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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., e Claire M. Perks. "Insulin-Like Growth Factor Physiology". Endocrinology and Metabolism Clinics of North America 41, n. 2 (giugno 2012): 249–63. http://dx.doi.org/10.1016/j.ecl.2012.04.009.

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2

Yakar, Shoshana, e Martin L. Adamo. "Insulin-Like Growth Factor 1 Physiology". Endocrinology and Metabolism Clinics of North America 41, n. 2 (giugno 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, n. 8 (1 agosto 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 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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4

Pollak, Michael. "Insulin-like growth factor physiology and neoplasia". Growth Hormone & IGF Research 10 (gennaio 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 e Claire E. H. Stewart. "Overview of insulin-like growth factor physiology". Growth Hormone & IGF Research 10 (gennaio 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, n. 4 (2003): 205–12. http://dx.doi.org/10.1155/edr.2003.205.

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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, n. 10 (giugno 2000): 1224–28. http://dx.doi.org/10.1016/s0959-8049(00)00102-7.

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8

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. 2 (1 agosto 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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9

Sheppard, M. S., e R. M. Bala. "Insulin-like growth factor inhibition of growth hormone secretion". Canadian Journal of Physiology and Pharmacology 64, n. 5 (1 maggio 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. The inhibition is small (16%) and usually not statistically significant until 2 h of incubation. The inhibition with IGF is additive to that produced with low concentrations of somatostatin. The IGF also sigificantly decrease the rate of GH release in all time periods tested (0–1, 1–2, 2–3 h). In addition, the IGF decrease the quantity of [14C]leucine protein eluted at the position of labelled rat GH on Sephadex G75, which would include newly synthesized GH extracted from the cells. Thus we conclude that the decreased GH released may be due to an effect of IGF on both rate of release and on GH synthesis.

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10

Sowers, James R. "Insulin and Insulin-Like Growth Factor in Normal and Pathological Cardiovascular Physiology". Hypertension 29, n. 3 (marzo 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, n. 5 (ottobre 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, n. 4 (dicembre 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 e Lynn Seely. "Preparation of insulin-like growth factor I and photoaffinity labeling of insulin-like growth factor I receptor". Peptides 14, n. 2 (marzo 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, n. 4 (1 ottobre 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 metabolic and transport processes in cultured glomerular mesangial cells and in isolated proximal tubular cells. IGF I is synthesized in cultured mesangial cells and is produced in a GH-dependent manner in cortical and medullary collecting duct. Evidence has accumulated that IGF I of renal origin functions as a paracrine growth factor in the settings of GH-induced hypertrophy and compensatory hypertrophy of the kidney, and in the setting of proximal tubular regeneration following ischemic injury. IGFs are embryonal mitogens and IGF II may act as a transforming agent for Wilms' tumor. Further characterization of the GH-IGF axis in kidney will provide additional insights into the roles of these peptides as regulators of renal function, growth, and development.

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15

Ashton, Nick. "Insulin-like growth factor, nephrogenesis and hypertension". Journal of Hypertension 24, n. 9 (settembre 2006): 1707–9. http://dx.doi.org/10.1097/01.hjh.0000242392.22720.e0.

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16

Roberts, CT,, e D. LeRoith. "Interactions in the Insulin-Like Growth Factor Signaling System". Physiology 7, n. 2 (1 aprile 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 e E. R. Froesch. "Insulin regulates insulin-like growth factor I mRNA in rat hepatocytes". American Journal of Physiology-Endocrinology and Metabolism 260, n. 6 (1 giugno 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 independently of each other. The half-maximal effective dose of insulin was 4.7 X 10(-10) M, and, in kinetic experiments, insulin was effective within 2 h. These findings demonstrate that insulin modulates hepatic IGF-I production by a direct regulation of the transcript levels of IGF-I.

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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, n. 2 (1 agosto 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 accelerated by 75 (1.8 microgram), 213 (6.0 micrograms), and 159% (10.0 micrograms; all P < 0.02). No change in forearm glucose uptake was observed at the lowest dose, whereas four- to sixfold increases were observed at both the 6 and 10 micrograms.kg-1.h-1 doses (both P < 0.02). Forearm Phe balance shifted positively at all three doses by 27 +/- 6, 48 +/- 7, and 51 +/- 9 nmol.min-1 x 100 ml-1, respectively (all P < 0.01). At all three doses, Phe Rd increased comparably by 49-74% (all P < 0.05). At the 6.0 and 10.0 but not the 1.8 microgram.kg-1.h-1 dose, Phe Ra decreased by approximately 45% (P < 0.02). Forearm muscle metabolism was also studied in the contralateral non-IGF-infused arm at these three doses. Despite increases in deep venous IGF-I up to 517 ng/ml due to recirculating IGF-I (10.0 micrograms.kg-1.h-1 dose), contralateral forearm muscle glucose, lactate, or Phe handling did not change. In conclusion, intra-arterial IGF-I exhibits growth hormone-like effects at all doses tested, whereas the insulin-like effects are observed at higher doses; these effects appear dependent on the route of administration.

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19

Hussain, MA, O. Schmitz e ER Froesch. "Growth Hormone, Insulin, and Insulin-Like Growth Factor I: Revisiting the Food and Famine Theory". Physiology 10, n. 2 (1 aprile 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., e S. B. Miller. "The growth hormone insulin-like growth factor axis in kidney revisited". American Journal of Physiology-Renal Physiology 265, n. 1 (1 luglio 1993): F1—F14. http://dx.doi.org/10.1152/ajprenal.1993.265.1.f1.

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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 production also occurs in diabetes mellitus. Renal IGF-I production is elevated in these settings in the absence of changes in circulating IGF-I, consistent with a causative role of renal IGF-I for the accompanying increased glomerular filtration rate and kidney growth. Actions of IGF in kidney are initiated following binding of peptides to specific receptors. Receptor number may be altered during compensatory growth and in diabetes mellitus. In addition to IGF, several IGF binding proteins (IGFBP) are produced in kidney and are likely to both inhibit and enhance the actions of IGF in different circumstances through sequestration of peptides and regulation of peptide interactions with their receptors. Administration of IGF-I to rats following acute ischemic injury hastens the recovery of normal renal function and accelerates the regeneration of the damaged proximal tubular epithelium. IGF-I increases the glomerular filtration rate in humans with normal and reduced functional kidney mass. These findings establish the potential for use of this peptide as a therapeutic agent in the settings of acute and chronic renal failure.

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21

Röttgering, Bas T., e Karoly Szuhai. "Insulin-Like Growth Factor 2 in Physiology, Cancer, and Cancer Treatment". OBM Genetics 3, n. 4 (14 maggio 2019): 1. http://dx.doi.org/10.21926/obm.genet.1904096.

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22

Froesch, E. Rudolf, Mehboob A. Hussain, Christoph Schmid e Jürgen Zapf. "Insulin-like Growth Factor I: Physiology, Metabolic Effects and Clinical Uses". Diabetes / Metabolism Reviews 12, n. 3 (ottobre 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 e S. B. Miller. "Insulin-like growth factor I preserves renal function postoperatively". American Journal of Physiology-Renal Physiology 272, n. 2 (1 febbraio 1997): F257—F259. http://dx.doi.org/10.1152/ajprenal.1997.272.2.f257.

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Abstract (sommario):

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 over 72 h. IGF-I (100 microg/kg subcutaneously every 12 h for 6 doses) or placebo was administered on admission to the intensive care unit immediately postoperatively. IGF-I- and placebo-treated groups were well matched for sex, age, type of surgery, renal ischemic time during surgery (ischemic index), baseline creatinine clearance, and baseline serum creatinine. No patient in the study developed acute renal failure postoperatively. IGF-I was well tolerated. A smaller proportion of patients in the IGF-I group had a postoperative decline in renal function (22%) than in the placebo-treated group (33%). There were no significant differences in levels of serum creatinine at time of discharge, length of hospital stay, length of intensive care unit stay, length of intubation, or incidence of dialysis or death. Our findings establish the feasibility and potential utility for the use of IGF-I to reduce the incidence of postoperative renal dysfunction in high-risk patients.

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24

Miller, S. C., e C. M. Bagi. "Systemic effects of transforming growth factor-β and insulin-like growth factor". Bone 19, n. 3 (settembre 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 e J. C. Chan. "Insulin-like growth factor and growth hormone receptor in nephrotic rats". American Journal of Physiology-Endocrinology and Metabolism 266, n. 1 (1 gennaio 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 < 0.005) in the nephrotic rats, compared with the pair-fed and the control groups. Hepatic IGF-I mRNA in the nephrotic rats averaged 36% that of control (P < 0.001) and 46% that of the pair-fed animals (P < 0.001). Hepatic growth hormone receptor (GHr) mRNA in the nephrotic rats averaged 19% of that of the control (P < 0.001) and 27% of that of the pair-fed rats (P < 0.001). These results indicate that the growth retardation of the nephrotic rats may be associated with the significant decrease in IGF-I mRNA and reduction in GHr mRNA.

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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, n. 1 (gennaio 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 e Peter Rotwein. "Defining human insulin-like growth factor I gene regulation". American Journal of Physiology-Endocrinology and Metabolism 311, n. 2 (1 agosto 2016): E519—E529. http://dx.doi.org/10.1152/ajpendo.00212.2016.

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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 other trophic factors control human IGF1 gene expression, in large part because of the absence of any cellular model systems that robustly express IGF-I. Here, we have addressed mechanisms of regulation of human IGF-I by GH after generating cells in which the IGF1 chromosomal locus has been incorporated into a mouse cell line. Using this model, we found that physiological levels of GH rapidly stimulate human IGF1 gene transcription and identify several potential transcriptional enhancers in chromatin that bind STAT5b in a GH-regulated way. Each of the putative enhancers also activates a human IGF1 gene promoter in reconstitution experiments in the presence of the GH receptor, STAT5b, and GH. Thus we have developed a novel experimental platform that now may be used to determine how human IGF1 gene expression is controlled under different physiological and pathological conditions.

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28

Eliakim, Alon, Youngman Oh e 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, n. 2 (1 agosto 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 but significant increases were found in both the resting and exercising arm for IGF-I and IGF binding protein-3 (IGFBP-3). GH was elevated in blood sampled from both the resting (from 1.04 ± 0.68 to a peak of 2.57 ± 0.53 ng/ml) and exercising arm (1.04 ± 0.66 to 2.43 ± 0.42 ng/ml, P < 0.05). Unilateral wrist exercise was not sufficiently intense to increase circulating lactate or heart rate, but it led to systemic changes in GH, IGF-I, IGFBP-3, and FGF-2. Low-intensity exercise involving small muscle groups can influence the circulating levels of growth factors.

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29

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

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30

Butler, Andrew A., Shoshana Yakar e Derek LeRoith. "Insulin-Like Growth Factor-I: Compartmentalization Within the Somatotropic Axis?" Physiology 17, n. 2 (aprile 2002): 82–85. http://dx.doi.org/10.1152/nips.01351.2001.

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Abstract (sommario):

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

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Abstract (sommario):

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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Bosche, William J., Daina Z. Ewton e James R. Florini. "Transforming growth factor-beta isoform expression in insulin-like growth factor stimulated myogenesis". Journal of Cellular Physiology 164, n. 2 (agosto 1995): 324–33. http://dx.doi.org/10.1002/jcp.1041640213.

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Belfiore, Antonino, Francesco Frasca, Giuseppe Pandini, Laura Sciacca e Riccardo Vigneri. "Insulin Receptor Isoforms and Insulin Receptor/Insulin-Like Growth Factor Receptor Hybrids in Physiology and Disease". Endocrine Reviews 30, n. 6 (1 ottobre 2009): 586–623. http://dx.doi.org/10.1210/er.2008-0047.

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Friedrich, Nele, Torben Jørgensen, Henri Wallaschofski e 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 (settembre 2012): e263. http://dx.doi.org/10.1097/01.hjh.0000420853.64612.b5.

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Scott, Carolyn D., e 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, n. 1 (gennaio 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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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 e 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, n. 2 (febbraio 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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37

Werner, Haim, e Ilan Bruchim. "The insulin-like growth factor-I receptor as an oncogene". Archives of Physiology and Biochemistry 115, n. 2 (maggio 2009): 58–71. http://dx.doi.org/10.1080/13813450902783106.

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38

Karadag, A. S., D. T. Ertugrul, E. Tutal e 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, n. 4 (1 febbraio 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 e 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, n. 4 (ottobre 2008): H1684—H1689. http://dx.doi.org/10.1152/ajpheart.00548.2008.

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Abstract (sommario):

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 receptor mRNA levels by 30% at 8 h compared with native LDL, and this decrease was maintained for up to 20 h. However, insulin-like growth factor-1 receptor protein synthesis rate was not altered by oxidized LDL. Pulse-chase labeling experiments revealed that oxidized LDL reduced insulin-like growth factor-1 receptor protein half-life to 12.2 ± 1.7 h from 24.4 ± 4.7 h with native LDL. This destabilization of insulin-like growth factor-1 receptor protein was accompanied by enhanced receptor ubiquitination. Overexpression of dominant-negative Nedd4 prevented oxidized LDL-induced downregulation of insulin-like growth factor-1 receptor, suggesting that Nedd4 was the ubiquitin ligase that mediated receptor downregulation. However, the proteasome inhibitors lactacystin, MG-132, and proteasome inhibitor-1 failed to block oxidized LDL-induced downregulation of insulin-like growth factor-1 receptor. Thus oxidized LDL downregulates insulin-like growth factor-1 receptor by destabilizing the protein via Nedd4-enhanced ubiquitination, leading to degradation via a proteasome-independent pathway. This finding provides novel insights into oxidized LDL-triggered oxidant signaling and mechanisms of smooth muscle cell depletion that contribute to plaque destabilization and coronary events.

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Han, Ho Jae, Chang Won Kang e 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, n. 12 (dicembre 2006): 1172–79. http://dx.doi.org/10.1111/j.1440-1681.2006.04495.x.

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41

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, n. 3 (marzo 1989): 338–42. http://dx.doi.org/10.1007/bf01536252.

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42

Olanrewaju, Hammed A., Eric D. Sanzenbacher e Edward R. Seidel. "Insulin-like growth factor I in suckling rat gastric contents". Digestive Diseases and Sciences 41, n. 7 (luglio 1996): 1392–97. http://dx.doi.org/10.1007/bf02088564.

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43

Cappon, J., J. A. Brasel, S. Mohan e D. M. Cooper. "Effect of brief exercise on circulating insulin-like growth factor I". Journal of Applied Physiology 76, n. 6 (1 giugno 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 preexercise to 25,316 ng/ml at 10 min of exercise; P < 0.05]. IGF-I peaked by the 10th min of exercise, like GH, and remained significantly elevated for only 20 min of recovery. We tested for possible GH-dependent mechanisms in which circulating IGF-I would increase 12-24 h after exercise. Ten subjects (age 23–32 yr) performed 10 min of above-lactate threshold exercise at 9, 10, and 11 A.M. GH was elevated after the first exercise bout (peak GH 6.05 +/- 1.45 ng/ml; P < 0.001) but was significantly reduced for the second and third bouts (peak GH 2.52 +/- 0.76 and 1.50 +/- 0.40 ng/ml, respectively). No increase in IGF-I was observed by 8 A.M. on the following day. Heavy ergometer exercise led to brief and small increases in circulating IGF-I that were independent of circulating GH.(ABSTRACT TRUNCATED AT 250 WORDS)

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Muhammad, Tahir, Mengjing Li, Jianfeng Wang, Tao Huang, Shigang Zhao, Han Zhao, Hongbin Liu e Zi-Jiang Chen. "Roles of insulin-like growth factor II in regulating female reproductive physiology". Science China Life Sciences 63, n. 6 (10 aprile 2020): 849–65. http://dx.doi.org/10.1007/s11427-019-1646-y.

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45

Haus, Erhard, E. Haus, L. Dumitriu, G. Y. Nicolau, S. Bologa e 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, n. 4 (gennaio 2001): 709–27. http://dx.doi.org/10.1081/cbi-100106083.

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46

Salehi, Zivar, Farhad Mashayekhi, Mohammad Naji e 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, n. 7 (luglio 2009): 950–53. http://dx.doi.org/10.1016/j.jocn.2008.09.018.

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GAUSSIN, V., e C. DEPRE. "Myostatin, the cardiac chalone of insulin-like growth factor-1". Cardiovascular Research 68, n. 3 (1 dicembre 2005): 347–49. http://dx.doi.org/10.1016/j.cardiores.2005.09.007.

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48

Radosavljevic, Tatjana, Vera Todorovic, Danijela Vucevic e Branka Sikic. "The growth hormone axis and insulin-like growth factors". Medical review 58, n. 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 growth factor-I (IGF-I) is essential for normal growth. Confirmation of the significance of IGF-I in human physiology was obtained by the discovery of a patient with intrauterine growth retardation and postnatal growth failure associated with a mutation in the IGF-1 gene. Stages of evolution of the somatomedin hypothesis The original somatomedin hypothesis postulated that somatic growth was regulated by growth hormone's (GH's) stimulation of hepatic IGF-1 production, with IGF-1 acting in an endocrine fashion to promote growth. The dual effectors theory proposed an alternative view, involving direct effects by GH on peripheral tissues not mediated by IGF-1 and GH-stimulated local IGF-1 production for autocrine/paracrine action. It is now clear that G H stimulates the formation of ternary IGF binding complex, which stabilizes IGF-I in the serum.

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Vardy, Daniel A., Csaba Kari, Gerald S. Lazarus, Pamela J. Jensen, Asher Zilberstein, Gregory D. Plowman e 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, n. 2 (maggio 1995): 257–65. http://dx.doi.org/10.1002/jcp.1041630206.

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50

Leibush, B., M. Párrizas, I. Navarro, Y. Lappova, M. A. Maestro, M. Encinas, E. M. Plisetskaya e J. Gutiérrez. "Insulin and insulin-like growth factor-I receptors in fish brain". Regulatory Peptides 61, n. 2 (febbraio 1996): 155–61. http://dx.doi.org/10.1016/0167-0115(95)00154-9.

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