, Department of Endocrinology, University Hospital Utrecht, HPL00.407, PO Box 85500, 3508 GA Utrecht, The Netherlands

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Mofid, MohammadReza, Elham Jafari, Ali Gheysarzadeh, Karim Mahnam, Rezvan Shahmohammadi, Amir Ansari e Hadi Bakhtyari. "In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1". Research in Pharmaceutical Sciences 13, n.º 4 (2018): 332. http://dx.doi.org/10.4103/1735-5362.235160.

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