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Articoli di riviste sul tema "Insulin-like growth factor I Physiology"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 28 gennaio 2023

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1

Holly, Jeff M. P., and Claire M. Perks. "Insulin-Like Growth Factor Physiology." Endocrinology and Metabolism Clinics of North America 41, no. 2 (June 2012): 249–63. http://dx.doi.org/10.1016/j.ecl.2012.04.009.

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2

Yakar, Shoshana, and Martin L. Adamo. "Insulin-Like Growth Factor 1 Physiology." Endocrinology and Metabolism Clinics of North America 41, no. 2 (June 2012): 231–47. http://dx.doi.org/10.1016/j.ecl.2012.04.008.

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3

Rosen, Clifford J. "Serum Insulin-like Growth Factors and Insulin-like Growth Factor-binding Proteins: Clinical Implications." Clinical Chemistry 45, no. 8 (August 1, 1999): 1384–90. http://dx.doi.org/10.1093/clinchem/45.8.1384.

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Abstract (sommario):

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 meas

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4

Pollak, Michael. "Insulin-like growth factor physiology and neoplasia." Growth Hormone & IGF Research 10 (January 2000): S6—S7. http://dx.doi.org/10.1016/s1096-6374(00)90002-9.

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5

Holly, Jeff M. P., Claire M. Perks, and Claire E. H. Stewart. "Overview of insulin-like growth factor physiology." Growth Hormone & IGF Research 10 (January 2000): S8—S9. http://dx.doi.org/10.1016/s1096-6374(00)90003-0.

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6

Roith, Derek Le. "The Insulin-Like Growth Factor System." Experimental Diabesity Research 4, no. 4 (2003): 205–12. http://dx.doi.org/10.1155/edr.2003.205.

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Abstract (sommario):

The insulin-like growth factor (IGF) system in ubiquitous and plays a role in every tissue of the body. It is comprised of ligands, receptors and binding proteins, each with specific functions. While it plays an essential role in embryonic and post-natal development, the IGF system is also important in normal adult physiology. There are now numerous examples of diseases such as diabetes, cancer, and malnutrition in which the IGF system is a major player and, not surprisingly, there are attempts to affect these disorders by manipulating the system.

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7

Pollak, M. "Insulin-like growth factor physiology and cancer risk." European Journal of Cancer 36, no. 10 (June 2000): 1224–28. http://dx.doi.org/10.1016/s0959-8049(00)00102-7.

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8

Gabbitas, Bari, and 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, no. 2 (August 1, 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

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9

Sheppard, M. S., and R. M. Bala. "Insulin-like growth factor inhibition of growth hormone secretion." Canadian Journal of Physiology and Pharmacology 64, no. 5 (May 1, 1986): 525–30. http://dx.doi.org/10.1139/y86-087.

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Somatomedins – insulin-like growth factors (SM/IGF) are growth hormone (GH) dependent serum growth factors. There is some evidence that IGF inhibit GH release (negative feedback) in 3- to 24-h incubations of cultured rat adenohypophysial cells. We have used acutely dispersed noncultured rat adenohypophysial cells to study the dynamics of IGF on GH secretion. In this system both IGF-I and IGF-II (100 ng/mL) slightly, but significantly, decrease the cumulative GH released by human pancreas growth hormone releasing factor 1–40 (GRF) and the phosphodiesterase inhibitor 3-isobutyl-1-methyl xanthine

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10

Sowers, James R. "Insulin and Insulin-Like Growth Factor in Normal and Pathological Cardiovascular Physiology." Hypertension 29, no. 3 (March 1997): 691–99. http://dx.doi.org/10.1161/01.hyp.29.3.691.

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11

Yoshimura, Yasunori. "Insulin-like Growth Factors and Ovarian Physiology." Journal of Obstetrics and Gynaecology Research 24, no. 5 (October 1998): 305–23. http://dx.doi.org/10.1111/j.1447-0756.1998.tb00103.x.

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12

Herington, Adrian C. "Insulin-like growth factors: biochemistry and physiology." Baillière's Clinical Endocrinology and Metabolism 5, no. 4 (December 1991): 531–51. http://dx.doi.org/10.1016/s0950-351x(10)80002-3.

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13

Yip, Cecil C., Helga Hsu, Jerrold M. Olefsky, and Lynn Seely. "Preparation of insulin-like growth factor I and photoaffinity labeling of insulin-like growth factor I receptor." Peptides 14, no. 2 (March 1993): 325–30. http://dx.doi.org/10.1016/0196-9781(93)90048-l.

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14

Hammerman, M. R. "The growth hormone-insulin-like growth factor axis in kidney." American Journal of Physiology-Renal Physiology 257, no. 4 (October 1, 1989): F503—F514. http://dx.doi.org/10.1152/ajprenal.1989.257.4.f503.

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Abstract (sommario):

Growth hormone (GH) exerts a variety of metabolic and anabolic effects on skeletal and soft tissues including kidney. Some of these actions are mediated directly, whereas others result from GH-dependent synthesis and release of polypeptide growth factors designated insulin-like growth factors (IGFs). Receptors for GH are present in proximal tubule and GH directly stimulates gluconeogenesis at this site. IGF receptors are found in glomerulus and proximal tubule. Mechanisms for signal transduction by GH and IGFs have been characterized using proximal tubular basolateral membranes. IGFs regulate

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15

Ashton, Nick. "Insulin-like growth factor, nephrogenesis and hypertension." Journal of Hypertension 24, no. 9 (September 2006): 1707–9. http://dx.doi.org/10.1097/01.hjh.0000242392.22720.e0.

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16

Roberts, CT,, and D. LeRoith. "Interactions in the Insulin-Like Growth Factor Signaling System." Physiology 7, no. 2 (April 1, 1992): 69–72. http://dx.doi.org/10.1152/physiologyonline.1992.7.2.69.

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Abstract (sommario):

The insulin-like growth factors, IGF-I and IGF-II, are mitogenic peptides structurally related to insulin, which have widespread effects on growth and differentiation during development. These effects are mediated via activation of specific cell-surface receptors, and this activation is modulated by several species of IGF-binding proteins.

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17

Boni-Schnetzler, M., C. Schmid, P. J. Meier, and E. R. Froesch. "Insulin regulates insulin-like growth factor I mRNA in rat hepatocytes." American Journal of Physiology-Endocrinology and Metabolism 260, no. 6 (June 1, 1991): E846—E851. http://dx.doi.org/10.1152/ajpendo.1991.260.6.e846.

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To evaluate the regulatory role of growth hormone (GH) and insulin on insulin-like growth factor I (IGF-I) mRNA levels, we employed primary rat hepatocytes. Cells were incubated for 16 h with 10 nM insulin, 10 nM GH, or a combination thereof, and IGF-I mRNA levels were analyzed by Northern blotting. Insulin results in 2.5-fold and GH in 3.8-fold higher IGF-I mRNA levels than hormone-free controls, and a combination of insulin and GH had an additive effect (6.7-fold). The effect of 10 nM insulin was constant at variable GH concentrations. Therefore, GH and insulin affect IGF-I mRNA levels indep

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18

Fryburg, D. A. "Insulin-like growth factor I exerts growth hormone- and insulin-like actions on human muscle protein metabolism." American Journal of Physiology-Endocrinology and Metabolism 267, no. 2 (August 1, 1994): E331—E336. http://dx.doi.org/10.1152/ajpendo.1994.267.2.e331.

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The effect of a 6-h intra-arterial infusion of recombinant human (rh) insulin-like growth factor I (IGF-I) on forearm muscle metabolism was studied in 19 postabsorptive subjects. Forearm glucose, lactate, and phenylalanine (Phe) balances, as well as estimates of protein degradation (Phe Ra) and synthesis (Phe Rd) were measured before and at 3 and 6 h into an infusion of rhIGF-I at a dose of 1.8 (n = 6), 6.0 (n = 8), or 10.0 (n = 5) micrograms.kg-1.h-1. In response to intra-arterial IGF-I, deep venous IGF-I rose by 55, 141, and 315%, respectively (all P < 0.01), and forearm blood flow accele

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19

Hussain, MA, O. Schmitz, and ER Froesch. "Growth Hormone, Insulin, and Insulin-Like Growth Factor I: Revisiting the Food and Famine Theory." Physiology 10, no. 2 (April 1, 1995): 81–86. http://dx.doi.org/10.1152/physiologyonline.1995.10.2.81.

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In the so-called "food and famine theory," insulin and growth hormone play major roles in the regulation of substrate combustion during the postprandial period as well as in the fasting state. Insulin-like growth factor I supports the actions of both insulin and growth hormone.

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20

Hammerman, M. R., and S. B. Miller. "The growth hormone insulin-like growth factor axis in kidney revisited." American Journal of Physiology-Renal Physiology 265, no. 1 (July 1, 1993): F1—F14. http://dx.doi.org/10.1152/ajprenal.1993.265.1.f1.

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Abstract (sommario):

Studies characterizing actions of growth hormone (GH) and insulin-like growth factors (IGF) in kidneys of adult and developing animals and humans have provided a good deal of insight into the functions of these peptides. Although certain of the actions may be mediated directly by GH, most appear to result from effects of GH to increase levels of circulating IGF or IGF produced in kidney. In addition to GH, epidermal growth factor (EGF) enhances the renal synthesis of IGF-I. Enhancement of renal IGF-I expression is GH independent in compensatory hypertrophy. Stimulation of kidney IGF-I producti

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21

Röttgering, Bas T., and Karoly Szuhai. "Insulin-Like Growth Factor 2 in Physiology, Cancer, and Cancer Treatment." OBM Genetics 3, no. 4 (May 14, 2019): 1. http://dx.doi.org/10.21926/obm.genet.1904096.

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22

Froesch, E. Rudolf, Mehboob A. Hussain, Christoph Schmid, and Jürgen Zapf. "Insulin-like Growth Factor I: Physiology, Metabolic Effects and Clinical Uses." Diabetes / Metabolism Reviews 12, no. 3 (October 1996): 195–215. http://dx.doi.org/10.1002/(sici)1099-0895(199610)12:3<195::aid-dmr164>3.0.co;2-g.

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23

Franklin, S. C., M. Moulton, G. A. Sicard, M. R. Hammerman, and S. B. Miller. "Insulin-like growth factor I preserves renal function postoperatively." American Journal of Physiology-Renal Physiology 272, no. 2 (February 1, 1997): F257—F259. http://dx.doi.org/10.1152/ajprenal.1997.272.2.f257.

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Deterioration of renal function, which can lead to postoperative renal failure, is a complication of surgery involving the suprarenal aorta and surgery involving the renal arteries. Fifty-four patients who were at risk for developing this complication were enrolled in a double-blind, randomized, placebo-controlled trial of insulin-like growth factor (IGF-I) as a therapeutic agent to prevent the decline in renal function. The primary end point was the incidence of renal dysfunction, defined as a reduction of the glomerular filtration rate (creatinine clearance) at each of three measurements ove

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24

Miller, S. C., та C. M. Bagi. "Systemic effects of transforming growth factor-β and insulin-like growth factor". Bone 19, № 3 (вересень 1996): 153. http://dx.doi.org/10.1016/s8756-3282(96)90821-2.

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25

Thabet, M. A., A. Challa, W. Chan, F. Liu, R. L. Hintz, and J. C. Chan. "Insulin-like growth factor and growth hormone receptor in nephrotic rats." American Journal of Physiology-Endocrinology and Metabolism 266, no. 1 (January 1, 1994): E102—E106. http://dx.doi.org/10.1152/ajpendo.1994.266.1.e102.

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In an attempt to elucidate the mechanism of growth retardation in the nephrotic syndrome, specific serum and hepatic growth factors were measured in Sprague-Dawley rats in which nephrotic syndrome was produced by administration of puromycin (1.5 mg.100 g body wt-1.day-1) for 12 days. On the 13th day, the results of these nephrotic animals were compared with those of an equal number of pair-fed and control animals: the mean dietary intake of the nephrotic group was 71% that of the control group (P < 0.001). Serum insulin-like growth factor (IGF) binding protein-3 was significantly reduced (P

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26

Conover, Cheryl A. "Insulin-like growth factor-binding proteins and bone metabolism." American Journal of Physiology-Endocrinology and Metabolism 294, no. 1 (January 2008): E10—E14. http://dx.doi.org/10.1152/ajpendo.00648.2007.

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Insulin-like growth factor-binding proteins (IGFBPs) are important regulators of bone metabolism. However, their precise roles are not fully understood, since IGFBPs can have both enhancing and inhibiting effects on IGF action, depending on context and posttranslational modifications, as well as IGF-independent effects. This review focuses on recent findings from cell culture, rodent models, and clinical studies concerning local IGFBP-2, IGFBP-4, and IGFBP-5 action in bone.

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27

Mukherjee, Aditi, Damir Alzhanov, and Peter Rotwein. "Defining human insulin-like growth factor I gene regulation." American Journal of Physiology-Endocrinology and Metabolism 311, no. 2 (August 1, 2016): E519—E529. http://dx.doi.org/10.1152/ajpendo.00212.2016.

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Abstract (sommario):

Growth hormone (GH) plays an essential role in controlling somatic growth and in regulating multiple physiological processes in humans and other species. Insulin-like growth factor I (IGF-I), a conserved, secreted 70-amino acid peptide, is a critical mediator of many of the biological effects of GH. Previous studies have demonstrated that GH rapidly and potently promotes IGF-I gene expression in rodents and in some other mammals through the transcription factor STAT5b, leading to accumulation of IGF-I mRNAs and production of IGF-I. Despite this progress, very little is known about how GH or ot

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28

Eliakim, Alon, Youngman Oh, and Dan Michael Cooper. "Effect of single wrist exercise on fibroblast growth factor-2, insulin-like growth factor, and growth hormone." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 279, no. 2 (August 1, 2000): R548—R553. http://dx.doi.org/10.1152/ajpregu.2000.279.2.r548.

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Anabolic effects of exercise are mediated, in part, by fibroblast growth factor-2 (FGF-2), insulin-like growth factor-I (IGF-I), and growth hormone (GH). To identify local vs. systemic modification of these mediators, 10 male subjects performed 10 min of unilateral wrist-flexion exercise. Blood was sampled from catheters placed in basilic veins of both arms. Lactate was significantly increased only in the exercising arm. FGF-2 decreased dramatically ( P < 0.01) in both the resting (from 1.49 ± 0.32 to nadir at 0.11 ± 0.11 pg/ml) and exercising arm (1.80 ± 0.60 to 0.29 ± 0.14 pg/ml). Small b

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29

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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30

Butler, Andrew A., Shoshana Yakar, and Derek LeRoith. "Insulin-Like Growth Factor-I: Compartmentalization Within the Somatotropic Axis?" Physiology 17, no. 2 (April 2002): 82–85. http://dx.doi.org/10.1152/nips.01351.2001.

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Insulin-like growth factor-I (IGF-I) is essential for normal growth; igf-1 gene mutations are associated with extreme growth retardation in mice and, very rarely, in humans. The relative contributions of tissue vs. endocrine (hepatic) IGF-I to the regulation of growth has been a fundamental question. New gene targeting technologies are providing answers for these questions.

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31

Bach, Leon A., Ping Fu, and Zhiyong Yang. "Insulin-like growth factor-binding protein-6 and cancer." Clinical Science 124, no. 4 (October 31, 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 physio

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32

Bosche, William J., Daina Z. Ewton, and James R. Florini. "Transforming growth factor-beta isoform expression in insulin-like growth factor stimulated myogenesis." Journal of Cellular Physiology 164, no. 2 (August 1995): 324–33. http://dx.doi.org/10.1002/jcp.1041640213.

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33

Belfiore, Antonino, Francesco Frasca, Giuseppe Pandini, Laura Sciacca, and Riccardo Vigneri. "Insulin Receptor Isoforms and Insulin Receptor/Insulin-Like Growth Factor Receptor Hybrids in Physiology and Disease." Endocrine Reviews 30, no. 6 (October 1, 2009): 586–623. http://dx.doi.org/10.1210/er.2008-0047.

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34

Friedrich, Nele, Torben Jørgensen, Henri Wallaschofski, and Allan Linneberg. "911 THE EFFECT OF INSULIN-LIKE GROWTH FACTOR 1 AND INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN 3 ON BLOOD PRESSURE." Journal of Hypertension 30 (September 2012): e263. http://dx.doi.org/10.1097/01.hjh.0000420853.64612.b5.

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35

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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36

Park, Jung H. Y., Mark R. Corkins, Jon A. Vanderhoof, Nia M. Caruso, Marjorie J. Hrbek, Beverly S. Schaffer, Dorothy H. Slentz, Robert H. McCusker, and Richard G. MacDonald. "Expression of insulin-like growth factor-II and insulin-like growth factor binding proteins during Caco-2 cell proliferation and differentiation." Journal of Cellular Physiology 166, no. 2 (February 1996): 396–406. http://dx.doi.org/10.1002/(sici)1097-4652(199602)166:2<396::aid-jcp18>3.0.co;2-9.

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Werner, Haim, and Ilan Bruchim. "The insulin-like growth factor-I receptor as an oncogene." Archives of Physiology and Biochemistry 115, no. 2 (May 2009): 58–71. http://dx.doi.org/10.1080/13813450902783106.

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38

Karadag, A. S., D. T. Ertugrul, E. Tutal, and K. O. Akin. "Short-term isotretinoin treatment decreases insulin-like growth factor-1 and insulin-like growth factor binding protein-3 levels: does isotretinoin affect growth hormone physiology?" British Journal of Dermatology 162, no. 4 (February 1, 2010): 798–802. http://dx.doi.org/10.1111/j.1365-2133.2009.09618.x.

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39

Higashi, Yusuke, Sergiy Sukhanov, Sampath Parthasarathy, and Patrice Delafontaine. "The ubiquitin ligase Nedd4 mediates oxidized low-density lipoprotein-induced downregulation of insulin-like growth factor-1 receptor." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 4 (October 2008): H1684—H1689. http://dx.doi.org/10.1152/ajpheart.00548.2008.

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Oxidized low-density lipoprotein (LDL) is proatherogenic and induces smooth muscle cell apoptosis, which contributes to atherosclerotic plaque destabilization. We showed previously that oxidized LDL downregulates insulin-like growth factor-1 receptor in human smooth muscle cells and that this is critical for induction of apoptosis. To identify mechanisms, we exposed smooth muscle cells to 60 μg/ml oxidized LDL or native LDL and assessed insulin-like growth factor-1 receptor mRNA levels, protein synthesis rate, and receptor protein stability. Oxidized LDL decreased insulin-like growth factor-1

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Han, Ho Jae, Chang Won Kang, and Soo Hyun Park. "TISSUE-SPECIFIC REGULATION OF INSULIN-LIKE GROWTH FACTORS AND INSULIN-LIKE GROWTH FACTOR BINDING PROTEINS IN MALE DIABETIC RATS IN VIVO AND IN VITRO." Clinical and Experimental Pharmacology and Physiology 33, no. 12 (December 2006): 1172–79. http://dx.doi.org/10.1111/j.1440-1681.2006.04495.x.

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Hayakawa, Tetsuo, Takaharu Kondo, Tokimune Shibata, Motoji Kitagawa, Hideki Ono, Yuzo Sakai, Katsumoto Kato, et al. "Serum insulin-like growth factor II in chronic liver disease." Digestive Diseases and Sciences 34, no. 3 (March 1989): 338–42. http://dx.doi.org/10.1007/bf01536252.

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42

Olanrewaju, Hammed A., Eric D. Sanzenbacher, and Edward R. Seidel. "Insulin-like growth factor I in suckling rat gastric contents." Digestive Diseases and Sciences 41, no. 7 (July 1996): 1392–97. http://dx.doi.org/10.1007/bf02088564.

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43

Cappon, J., J. A. Brasel, S. Mohan, and D. M. Cooper. "Effect of brief exercise on circulating insulin-like growth factor I." Journal of Applied Physiology 76, no. 6 (June 1, 1994): 2490–96. http://dx.doi.org/10.1152/jappl.1994.76.6.2490.

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Abstract (sommario):

An acute insulin-like growth factor I (IGF-I) response to 10 min of above-lactate threshold cycle ergometer exercise was studied in 10 subjects (age 22–35 yr). Each subject exercised on three separate mornings after ingesting one of two isocaloric isovolemic liquid meals high in either fat or glucose or an isovolemic noncaloric placebo. The high-fat meal attenuated the growth hormone (GH) response (Cappon et al., J. Clin. Endocrinol. Metab. 76: 1418–1422, 1993). In contrast, IGF-I increased equally for all protocols [e.g., after the placebo meal IGF-I increased from 21,716 (SE) ng/ml preexerci

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Muhammad, Tahir, Mengjing Li, Jianfeng Wang, Tao Huang, Shigang Zhao, Han Zhao, Hongbin Liu, and Zi-Jiang Chen. "Roles of insulin-like growth factor II in regulating female reproductive physiology." Science China Life Sciences 63, no. 6 (April 10, 2020): 849–65. http://dx.doi.org/10.1007/s11427-019-1646-y.

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Haus, Erhard, E. Haus, L. Dumitriu, G. Y. Nicolau, S. Bologa, and L. Sackett-Lundeen. "CIRCADIAN RHYTHMS OF BASIC FIBROBLAST GROWTH FACTOR (bFGF), EPIDERMAL GROWTH FACTOR (EGF), INSULIN-LIKE GROWTH FACTOR-1 (IGF-1), INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN-3 (IGFBP-3), CORTISOL, AND MELATONIN IN WOMEN WITH BREAST CANCER." Chronobiology International 18, no. 4 (January 2001): 709–27. http://dx.doi.org/10.1081/cbi-100106083.

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46

Salehi, Zivar, Farhad Mashayekhi, Mohammad Naji, and Sareh Pandamooz. "Insulin-like growth factor-1 and insulin-like growth factor binding proteins in cerebrospinal fluid during the development of mouse embryos." Journal of Clinical Neuroscience 16, no. 7 (July 2009): 950–53. http://dx.doi.org/10.1016/j.jocn.2008.09.018.

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47

GAUSSIN, V., and C. DEPRE. "Myostatin, the cardiac chalone of insulin-like growth factor-1." Cardiovascular Research 68, no. 3 (December 1, 2005): 347–49. http://dx.doi.org/10.1016/j.cardiores.2005.09.007.

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Radosavljevic, Tatjana, Vera Todorovic, Danijela Vucevic, and Branka Sikic. "The growth hormone axis and insulin-like growth factors." Medical review 58, no. 11-12 (2005): 558–62. http://dx.doi.org/10.2298/mpns0512558r.

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Abstract (sommario):

Introduction Growth is regulated by the interaction of environmental signals with endogenous neuroendocrine responses to the genetic programs that determine the body plan. The insulin-like growth factors (IGFs) are integral components of multiple systems controlling both growth and metabolism. The IGF system The IGF system is thought to be more complex than other endocrine systems, as genes for six IGF-binding proteins (IGFBPs) have been identified so far. The IGFs play a critical role in both cell cycle control and apoptosis, two functions involved in regulation of tumorigenesis. Insulin-like

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Vardy, Daniel A., Csaba Kari, Gerald S. Lazarus, Pamela J. Jensen, Asher Zilberstein, Gregory D. Plowman, and Ulrich Rodeck. "Induction of autocrine epidermal growth factor receptor ligands in human keratinocytes by insulin/insulin-like growth factor-1." Journal of Cellular Physiology 163, no. 2 (May 1995): 257–65. http://dx.doi.org/10.1002/jcp.1041630206.

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Leibush, B., M. Párrizas, I. Navarro, Y. Lappova, M. A. Maestro, M. Encinas, E. M. Plisetskaya, and J. Gutiérrez. "Insulin and insulin-like growth factor-I receptors in fish brain." Regulatory Peptides 61, no. 2 (February 1996): 155–61. http://dx.doi.org/10.1016/0167-0115(95)00154-9.

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