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

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Published: 4 June 2021

Last updated: 29 July 2024

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Chang, Shiuh Y., and Yat-Sen Ho. "Immunohistochemical analysis of insulin-like growth factor I, insulin-like growth factor I receptor and insulin-like growth factor II in endometriotic tissue and endometrium." Acta Obstetricia et Gynecologica Scandinavica 76, no. 2 (January 1997): 112–17. http://dx.doi.org/10.3109/00016349709050064.

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12

Bell, G. I., D. S. Gerhard, N. M. Fong, R. Sanchez-Pescador, and L. B. Rall. "Isolation of the human insulin-like growth factor genes: insulin-like growth factor II and insulin genes are contiguous." Proceedings of the National Academy of Sciences 82, no. 19 (October 1, 1985): 6450–54. http://dx.doi.org/10.1073/pnas.82.19.6450.

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13

Zhang, Qimin, Per-Olof Berggren, Olof Larsson, Kerstin Hall, and Michael Tally. "Insulin-like Growth Factor II Inhibits Glucose-Induced Insulin Exocytosis." Biochemical and Biophysical Research Communications 243, no. 1 (February 1998): 117–21. http://dx.doi.org/10.1006/bbrc.1997.8053.

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14

Rey, F., F. M. Rodríguez, N. R. Salvetti, M. M. Palomar, C. G. Barbeito, N. S. Alfaro, and H. H. Ortega. "Insulin-Like Growth Factor-II and Insulin-Like Growth Factor-Binding Proteins in Bovine Cystic Ovarian Disease." Journal of Comparative Pathology 142, no. 2-3 (February 2010): 193–204. http://dx.doi.org/10.1016/j.jcpa.2009.11.002.

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15

Zumkeller, Walter, and Kerstin Hall. "Immunoreactive insulin-like growth factor II in urine." Acta Endocrinologica 123, no. 5 (November 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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16

YAMASHIRO, DONALD, and CHOH HAO LI. "Chemical synthesis of insulin-like growth factor II." International Journal of Peptide and Protein Research 26, no. 3 (January 12, 2009): 299–304. http://dx.doi.org/10.1111/j.1399-3011.1985.tb03208.x.

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17

Reeve, Anthony E., David MO Becroft, Ian M. Morison, and Ryuji Fukuzawa. "Insulin-like growth factor-II imprinting in cancer." Lancet 359, no. 9323 (June 2002): 2050–51. http://dx.doi.org/10.1016/s0140-6736(02)08947-x.

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18

Jeng, Jeng-Eing, Lea-Yea Chuang, Wang-Lung Chuang, Jan-Gowth Chang, and Jung-Fa Tsai. "Insulin-like growth factor II in hepatocellular carcinoma." Biomarkers in Medicine 1, no. 2 (August 2007): 261–71. http://dx.doi.org/10.2217/17520363.1.2.261.

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19

Zhang, Q., M. Tally, O. Larsson, R. T. Kennedy, L. Huang, K. Hall, and P. O. Berggren. "Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells." Proceedings of the National Academy of Sciences 94, no. 12 (June 10, 1997): 6232–37. http://dx.doi.org/10.1073/pnas.94.12.6232.

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20

O'Dell, Sandra D., and Ian N. M. Day. "Molecules in focus Insulin-like growth factor II (IGF-II)." International Journal of Biochemistry & Cell Biology 30, no. 7 (July 1998): 767–71. http://dx.doi.org/10.1016/s1357-2725(98)00048-x.

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21

GAMMELTOFT, STEEN, GISELA HASELBACHER, ROBERT BALLOTTI, BENGT WESTERMARK, RENÉ E. HUMBEL, and EMMANUEL Van OBBERGHEN. "Insulin-like growth factor II in mammalian brain interacts with two types of insulin-like growth factor receptor." Biochemical Society Transactions 14, no. 6 (December 1, 1986): 1161–62. http://dx.doi.org/10.1042/bst0141161.

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22

Merriman, Harold L., Donn La Tour, Thomas A. Linkhart, Subburaman Mohan, David J. Baylink, and Donna D. Strong. "Insulin-like growth factor-I and insulin-like growth factor-II induce c-fos in mouse osteoblastic cells." Calcified Tissue International 46, no. 4 (April 1990): 258–62. http://dx.doi.org/10.1007/bf02555005.

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23

Samaan, Naguib A., Pamela N. Schultz, and Frank K. Pham. "Insulin-like growth factor II and nonsuppressible insulin-like activity levels in newborns." American Journal of Obstetrics and Gynecology 163, no. 6 (December 1990): 1836–39. http://dx.doi.org/10.1016/0002-9378(90)90760-5.

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24

Hari, J., S. B. Pierce, D. O. Morgan, V. Sara, M. C. Smith, and R. A. Roth. "The receptor for insulin-like growth factor II mediates an insulin-like response." EMBO Journal 6, no. 11 (November 1987): 3367–71. http://dx.doi.org/10.1002/j.1460-2075.1987.tb02658.x.

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25

Scott, Carolyn D., and Jocelyn Weiss. "Soluble insulin-like growth factor II/mannose 6-phosphate receptor inhibits DNA synthesis in insulin-like growth factor II sensitive cells." Journal of Cellular Physiology 182, no. 1 (January 2000): 62–68. http://dx.doi.org/10.1002/(sici)1097-4652(200001)182:1<62::aid-jcp7>3.0.co;2-x.

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26

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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27

Marinaro, Joe A., Gary P. Jamieson, P. Mark Hogarth, and 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, no. 3 (May 7, 1999): 240–44. http://dx.doi.org/10.1016/s0014-5793(99)00499-8.

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28

Germain-Lee, E. L., M. Janicot, R. Lammers, A. Ullrich, and S. J. Casella. "Expression of a type I insulin-like growth factor receptor with low affinity for insulin-like growth factor II." Biochemical Journal 281, no. 2 (January 15, 1992): 413–17. http://dx.doi.org/10.1042/bj2810413.

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We investigated the binding properties of the type I insulin-like growth factor (IGF) receptor expressed in NIH-3T3 fibroblasts transfected with a human type I receptor cDNA. Cell surface receptors bound IGF-I with KD = 1 nM as predicted. Although recent studies have suggested that IGF-I and IGF-II bind to type I receptors with near-equal affinity, the receptors in this system bound IGF-II with much lower affinity (KD = 15-20 nM). When type I receptors from the transfected cells were solubilized and immunopurified, however, both 125I-IGF-I and 125I-IGF-II bound to the purified receptors with extremely high and relatively similar affinities (KD = 8 and 17 pM respectively). Thus the immunopurified receptors had higher affinity but lower specificity for the two ligands. The monoclonal antibody alpha IR-3 effectively inhibited IGF-I binding to cell surface receptors (75 +/- 10%), but did not inhibit IGF-II binding. In the purified receptor assay, alpha IR-3 also inhibited IGF-I binding more effectively than IGF-II binding (38 +/- 7% versus 10 +/- 4%). We conclude that the products of this cDNA can account for the binding patterns that we previously observed in receptors immunopurified from human placenta. The differential effect of alpha IR-3 on IGF-I versus IGF-II raises the possibility that these homologous growth factors bind to immunologically distinct epitopes on the type I receptor.

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29

FORSYTH, ISABEL A., GIANFRANCO GABAI, and GEOFF MORGAN. "Spatial and temporal expression of insulin-like growth factor-I, insulin-like growth factor-II and the insulin-like growth factor-I receptor in the sheep fetal mammary gland." Journal of Dairy Research 66, no. 1 (February 1999): 35–44. http://dx.doi.org/10.1017/s0022029998003240.

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The mammary gland is an example of a tissue of epidermal origin that depends for the development of its characteristic morphology on underlying mesenchymal cells. The interaction between mesenchyme and epithelium appears to be mediated by polypetide growth factors. In situ hybridization has been used to study, in the mammary gland of female sheep fetuses, the distribution of mRNA for the mammary mitogens, insulin-like growth factor (IGF)-I and IGF-II, and the IGF-I receptor, from 10 to 20 weeks of intrauterine life (term is ∼22 weeks). At 10 weeks, secondary ducts had formed from the primary duct. By week 20, the gland had increased in volume and complexity, showing primitive lobules embedded in intralobular connective tissue disposed around main ducts. IGF-I and IGF-II mRNA were expressed in cells of the intralobular connective tissue underlying the epithelium, while the IGF-I receptor was expressed in epithelium. Quantitation by absorbance measurements showed that mRNA expression increased with pregnancy stage for IGF-I and IGF-II, but not significantly for the IGF-I receptor, and that IGF-II was more highly expressed than IGF-I. A role for the IGF system in mediating mesenchymal–epithelial interactions in mammary development is indicated.

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30

Miettinen, P. J., T. Otonkoski, and R. Voutilainen. "Insulin-like growth factor-II and transforming growth factor-α in developing human fetal pancreatic islets." Journal of Endocrinology 138, no. 1 (July 1993): 127—NP. http://dx.doi.org/10.1677/joe.0.1380127.

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ABSTRACT To understand the development of the human pancreas better, we studied the expression and regulation of insulin, insulin-like growth factor-II (IGF-II) and transforming growth factor-α (TGF-α) genes in the human fetal pancreas and islet-like cell clusters (ICC) from the second trimester human fetuses. Northern blot analysis revealed an abundant expression of IGF-II, insulin and TGF-α mRNAs in the intact pancreas and the cultured ICCs. Furthermore, transcripts for insulin receptor, type-1 and -2 IGF receptors, and GH receptor could be amplified by polymerase chain reaction analysis from the pancreas and the ICCs. With in-situ hybridization, IGF-II mRNA was found in abundance in both the exocrine and endocrine pancreas, exceeding the amount of insulin mRNA. In ICCs, insulin mRNA-containing cells were present as small clusters in the periphery and in the centre of the clusters corresponding to the immunolocation of insulin. The ICCs also contained many epidermal growth factor-, insulin- and type-1 IGF receptor- and TGF-α-positive cells. When the ICCs were cultured in the presence of various secretagogues, only dibutyryl cyclic AMP was found to up-regulate insulin mRNA (39%; P < 0·05). IGF-II mRNA was also under cyclic AMP-dependent regulation (threefold increase; P = 0·025). Furthermore, blocking the type-1 IGF receptor with a monoclonal receptor antibody drastically reduced insulin expression (87%; P = 0·005) and additionally down-regulated IGF-II mRNA (49%; P = 0·005). IGF-1, IGF-II, TGF-α or epidermal growth factor-receptor antibody had no significant effect on either insulin or IGF-II mRNA. Exogenous TGF-α inhibited the release of insulin by the ICCs. It was concluded that IGF-II and TGF-α may be involved in the regulation of islet growth and differentiation. Journal of Endocrinology (1993) 138, 127–136

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31

van Buul-Offers, Sylvia, C. M. Hoogerbrugge, and T. L. de Poorter. "The bovine placenta: a specific radioreceptor assay for both insulin-like growth factor I and insulin-like growth factor II." Acta Endocrinologica 118, no. 2 (June 1988): 306–13. http://dx.doi.org/10.1530/acta.0.1180306.

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Abstract. Binding of labelled IGF-I and IGF-II was studied to bovine, ovine and human placental cell membranes. The data show a preponderance of type I receptors in human placental membranes, and of type II receptors in ovine placental membranes, confirming reported data. In contrast, bovine placental membranes are rich in both type I and type II receptors. Therefore, the bovine placenta offers a good model for measuring specifically IGF-I (cross-reactivity with IGF-II 7%) and IGF-II (cross-reactivity with IGF-I 4%). By Scatchard analysis the apparent Kd (1–1.36 nmol/l) for the high affinity binding sites of the type I receptor is similar in all three preparations. Total binding capacity in ovine placental membranes is, however, 4 times lower. The affinity for the type II receptor is lower than for type I, whereas total binding capacity is higher. Affinity cross-linking confirms the competition experiments, showing binding of IGF-I to typical type I and of IGF-II to type II receptors.

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32

Han, R. N., V. K. Han, S. Buch, B. A. Freeman, M. Post, and A. K. Tanswell. "Insulin-like growth factor-I and type I insulin-like growth factor receptor in 85% O2-exposed rat lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 271, no. 1 (July 1, 1996): L139—L149. http://dx.doi.org/10.1152/ajplung.1996.271.1.l139.

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The expression of insulin-like growth factor I (IGF-I) and insulin-like growth factor II (IGF-II) was studied in the lungs of adult rats exposed to air or 85% O2, using Northern analysis, in situ hybridization, and immunohistochemistry. Distribution of the type I insulin-like growth factor receptor (IGF-IR) was assessed by immunohistochemistry. IGF-I, but not IGF-II, was localized to airway epithelium, while IGF-IR was localized to perivascular and peribronchial cells, in the lungs of animals breathing air. IGF-II mRNA did not increase with exposure to 85% O2, but IGF-II was localized to sites of perivascular edema and to occasional peribronchial cells. A widespread increase in IGF-I mRNA and peptide was seen after both a 6-day and a 14-day exposure to O2, with maximal expression in the airway and alveolar epithelium, and lesser expression in interstitial cells. After 6 days in 85% O2, increased IGF-IR immunoreactivity was localized to both perivascular and peribronchial cells and to endothelial cells. By 14 days in 85% O2, IGF-IR immunoreactivity was also localized to alveolar epithelial cells. The distribution of IGF-IR immunoreactivity was consistent with a paracrine role for IGF-I in O2-mediated pulmonary hypertension and airway hyperreactivity, by mediating smooth muscle cell hyperplasia, as well as a role in endothelial cell repair and late pneumocyte hyperplasia. The relative insensitivity of IGF-IR immunohistochemistry did not allow us to identify cells with low abundance IGF-IR, and potential cellular targets for IGF-I actions after O2-exposure may be even more extensive than those recognized here.

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33

Renehan, A. G. "Circulating Insulin-Like Growth Factor II and Colorectal Adenomas." Journal of Clinical Endocrinology & Metabolism 85, no. 9 (September 1, 2000): 3402–8. http://dx.doi.org/10.1210/jc.85.9.3402.

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34

Renehan, Andrew G., John E. Painter, Domhnall O’Halloran, Wendy S. Atkin, Christopher S. Potten, Sarah T. O’Dwyer, and Stephen M. Shalet. "Circulating Insulin-Like Growth Factor II and Colorectal Adenomas*." Journal of Clinical Endocrinology & Metabolism 85, no. 9 (September 1, 2000): 3402–8. http://dx.doi.org/10.1210/jcem.85.9.6770.

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Abstract Circulating insulin-like growth factor I (IGF-I) and IGF-binding protein-3 (IGFBP-3) may be risk factors for the development of colorectal cancer. On the other hand, IGF-II and IGFBP-2 are overexpressed in colorectal carcinomas. These contrasting backgrounds led us to investigate the relationship between serum IGF-I, IGF-II, IGFBP-2, and IGFBP-3 and the presence of colorectal adenomas, known precursors of colorectal carcinoma, in 345 volunteers attending a screening flexible sigmoidoscopy trial (entry criteria: healthy, aged 55–64 yr). The most striking finding was an elevated mean serum IGF-II in individuals with adenomas (n = 52) compared with controls (mean difference, 139 ng/mL; 95% confidence intervals, 82, 196; P < 0.0001). Logistic regression adjusting for confounding factors confirmed the significant association between IGF-II and adenoma occurrence (P < 0.0001) and revealed an additional positive association with serum IGFBP-2 (P < 0.0001). However, there was no association found between either serum IGF-I and/or IGFBP-3 and the presence of adenomas. Additionally, in 31 individuals with adenomas in whom levels were determined pre- and postpolypectomy, there was a significant fall in mean IGF-II (P < 0.001) and IGFBP-2 (P < 0.001) after adenoma removal, but no difference in IGF-II and IGFBP-2 concentrations between repeated samples in 20 individuals without adenomas. Immunohistochemical studies demonstrated IGF-II expression in 83% of all adenomas, which contrasted with absent expression in normal colonic expression and hyperplastic polyps. This study has shown for the first time that serum IGF-II may be a tumor marker in individuals with colorectal adenomas. Further studies are needed to validate these relationships in larger populations, including individuals undergoing colonoscopy.

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35

Prosser, C. G., and I. R. Fleet. "Secretion of insulin-like growth factor II into milk." Biochemical and Biophysical Research Communications 183, no. 3 (March 1992): 1230–37. http://dx.doi.org/10.1016/s0006-291x(05)80322-5.

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36

MOZELL, ROBIN, KENNETH M. ROSEN, PIETER DIKKES, HEIDI CIPOLLONE, and LYDIA VILLA-KOMAROFF. "Insulin-like Growth Factor-II in Developing Murine Cerebellum." Annals of the New York Academy of Sciences 692, no. 1 The Role of I (August 1993): 277–80. http://dx.doi.org/10.1111/j.1749-6632.1993.tb26233.x.

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37

Gronowicz, Gloria A., Mary-Beth McCarthy, Hai Zhang, and Wenjian Zhang. "Insulin-like growth factor II induces apoptosis in osteoblasts." Bone 35, no. 3 (September 2004): 621–28. http://dx.doi.org/10.1016/j.bone.2004.05.005.

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38

Near, S. L., L. R. Whalen, J. A. Miller, and D. N. Ishii. "Insulin-like growth factor II stimulates motor nerve regeneration." Proceedings of the National Academy of Sciences 89, no. 24 (December 15, 1992): 11716–20. http://dx.doi.org/10.1073/pnas.89.24.11716.

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39

Braulke, Thomas, Christa Causin, Abdul Waheed, Ulrich Junghans, Andrej Hasilik, Peter Maly, RenéE Humbel, and Kurt von Figura. "Mannose 6-phosphate/insulin-like growth factor II receptor: Distinct binding sites for mannose 6-phosphate and insulin-like growth factor II." Biochemical and Biophysical Research Communications 150, no. 3 (February 1988): 1287–93. http://dx.doi.org/10.1016/0006-291x(88)90769-3.

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40

Doorn, Jaap. "Insulin‐like growth factor‐II and bioactive proteins containing a part of the E‐domain of pro‐insulin‐like growth factor‐II." BioFactors 46, no. 4 (February 6, 2020): 563–78. http://dx.doi.org/10.1002/biof.1623.

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41

Bach, L. A., S. Hsieh, K. Sakano, H. Fujiwara, J. F. Perdue, and M. M. Rechler. "Binding of mutants of human insulin-like growth factor II to insulin-like growth factor binding proteins 1-6." Journal of Biological Chemistry 268, no. 13 (May 1993): 9246–54. http://dx.doi.org/10.1016/s0021-9258(18)98342-0.

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42

Rosenfeld, R. G., C. A. Conover, D. Hodges, P. D. K. Lee, P. Misra, R. L. Hintz, and C. H. Li. "Heterogeneity of insulin-like growth factor-I affinity for the insulin-like growth factor-II receptor: Comparison of natural, synthetic and recombinant DNA-derived insulin-like growth factor-I." Biochemical and Biophysical Research Communications 143, no. 1 (February 1987): 199–205. http://dx.doi.org/10.1016/0006-291x(87)90650-4.

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43

Beguinot, F., C. R. Kahn, A. C. Moses, and R. J. Smith. "Distinct biologically active receptors for insulin, insulin-like growth factor I, and insulin-like growth factor II in cultured skeletal muscle cells." Journal of Biological Chemistry 260, no. 29 (December 1985): 15892–98. http://dx.doi.org/10.1016/s0021-9258(17)36342-1.

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44

Ogino, Shuji, Shigeki Kubo, Fadi W. Abdul-Karim, and Mark L. Cohen. "Comparative Immunohistochemical Study of Insulin-like Growth Factor II and Insulin-like Growth Factor Receptor Type 1 in Pediatric Brain Tumors." Pediatric and Developmental Pathology 4, no. 1 (January 2001): 23–31. http://dx.doi.org/10.1007/s100240010112.

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Insulin-like growth factor (IGF)-II is an important growth factor in development of the central nervous system. The purpose of this study was to evaluate expression of IGF-II and IGF receptor type 1 (IGFR1) in various pediatric brain tumors. Immunohistochemistry for IGF-II and IGFR1 was performed on 15 choroid plexus papillomas (CPPs) including 1 atypical CPP, 2 choroid plexus carcinomas (CPCs), 5 anaplastic ependymomas, 7 nonanaplastic ependymomas (simply referred to as “ependymoma”), 5 medulloblastomas, 1 cerebral neuroblastoma, and 1 atypical teratoid/rhabdoid tumor (ATRT) along with 10 non-neoplastic choroid plexus and 3 non-neoplastic ependymal linings. All non-neoplastic choroid plexus, CPPs, CPCs, anaplastic ependymomas, ATRT, 71% of ependymomas, and 67% of non-neoplastic ependymal linings showed cytoplasmic positivity for IGF-II, whereas all medulloblastomas and the cerebral neuroblastoma were negative for IGF-II. In addition to cytoplasmic positivity for IGFR1, membranous positivity was observed in 73% of CPPs, both CPCs, the ATRT, 22% of non-neoplastic choroid plexus, 80% of anaplastic ependymomas, and 29% of ependymomas, but not in any medulloblastoma, cerebral neuroblastoma, or non-neoplastic ependymal lining. IGF-II and IGFR1 may play roles in the pathogeneses of CPP, CPC, anaplastic ependymoma, ependymoma, and ATRT. Immunohistochemical testing for IGF-II and IGFR1 may be useful in differentiating ATRT, CPC, and anaplastic ependymoma from medulloblastoma and cerebral neuroblastoma.

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KIESS, Wieland, Cheryl L. THOMAS, Mark M. SKLAR, and S. Peter NISSLEY. "beta-Galactosidase decreases the binding affinity of the insulin-like-growth-factor-II/mannose-6-phosphate receptor for insulin-like-growth-factor II." European Journal of Biochemistry 190, no. 1 (May 1990): 71–77. http://dx.doi.org/10.1111/j.1432-1033.1990.tb15547.x.

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Morrione, A., B. Valentinis, S. q. Xu, G. Yumet, A. Louvi, A. Efstratiadis, and R. Baserga. "Insulin-like growth factor II stimulates cell proliferation through the insulin receptor." Proceedings of the National Academy of Sciences 94, no. 8 (April 15, 1997): 3777–82. http://dx.doi.org/10.1073/pnas.94.8.3777.

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Norstedt, Gunnar, Agneta Levinovitz, and Håkan Eriksson. "Regulation of uterine insulin-like growth factor I mRNA and insulin-like growth factor II mRNA by estrogen in the rat." Acta Endocrinologica 120, no. 4 (April 1989): 466–72. http://dx.doi.org/10.1530/acta.0.1200466.

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Abstract. IGF-I and IGF-II are peptides with mitogenic properties. In this study mRNA for IGF-I and IGF-II was analysed in rat uterine tissue after different endocrine manipulations and the possibility of an estrogenic regulation of IGF expression was investigated. Both IGF-I and IGF-II mRNA were present in uterine tissue. The level of IGF-I mRNA, but not IGF-II mRNA, was reduced following ovariectomy. Administration of estradiol (2.5 μg/day for 4 days) to ovariectomized rats increased IGF-I mRNA 8-fold to levels seen in intact animals. In adult animals hepatic IGF-I mRNA did not appear to be increased by estrogen treatment. Low levels of IGF-II mRNA were detected in the uterus, but showed no dependence on estrogen. The inductive effect of estrogen on uterine IGF-I mRNA could not be substituted for by growth hormone administration (0.5 mg/100 g, ip for 6 h). The present results suggest IGF-I as a potential candidate for a mediator of estrogen-induced growth. Both estrogen and GH induce IGF-I mRNA and a tissue specificity for these hormones is indicated where GH regulates hepatic and estrogen uterine IGF-I mRNA.

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Giudice, Linda C., Natalie A. Martina, Ruth Ann Crystal, Salli Tazuke, and Maurice Druzin. "Insulin-like growth factor binding protein-1 at the maternal-fetal interface and insulin-like growth factor-I, insulin-like growth factor-II, and insulin-like growth factor binding protein-1 in the circulation of women with severe preeclampsia." American Journal of Obstetrics and Gynecology 176, no. 4 (April 1997): 751–58. http://dx.doi.org/10.1016/s0002-9378(97)70598-2.

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Lund, P. K., B. M. Moats-Staats, M. A. Hynes, J. G. Simmons, M. Jansen, A. J. D'Ercole, and J. J. Van Wyk. "Somatomedin-C/insulin-like growth factor-I and insulin-like growth factor-II mRNAs in rat fetal and adult tissues." Journal of Biological Chemistry 261, no. 31 (November 1986): 14539–44. http://dx.doi.org/10.1016/s0021-9258(18)66903-0.

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Slipicevic, Ana, Geir Frode Øy, Inger Cecilie Askildt, Arild Holth, Ellen Hellesylt, Vivi Ann Flørenes, and Ben Davidson. "Diagnostic and prognostic role of the insulin growth factor pathway members insulin-like growth factor-II and insulin-like growth factor binding protein-3 in serous effusions." Human Pathology 40, no. 4 (April 2009): 527–37. http://dx.doi.org/10.1016/j.humpath.2008.10.003.

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