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Journal articles on the topic 'Insulin-like growth factor-binding proteins Molecular aspects'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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1

Wetterau, Lawrence A., Michael G. Moore, Kuk-Wah Lee, Melanie L. Shim, and Pinchas Cohen. "Novel Aspects of the Insulin-like Growth Factor Binding Proteins." Molecular Genetics and Metabolism 68, no. 2 (October 1999): 161–81. http://dx.doi.org/10.1006/mgme.1999.2920.

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2

Roberts, Charles T., and Derek Leroith. "11 Molecular aspects of insulin-like growth factors, their binding proteins and receptors." Baillière's Clinical Endocrinology and Metabolism 2, no. 4 (November 1988): 1069–85. http://dx.doi.org/10.1016/s0950-351x(88)80030-2.

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3

Wang, Peng-Fei, Xiaoyu Wang, Min Liu, Zheng Zeng, Caiji Lin, Wenwen Xu, Wenqing Ma, et al. "The Oncogenic Functions of Insulin-like Growth Factor 2 mRNA-Binding Protein 3 in Human Carcinomas." Current Pharmaceutical Design 26, no. 32 (September 24, 2020): 3939–54. http://dx.doi.org/10.2174/1381612826666200413080936.

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IGF2BP3 (also known as IMP3, KOC), a member of the insulin-like growth factor mRNA-binding protein family (IMPs), has been a research target in recent studies of promoting embryo development and exacerbating cancer. IGF2BP3 is ubiquitously expressed in early embryogenesis stages but limited in postembryonic stages, which is important in many physiological aspects such as stem cell renewal, morphological development and metabolism. A large number of studies show that IGF2BP3 interacts with many kinds of non-coding RNAs and proteins to promote cancer cell proliferation and metastasis and inhibit cancer cell apoptosis. As IGF2BP3 is highly expressed in advanced cancers and associated with poor overall survival rates of patients, it may be a potential molecular marker in cancer diagnosis for the detection of cancerous tissues and an indicator of cancer stages. Therefore, anti-IGF2BP3 drugs or monoclonal antibodies are expected as new therapeutic methods in cancer treatment. This review summarizes recent findings among IGF2BP3, RNA and proteins in cancer processes, with a focus on its cancer-promoting mechanisms and potential application as a new biomarker for cancer diagnosis and treatment.

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4

Ruan, Wenjing, Jing Deng, and Kejing Ying. "Novel Aspects of Insulin-like Growth Factor 1/insulin Network in Chronic Inflammatory Airway Disease." Current Medicinal Chemistry 27, no. 42 (December 16, 2020): 7256–63. http://dx.doi.org/10.2174/0929867326666191113140826.

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At least a proportion of patients suffering from chronic inflammatory airway diseases respond poorly to the bronchodilator and corticosteroid therapies. There is a need for the development of improved anti-inflammatory treatment. Insulin Growth Factor 1 (IGF1) and insulin participate in not only metabolism and glucose homeostasis, but also many other physiological and pathophysiological processes, including growth and inflammation. Recently, it was shown that not only the classical IGF1 and IGF1 Receptor (IGF1R), but also the other molecules in the IGF1/insulin network, including insulin, insulin-like growth factor-binding protein (IGFBP), and IGFBP protease, have roles in chronic inflammatory airway diseases. This review aims to provide a comprehensive insight into recent endeavors devoted to the role of the IGF1/insulin network in chronic inflammatory airway diseases. Its participation in airway inflammation, remodeling, and hyper-responsiveness (AHR), as well as acute exacerbation, has been conclusively demonstrated. Its possible relation to glucocorticoid insensitivity has also been indicated. A better understanding of the IGF1/insulin network by further bench-to-bedside research may provide us with rational clinical therapeutic approaches against chronic inflammatory airway diseases.

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5

Pang, Ying, Xiaojun Zhang, Jianbo Yuan, Xiaoxi Zhang, Jianhai Xiang, and Fuhua Li. "Characterization and Expression Analysis of Insulin Growth Factor Binding Proteins (IGFBPs) in Pacific White Shrimp Litopenaeus vannamei." International Journal of Molecular Sciences 22, no. 3 (January 21, 2021): 1056. http://dx.doi.org/10.3390/ijms22031056.

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The insulin signaling (IIS) pathway plays an important role in the metabolism, growth, development, reproduction, and longevity of an organism. As a key member of the IIS pathway, insulin-like growth factor binding proteins (IGFBPs) are widely distributed a family in invertebrates and vertebrates that are critical in various aspects of physiology. As an important mariculture species, the growth of Pacific white shrimp, Litopenaeus vannamei, is one of the most concerning characteristics in this area of study. In this study, we identified three IGFBP genes in the genome of L. vannamei and analyzed their gene structures, phylogenetics, and expression profiles. LvIGFBP1 was found to contain three domains (the insulin growth factor binding (IB) domain, the Kazal-type serine proteinase inhibitor (Kazal) domain, and the immunoglobulin C-2 (IGc2) domain), while LvIGFBP2 and LvIGFBP3 only contained a single IB domain. LvIGFBP1 exhibited high expression in most tissues and different developmental stages, while LvIGFBP2 and LvIGFBP3 were only slightly expressed in hemocytes. The RNA interference of LvIGFBP1 resulted in a significantly smaller increment of body weight than that of control groups. These results will improve our understanding of the conservative structure and function of IGFBPs and show potential applications for the growth of shrimp.

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6

Ning, Yun, Alwin G. P. Schuller, Cheryl A. Conover, and John E. Pintar. "Insulin-Like Growth Factor (IGF) Binding Protein-4 Is Both a Positive and Negative Regulator of IGF Activity in Vivo." Molecular Endocrinology 22, no. 5 (May 1, 2008): 1213–25. http://dx.doi.org/10.1210/me.2007-0536.

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Abstract IGFs are required for normal prenatal and postnatal growth. Although actions of IGFs can be modulated by a family of IGF-binding proteins (IGFBPs) in vitro, these studies have identified a complicated pattern of stimulatory and inhibitory IGFBP effects, so that understanding relevant aspects of IGFBP action in vivo has been limited. Here we have produced a null mutation of one specific IGFBP, IGFBP-4, which is coexpressed with IGF-II early in development. Surprisingly, mutation of IGFBP-4, believed from in vitro studies to be exclusively inhibitory, leads to a prenatal growth deficit that is apparent from the time that the IGF-II growth deficit first arises, which strongly suggests that IGFBP-4 is required for optimal IGF-II-promoted growth during fetal development. Mice encoding a mutant IGFBP-4 protease (pregnancy-associated plasma protein-A), which facilitates IGF-II release from an inactive IGF-II/IGFBP-4 complex in vitro, are even smaller than IGFBP-4 mutant mice. However, the more modest IGFBP-4 growth deficit is completely restored in double IGFBP-4/pregnancy-associated plasma protein-A-deficient mice. Taken together these results indicate not only that IGFBP-4 functions as a local reservoir to optimize IGF-II actions needed for normal embryogenesis, but also establish that IGFBP-4 proteolysis is required to activate most, if not all, IGF-II mediated growth-promoting activity.

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7

Dean, Richard A., Georgina S. Butler, Yamina Hamma-Kourbali, Jean Delbé, David R. Brigstock, José Courty, and Christopher M. Overall. "Identification of Candidate Angiogenic Inhibitors Processed by Matrix Metalloproteinase 2 (MMP-2) in Cell-Based Proteomic Screens: Disruption of Vascular Endothelial Growth Factor (VEGF)/Heparin Affin Regulatory Peptide (Pleiotrophin) and VEGF/Connective Tissue Growth Factor Angiogenic Inhibitory Complexes by MMP-2 Proteolysis." Molecular and Cellular Biology 27, no. 24 (October 1, 2007): 8454–65. http://dx.doi.org/10.1128/mcb.00821-07.

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ABSTRACT Matrix metalloproteinases (MMPs) exert both pro- and antiangiogenic functions by the release of cytokines or proteolytically generated angiogenic inhibitors from extracellular matrix and basement membrane remodeling. In the Mmp2 −/− mouse neovascularization is greatly reduced, but the mechanistic aspects of this remain unclear. Using isotope-coded affinity tag labeling of proteins analyzed by multidimensional liquid chromatography and tandem mass spectrometry we explored proteome differences between Mmp2 −/− cells and those rescued by MMP-2 transfection. Proteome signatures that are hallmarks of proteolysis revealed cleavage of many known MMP-2 substrates in the cellular context. Proteomic evidence of MMP-2 processing of novel substrates was found. Insulin-like growth factor binding protein 6, follistatin-like 1, and cystatin C protein cleavage by MMP-2 was biochemically confirmed, and the cleavage sites in heparin affin regulatory peptide (HARP; pleiotrophin) and connective tissue growth factor (CTGF) were sequenced by matrix-assisted laser desorption ionization-time of flight mass spectrometry. MMP-2 processing of HARP and CTGF released vascular endothelial growth factor (VEGF) from angiogenic inhibitory complexes. The cleaved HARP N-terminal domain increased HARP-induced cell proliferation, whereas the HARP C-terminal domain was antagonistic and decreased cell proliferation and migration. Hence the unmasking of cytokines, such as VEGF, by metalloproteinase processing of their binding proteins is a new mechanism in the control of cytokine activation and angiogenesis.

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8

Mancarella, Caterina, Andrea Morrione, and Katia Scotlandi. "Novel Regulators of the IGF System in Cancer." Biomolecules 11, no. 2 (February 12, 2021): 273. http://dx.doi.org/10.3390/biom11020273.

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The insulin-like growth factor (IGF) system is a dynamic network of proteins, which includes cognate ligands, membrane receptors, ligand binding proteins and functional downstream effectors. It plays a critical role in regulating several important physiological processes including cell growth, metabolism and differentiation. Importantly, alterations in expression levels or activation of components of the IGF network are implicated in many pathological conditions including diabetes, obesity and cancer initiation and progression. In this review we will initially cover some general aspects of IGF action and regulation in cancer and then focus in particular on the role of transcriptional regulators and novel interacting proteins, which functionally contribute in fine tuning IGF1R signaling in several cancer models. A deeper understanding of the biological relevance of this network of IGF1R modulators might provide novel therapeutic opportunities to block this system in neoplasia.

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9

Jonas, Katharina, George A. Calin, and Martin Pichler. "RNA-Binding Proteins as Important Regulators of Long Non-Coding RNAs in Cancer." International Journal of Molecular Sciences 21, no. 8 (April 23, 2020): 2969. http://dx.doi.org/10.3390/ijms21082969.

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The majority of the genome is transcribed into pieces of non-(protein) coding RNA, among which long non-coding RNAs (lncRNAs) constitute a large group of particularly versatile molecules that govern basic cellular processes including transcription, splicing, RNA stability, and translation. The frequent deregulation of numerous lncRNAs in cancer is known to contribute to virtually all hallmarks of cancer. An important regulatory mechanism of lncRNAs is the post-transcriptional regulation mediated by RNA-binding proteins (RBPs). So far, however, only a small number of known cancer-associated lncRNAs have been found to be regulated by the interaction with RBPs like human antigen R (HuR), ARE/poly(U)-binding/degradation factor 1 (AUF1), insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1), and tristetraprolin (TTP). These RBPs regulate, by various means, two aspects in particular, namely the stability and the localization of lncRNAs. Importantly, these RBPs themselves are commonly deregulated in cancer and might thus play a major role in the deregulation of cancer-related lncRNAs. There are, however, still many open questions, for example regarding the context specificity of these regulatory mechanisms that, in part, is based on the synergistic or competitive interaction between different RBPs. There is also a lack of knowledge on how RBPs facilitate the transport of lncRNAs between different cellular compartments.

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10

Huang, Xinqiang, Hong Cai, Ron Ammar, Yan Zhang, Yihe Wang, Kandasamy Ravi, John Thompson, and Gabor Jarai. "Molecular characterization of a precision-cut rat liver slice model for the evaluation of antifibrotic compounds." American Journal of Physiology-Gastrointestinal and Liver Physiology 316, no. 1 (January 1, 2019): G15—G24. http://dx.doi.org/10.1152/ajpgi.00281.2018.

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Precision-cut liver tissue slice (PCLS) contains all major cell types of the liver parenchyma and preserves the original cell-cell and cell-matrix contacts. It represents a promising ex vivo model to study liver fibrosis and test the antifibrotic effect of experimental compounds in a physiological environment. In this study using RNA sequencing, we demonstrated that various pathways functionally related to fibrotic mechanisms were dysregulated in PCLSs derived from rats subjected to bile duct ligation. The activin receptor-like kinase-5 (Alk5) inhibitor SB525334, nintedanib, and sorafenib each reversed a subset of genes dysregulated in fibrotic PCLSs, and of those genes we identified 608 genes whose expression was reversed by all three compounds. These genes define a molecular signature characterizing many aspects of liver fibrosis pathology and its attenuation in the model. A panel of 12 genes and 4 secreted biomarkers including procollagen I, hyaluronic acid (HA), insulin-like growth factor binding protein 5 (IGFBP5), and WNT1-inducible signaling pathway protein 1 (WISP1) were further validated as efficacy end points for the evaluation of antifibrotic activity of experimental compounds. Finally, we showed that blockade of αV-integrins with a small molecule inhibitor attenuated the fibrotic phenotype in the model. Overall, our results suggest that the rat fibrotic PCLS model may represent a valuable system for target validation and determining the efficacy of experimental compounds. NEW & NOTEWORTHY We investigated the antifibrotic activity of three compounds, the activin receptor-like kinase-5 (Alk5) inhibitor SB525334, nintedanib, and sorafenib, in a rat fibrotic precision-cut liver tissue slice model using RNA sequencing analysis. A panel of 12 genes and 4 secreted biomarkers including procollagen I, hyaluronic acid (HA), insulin-like growth factor binding protein 5 (IGFBP5), and WNT1-inducible signaling pathway protein 1 (WISP1) were then established as efficacy end points to validate the antifibrotic activity of the αV-integrin inhibitor CWHM12. This study demonstrated the value of the rat fibrotic PCLS model for the evaluation of antifibrotic drugs.

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11

Fouladi-Nashta, A. A., and K. H. S. Campbell. "Dissociation of oocyte nuclear and cytoplasmic maturation by the addition of insulin in cultured bovine antral follicles." Reproduction 131, no. 3 (March 2006): 449–60. http://dx.doi.org/10.1530/rep.1.00581.

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Follicles of 4–8 mm in diameter were dissected from ovaries and cultured in Waymouth culture medium in the presence or absence of insulin (5 μg/ml) at 39 °C in a humidified atmosphere of 45% O2, 5% CO2and 50% N2for 24 h. Following follicle culture, the oocytes were collected and examined for developmental potential, total protein profile and ultrastructural aspects. Oocytes aspirated directly from follicles of the same size were used as controls. Addition of insulin to the follicle culture medium significantly reduced expression of the low molecular weight insulin-like growth factor-binding proteins (IGFBPs) in the follicular fluid, and significantly reduced the cleavage rate of subsequently matured and fertilised oocytes (0.52 vs 0.61). However, there were no differences in the proportion of cleaved embryos which developed to the blastocyst stage (0.30 vs 0.28), nor embryo quality as assessed by total cell number (137 ± 8.53 vs124.6 ± 6.95). The total protein profiles of immature oocytes recovered after 24 h of follicle culture were compared by PAGE. There were marked differences between the two groups, unmatured oocytes recovered from the insulin-positive follicle group showed a protein pattern similar to that of matured oocytes. In addition, examination of ultrastructural features by transmission electron microscopy indicated that oocytes from follicles cultured in the presence of insulin undergo many of the cytoplasmic changes associated with oocyte maturation. In conclusion, follicle culture in the presence of insulin is beneficial for follicular survival and significantly reduces cleavage but has no detrimental effects on the development of cultured embryos. However, many of the cytoplasmic changes associated with oocyte maturation occur prior to the induction of nuclear maturation.

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12

Benjamin, Jeremy J. R., Pak P. Poon, John D. Drysdale, Xiangmin Wang, Richard A. Singer, and Gerald C. Johnston. "Dysregulated Arl1, a regulator of post-Golgi vesicle tethering, can inhibit endosomal transport and cell proliferation in yeast." Molecular Biology of the Cell 22, no. 13 (July 2011): 2337–47. http://dx.doi.org/10.1091/mbc.e10-09-0765.

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Small monomeric G proteins regulated in part by GTPase-activating proteins (GAPs) are molecular switches for several aspects of vesicular transport. The yeast Gcs1 protein is a dual-specificity GAP for ADP-ribosylation factor (Arf) and Arf-like (Arl)1 G proteins, and also has GAP-independent activities. The absence of Gcs1 imposes cold sensitivity for growth and endosomal transport; here we present evidence that dysregulated Arl1 may cause these impairments. We show that gene deletions affecting the Arl1 or Ypt6 vesicle-tethering pathways prevent Arl1 activation and membrane localization, and restore growth and trafficking in the absence of Gcs1. A mutant version of Gcs1 deficient for both ArfGAP and Arl1GAP activity in vitro still allows growth and endosomal transport, suggesting that the function of Gcs1 that is required for these processes is independent of GAP activity. We propose that, in the absence of this GAP-independent regulation by Gcs1, the resulting dysregulated Arl1 prevents growth and impairs endosomal transport at low temperatures. In cells with dysregulated Arl1, an increased abundance of the Arl1 effector Imh1 restores growth and trafficking, and does so through Arl1 binding. Protein sequestration at the trans-Golgi membrane by dysregulated, active Arl1 may therefore be the mechanism of inhibition.

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13

Epperlein, Sarah, Claudia Gebhardt, Kerstin Rohde, Rima Chakaroun, Marie Patt, Imke Schamarek, Susan Kralisch, et al. "The Effect of FGF21 and Its Genetic Variants on Food and Drug Cravings, Adipokines and Metabolic Traits." Biomedicines 9, no. 4 (March 29, 2021): 345. http://dx.doi.org/10.3390/biomedicines9040345.

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Fibroblast growth factor 21 (FGF21) is a regulator of addictive behavior. Increasing evidence suggests an impact of FGF21 on eating behavior, food and drug cravings and on other adipokines like insulin-like growth factor 1 (IGF-1) or adiponectin. We investigated the association of serum FGF21 and genetic variants with aspects of food and drug craving and obesity related metabolic parameters including serum adipokine levels. Standardized questionnaires, blood samples and anthropometric data of the Sorbs cohort (n = 1046) were analyzed using SPSS. For genetic analyses, the FGF21-locus ±10 kb was genotyped and analyzed using PLINK. Validation was conducted in a second independent cohort (n = 704). FGF21 was significantly associated with alcohol and coffee consumption, smoking and eating behavior (disinhibition). We confirmed correlations of FGF21 serum levels with IGF-1, adiponectin, pro-enkephalin, adipocyte fatty-acid-binding protein, chemerin and progranulin. FGF21 genetic variants were associated with anthropometric and metabolic parameters, adipokines, food and drug craving while strongest evidence was seen with low-density lipoprotein cholesterol (LDL-C). We highlight the potential role of FGF21 in food and drug cravings and provide new insights regarding the link of FGF21 with other adipokines as well as with metabolic traits, in particular those related to lipid metabolism (LDL-C).

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14

Chan, Kam, and E. Martin Spencer. "General aspects of insulin-like growth factor binding proteins." Endocrine 7, no. 1 (August 1997): 95–97. http://dx.doi.org/10.1007/bf02778072.

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15

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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16

Hodgkinson, S. C., J. R. Napier, G. S. G. Spencer, and J. J. Bass. "Glycosaminoglycan binding characteristics of the insulin-like growth factor-binding proteins." Journal of Molecular Endocrinology 13, no. 1 (August 1, 1994): 105–12. http://dx.doi.org/10.1677/jme.0.0130105.

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17

Prosser, C. G., and R. D. McLaren. "Insulin-like growth factor binding proteins of equine serum." Biochemical and Biophysical Research Communications 189, no. 3 (December 1992): 1255–60. http://dx.doi.org/10.1016/0006-291x(92)90208-3.

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18

Lamson, George, Linda C. Giudice, and Ron G. Rosenfeld. "Insulin-Like Growth Factor Binding Proteins: Structural and Molecular Relationships." Growth Factors 5, no. 1 (January 1991): 19–28. http://dx.doi.org/10.3109/08977199109000268.

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19

Holly, Jeff, and Claire Perks. "The Role of Insulin-Like Growth Factor Binding Proteins." Neuroendocrinology 83, no. 3-4 (2006): 154–60. http://dx.doi.org/10.1159/000095523.

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20

Murphy, LJ. "Insulin-like growth factor-binding proteins: functional diversity or redundancy?" Journal of Molecular Endocrinology 21, no. 2 (October 1, 1998): 97–107. http://dx.doi.org/10.1677/jme.0.0210097.

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21

Veomett, George E., Lora L. Munger, Gary L. Smith, and Judith E. Schollmeyer. "Heterogeneity of insulin-like growth factor binding proteins in swine." Molecular and Cellular Endocrinology 65, no. 1-2 (August 1989): 49–57. http://dx.doi.org/10.1016/0303-7207(89)90164-0.

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22

Yamanaka, Yoshitaka, Elizabeth M. Wilson, Ron G. Rosenfeld, and Youngman Oh. "Inhibition of Insulin Receptor Activation by Insulin-like Growth Factor Binding Proteins." Journal of Biological Chemistry 272, no. 49 (December 5, 1997): 30729–34. http://dx.doi.org/10.1074/jbc.272.49.30729.

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23

Nakamura, Michio, Shin’ichi Miyamoto, Hiroyuki Maeda, Genichiro Ishii, Takahiro Hasebe, Tsutomu Chiba, Masahiro Asaka, and Atsushi Ochiai. "Matrix metalloproteinase-7 degrades all insulin-like growth factor binding proteins and facilitates insulin-like growth factor bioavailability." Biochemical and Biophysical Research Communications 333, no. 3 (August 2005): 1011–16. http://dx.doi.org/10.1016/j.bbrc.2005.06.010.

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24

Kelley, KM, KE Schmidt, L. Berg, K. Sak, MM Galima, C. Gillespie, L. Balogh, A. Hawayek, JA Reyes, and M. Jamison. "Comparative endocrinology of the insulin-like growth factor-binding protein." Journal of Endocrinology 175, no. 1 (October 1, 2002): 3–18. http://dx.doi.org/10.1677/joe.0.1750003.

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Emerging early in chordate evolution, the IGF-regulatory axis diverged from an insulin-like predecessor into a vertebrate regulatory system specializing in cell growth activation and allied anabolic functions. Essential to the divergence of the IGF and insulin systems was an early presence of soluble IGF-binding proteins (IGFBPs), which bind IGF peptides at much higher affinity than that of the insulin receptor but at comparable affinities to that of the IGF receptor. IGFBPs have no homology with IGF receptors. Instead, IGFBPs are a derived group of proteins within a superfamily of cysteine-rich growth factors, whose members are found throughout the animal taxa. While blocking IGF actions through the insulin receptor is a fundamental role, IGFBPs evolved within the vertebrate line into centralized, 'integrators' of the endocrine growth-regulatory apparatus. IGFBPs have substantial influences on the distribution and bioavailability of IGF peptides in the cellular and physiological environments, but they have a variety of other properties. The six principal mammalian IGFBPs exhibit an array of specialized properties that appear to be derived from a complex evolutionary history (including cell membrane association, interaction with proteins that post-translationally modify them, direct IGF-independent effects on cells, and others) and they are regulated by a diversity of 'outside' factors (e.g. other hormones, metabolic status, stress). Thus, IGFBPs are multifunctional integrators having diverse physiological 'agendas'. Much less is known about IGFBPs and their properties in the other vertebrate taxa. Increasingly, however, it is being recognized that they play equally important endocrine roles, in both conserved and non-conserved ways, when compared with those currently defined in mammals. This review highlights selected 'comparative aspects' in current IGFBP research, in an attempt to view this essential group of endocrine regulators from a wider, biological perspective.

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Ilvesmäki, Vesa, Werner F. Blum, and Raimo Voutilainen. "Insulin-like growth factor binding proteins in the human adrenal gland." Molecular and Cellular Endocrinology 97, no. 1-2 (November 1993): 71–79. http://dx.doi.org/10.1016/0303-7207(93)90212-3.

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26

Drop, S. L. S. "On the nomenclature of the insulin-like growth factor binding proteins." Molecular and Cellular Endocrinology 67, no. 2-3 (December 1989): 243–44. http://dx.doi.org/10.1016/0303-7207(89)90214-1.

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27

Taguchi, Tomoko, Hisami Takenouchi, Jun Matsui, Wei-Ran Tang, Mitsuko Itagaki, Yusuke Shiozawa, Kyoko Suzuki, et al. "Involvement of insulin-like growth factor-I and insulin-like growth factor binding proteins in pro–B-cell development." Experimental Hematology 34, no. 4 (April 2006): 508–18. http://dx.doi.org/10.1016/j.exphem.2006.01.009.

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28

Costello, Lisa M., Padraic O'Boyle, Michael G. Diskin, Ailish C. Hynes, and Dermot G. Morris. "Insulin-like growth factor and insulin-like growth factor-binding proteins in the bovine uterus throughout the oestrous cycle." Reproduction, Fertility and Development 26, no. 4 (2014): 599. http://dx.doi.org/10.1071/rd13105.

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The aims of the present study were to assess several components of the insulin-like growth factor (IGF) system in bovine uterine flushings across different days of the oestrous cycle and to examine the relationship between the IGF system and systemic progesterone concentrations. Uterine flushings and plasma were collected from cows on Days 3, 7, 11 and 15 of the oestrous cycle. The IGF-1 concentration was more than 5-fold higher in the uterus compared with plasma on Days 7 and 11 of the cycle, with values similar on Days 3 and 15. Similarly, uterine concentrations of IGF-binding protein (IGFBP)-2 and IGFBP-3 were up to 10- and 4-fold higher than in plasma, respectively, suggesting synthesis and/or transportation of the IGFBPs into the uterus. In addition, concentrations of IGFBP-2 and IGFBP-3 were higher in the uterine horns, ipsilateral to the corpus luteum, on Day 15. This difference could indicate a local controlling mechanism with progesterone possibly playing a role in regulating the concentration of IGFBPs between the uterine horns. There was no significant relationship between systemic progesterone concentrations and IGFBP concentrations on Day 7 of the oestrous cycle. The present study shows that uterine concentrations of IGFBPs are cycle stage specific and also suggests IGF-dependent and -independent functions for IGFBPs during a time of major change in the developing embryo.

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29

Leung, Kin-Chuen, and Ken K. Y. Ho. "Measurement of growth hormone, insulin-like growth factor I and their binding proteins: the clinical aspects." Clinica Chimica Acta 313, no. 1-2 (November 2001): 119–23. http://dx.doi.org/10.1016/s0009-8981(01)00662-3.

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30

OCRANT, IAN. "Insulin-like Growth Factor Binding Proteins in Nervous-Tissue-Derived Cells." Annals of the New York Academy of Sciences 692, no. 1 The Role of I (August 1993): 44–50. http://dx.doi.org/10.1111/j.1749-6632.1993.tb26204.x.

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31

BELL, STEPHEN C. "The Insulin-like Growth Factor Binding Proteins ? The Endometrium and Decidua." Annals of the New York Academy of Sciences 622, no. 1 The Primate E (May 1991): 120–37. http://dx.doi.org/10.1111/j.1749-6632.1991.tb37856.x.

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32

Grønbæk, H., J. Frystyk, H. Ørskov, and A. Flyvbjerg. "Effect of sodium selenite on growth, insulin-like growth factor-binding proteins and insulin-like growth factor-I in rats." Journal of Endocrinology 145, no. 1 (April 1995): 105–12. http://dx.doi.org/10.1677/joe.0.1450105.

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Abstract Selenium is an essential trace element although at higher doses it is also known to be a toxic agent causing a wide range of symptoms including growth retardation. In order to investigate the effect of sodium selenite on growth, insulin-like growth factor-binding proteins (IGFBPs) and insulin-like growth factor-I (IGF-I), 30 male Wistar rats were randomized into three groups. Group A was treated with sodium selenite in the drinking water (3·3 mg selenium/l). Group B was ad libitum fed with free access to standard fodder and tap water and group C was pair fed relative to the selenium-treated rats. Serum IGF-I and IGFBPs were determined on days 0, 14 and at the end of the study on day 35. Selenium-treated rats had significantly lower body weights compared with group B rats on day 9 and group C rats on day 14 (P<0·05). Tibia length was measured at the end of the study and no difference was observed between groups B and C (3·77 ± 0·04 cm vs 3·60±0·02 cm); however, selenium-treated rats had significantly shorter tibia lengths (3·46±0·03 cm) compared with rats in groups B (P<0·001) and C (P<0·05). Selenium treatment induced a significant reduction in circulating IGF-I by the end of the study compared with ad libitum and pair fed rats (P<0·05). Serum subjected to Western ligand blots showed four distinct IGFBP bands with apparent relative molecular weights of 38–47 kDa (doublet) (IGFBP-3), 30 kDa (IGFBP-1 and/or IGFBP-2) and 24 kDa (IGFBP-4). At the end of the study a significant reduction in IGFBP-3 was observed in group A compared with groups B and C (P<0·05). Selenium treatment also caused a reduction in IGFBP-1 and/or IGFBP-2 compared with ad libitum fed rats; in addition, a reduction was observed in pair fed controls. In conclusion, sodium selenite treatment leads to growth retardation accompanied by reduced circulating levels of IGF-I, IGFBP-3, and IGFBP-1 and/or IGFBP-2. The reduction in IGF-I and IGFBP-3 could not be attributed to reduced caloric intake but seems to be a specific action of selenium. Journal of Endocrinology (1995) 145, 105–112

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33

Carrick, Francine E., John C. Wallace, and Briony E. Forbes. "The interaction of Insulin-like Growth Factors (IGFs) with Insulin-like Growth Factor Binding Proteins (IGFBPs): a review." Letters in Peptide Science 8, no. 3-5 (May 2001): 147–53. http://dx.doi.org/10.1007/bf02446511.

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Moser, D. R. "Endothelial cells express insulin-like growth factor-binding proteins 2 to 6." Molecular Endocrinology 6, no. 11 (November 1, 1992): 1805–14. http://dx.doi.org/10.1210/me.6.11.1805.

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35

Komatsu, Setsuko, and Hisashi Hirano. "Plant basic 7 S globulin-like proteins have insulin and insulin-like growth factor binding activity." FEBS Letters 294, no. 3 (December 9, 1991): 210–12. http://dx.doi.org/10.1016/0014-5793(91)80671-o.

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36

CLEMMONS, D. R., J. I. JONES, W. H. BUSBY, and G. WRIGHT. "Role of Insulin-like Growth Factor Binding Proteins in Modifying IGF Actions." Annals of the New York Academy of Sciences 692, no. 1 The Role of I (August 1993): 10–21. http://dx.doi.org/10.1111/j.1749-6632.1993.tb26201.x.

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37

Rodgers, B. D., R. M. Bautista, and C. S. Nicoll. "Regulation of Insulin-Like Growth Factor-Binding Proteins in Rats with Insulin-Dependent Diabetes Mellitus." Experimental Biology and Medicine 210, no. 3 (December 1, 1995): 234–41. http://dx.doi.org/10.3181/00379727-210-43944.

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38

Ooi, Guck T. "Insulin-like growth factor-binding proteins (IGFBPs): more than just 1, 2, 3." Molecular and Cellular Endocrinology 71, no. 2 (June 1990): C39—C43. http://dx.doi.org/10.1016/0303-7207(90)90243-2.

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39

Silha, Josef V., and Liam J. Murphy. "Minireview: Insights from Insulin-Like Growth Factor Binding Protein Transgenic Mice." Endocrinology 143, no. 10 (October 1, 2002): 3711–14. http://dx.doi.org/10.1210/en.2002-220116.

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Abstract The existence of abundant high affinity binding proteins for the IGFs, the IGF binding proteins (IGFBPs), was first demonstrated more than 40 yr ago in the very early days of somatomedin research. With the development of molecular techniques and transgenic and knockout mouse models, the nature, complexity, and redundancy of the IGFBPs have now started to be elucidated. Indeed the functional role of the circulating IGFs and the originally proposed endocrine somatomedin hypothesis have recently been questioned. The limited reports to date indicate that IGFBP knockout mice have few phenotypic manifestations. In contrast, overexpression of IGFBPs in transgenic mice is associated with manifestations that provide some insight into the physiological role of the binding proteins. The predominant effect of generalized or tissue-specific overexpression of the IGFBPs has been growth inhibition as would be anticipated from inhibition of the actions of IGF-I and -II. In addition, impaired glucose homeostasis and reduced fecundity have been observed in both IGFBP-1- and IGFBP-3-overexpressing transgenic mice. This review examines the data reported to date for transgenic mouse models that overexpress IGFBPs. In addition, data from transgenic mice that overexpress the acid-labile subunit, an important component of the ternary complex, have also been reviewed.

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40

BRADSHAW, S. L., and V. K. M. HAN. "Growth Factors Modulate the Biosynthesis of Rat Astroglial Insulin-like Growth Factor Binding Proteins." Annals of the New York Academy of Sciences 692, no. 1 The Role of I (August 1993): 249–52. http://dx.doi.org/10.1111/j.1749-6632.1993.tb26224.x.

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41

De Leon, Daisy D., Darrell M. Wilson, Bert Bakker, George Lamsom, Raymond L. Hintz, and Ron G. Rosenfeld. "Characterization of Insulin-Like Growth Factor Binding Proteins from Human Breast Cancer Cells." Molecular Endocrinology 3, no. 3 (March 1989): 567–74. http://dx.doi.org/10.1210/mend-3-3-567.

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42

Lord, A. P. D., A. A. Martin, P. E. Walton, F. J. Ballard, and L. C. Read. "Insulin-like growth factor-binding proteins in tissue fluids from the lamb." Journal of Endocrinology 129, no. 1 (April 1991): 59–68. http://dx.doi.org/10.1677/joe.0.1290059.

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ABSTRACT Heparinized samples of plasma, cerebrospinal fluid (CSF) and lymph from intestinal, prescapular and popliteal lymph nodes were collected from young lambs in order to characterize and compare the insulin-like growth factor-binding proteins (IGFBPs) in extracellular fluids with those from the circulation. Prior to collection and analysis, the superiority of heparin for plasma preparation was established over EDTA and citrate or the use of serum, according to the extent of IGF-I and IGF-II binding achieved in the high molecular mass IGFBP region in vitro. The IGFBPs were characterized by ligand blotting and competitive binding techniques using radiolabelled IGF-I, IGF-II and the truncated IGF analogue, des(1–3)IGF-I, as well as by ligand blotting of fractions after Superose 6 chromatography of incubations of fluids with labelled factors. This combined analysis demonstrated an IGF-II-specific binding protein at approximately 250 kDa that was present in plasma and each lymph type and presumably represented the soluble type-2 IGF receptor; a complex of 130 kDa containing 52 kDa and 46 kDa binding proteins that was labelled by all three IGF peptides was particularly evident in plasma and intestinal lymph and was probably a complex between IGFBP-3 and the acid-labile subunit; and a group of binding proteins that chromatographed as IGF complexes at approximately 50 kDa. This last group contained IGFBP bands of 52, 46, 35, 28 and 23·5 kDa in plasma and all lymphs as well as an IGF-II-specific band of 22 kDa in prescapular and popliteal lymphs. CSF differed qualitatively from plasma and lymph in that the 52/46 kDa IGFBP bands were undetectable in this fluid; the 35 kDa band was the predominant binding protein, and neither this nor the 28, 23·5 and 22 kDa proteins bound des(1–3)IGF-I to any significant extent. The 52,46 and 28 kDa bands in plasma and lymph did bind this ligand. Immunoblots using antisera against bovine IGFBP-2 showed binding at 35 kDa in all fluids as well as several bands at lower molecular masses. Taken together these results show not only marked differences in the binding protein profiles of sheep plasma, lymph and CSF, but both qualitative and quantitative differences between intestinal, prescapular and popliteal lymphs. We speculate that the differences between lymphs may result from tissuespecific release of binding proteins into extracellular fluid. Journal of Endocrinology (1991) 129, 59–68

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43

Hodgkinson, S. C., S. R. Davis, L. G. Moore, H. V. Henderson, and P. D. Gluckman. "Metabolic clearance of insulin-like growth factor-II in sheep." Journal of Endocrinology 123, no. 3 (December 1989): 461–68. http://dx.doi.org/10.1677/joe.0.1230461.

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ABSTRACT The metabolic clearance of ovine insulin-like growth factor-II (IGF-II) was examined in sheep using 131I-labelled IGF-II. Following i.v. administration the tracer was distributed in a volume similar to that of the vascular space (58-5 ±3.3 ml/kg; mean ± s.e.m., n = 5) and demonstrated a triphasic pattern of clearance. Size-exclusion chromatography of a plasma sample collected 1 min after injection revealed peaks of radioactivity corresponding to hormone complexed to binding proteins of 150 and 40–50 kDa (relative abundance 21 and 65% respectively), a high molecular weight binding protein (>200 kDa; 5%) and 'free' tracer (9%). Chromatography of sequential plasma samples revealed different patterns of clearance for these constituents. Half-lives of 131I-labelled IGF-II complexed to the 150 and 40–50 kDa binding proteins, as calculated from rate constants for their decay, were 351 ± 30 and 9.6 ± min respectively (n = 5). These differ markedly from estimates for the clearance of IGF-I (545 ± 25 min, n = 8, and 34 ± 2.3 min, n = 6) associated with carrier proteins of the same apparent molecular weights. This was reflected in calculated metabolic clearance rates for IGF-I (3.9 ± 0.5 ml/min) and IGF-II (7.8 ±1.0 ml/min). Chromatography also revealed that free IGF-II was reduced to negligible levels by 12 min. In contrast, radioactivity eluting in the position expected for the > 200 kDa binding protein was cleared from the circulation very slowly. However, the small proportion of total radioactivity eluting in these molecular weight regions precluded calculation of decay constants for these species. Tracer degradation was monitored throughout the clearance study and estimated to be <20% at 800 min following i.v. administration. Less than 20% of tracer was cleared into urine over the 24 h of sampling, concurrent with a >90% fall in plasma radioactivity. Tracer in urine was completely degraded. Journal of Endocrinology (1989) 123, 461–468

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44

Panek, Bogusław, Marek Gacko, and Jerzy Pałka. "Metalloproteinases, insulin-like growth factor-I and its binding proteins in aortic aneurysm." International Journal of Experimental Pathology 85, no. 3 (July 16, 2004): 159–64. http://dx.doi.org/10.1111/j.0959-9673.2004.00386.x.

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45

Martínez-Castillo, Moisés, Dorothy Rosique-Oramas, Zaira Medina-Avila, José Luis Pérez-Hernández, Fatima Higuera-De la Tijera, Daniel Santana-Vargas, Eduardo Esteban Montalvo-Jave, et al. "Differential production of insulin-like growth factor-binding proteins in liver fibrosis progression." Molecular and Cellular Biochemistry 469, no. 1-2 (April 16, 2020): 65–75. http://dx.doi.org/10.1007/s11010-020-03728-4.

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46

Luo, J., and L. J. Murphy. "Differential expression of the insulin-like growth factor binding proteins in spontaneously diabetic rats." Journal of Molecular Endocrinology 8, no. 2 (April 1992): 155–63. http://dx.doi.org/10.1677/jme.0.0080155.

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ABSTRACT Diabetes-induced growth retardation in the rodent is associated with both reduced circulating insulin-like growth factor-I (IGF-I) and enhanced levels of inhibitors of somatomedin activity. IGF-binding proteins (IGFBPs) are present in the circulation and tissue fluids and are believed to modulate the actions of IGF-I. Since elevated concentrations of the IGFBPs may contribute to the enhanced somatomedin-inhibitor activity observed in serum from diabetic animals, we have examined the amounts of hepatic IGFBP-1, -2, -3 and -4 mRNA in the spontaneously diabetic BioBreeding/Worcester rat. The study used two types of diabetic animal: mildly diabetic animals, which received suboptimal insulin treatment (0.5–1 U/day) and diabetic animals, which received intensive insulin treatment (3–6 U/day). A significant increase in the amount of IGFBP-1 and IGFBP-2 mRNA was seen 1 month and 3 months after the onset of diabetes. Intensive insulin treatment for 3 weeks normalized the amount of IGFBP-1 mRNA in diabetic rats and resulted in a decrease in IGFBP-2 mRNA. In contrast to the increase in IGFBP-1 and IGFBP-2 mRNA, a significant decrease in IGFBP-3 mRNA was seen in diabetic rats (54.6% of control, P < 0.0005 and 64.6% of control, P < 0.005 for 1 and 3 months respectively) and intensive insulin treatment for 3 weeks did not restore the IGFBP-3 mRNA level in diabetic rats. No significant difference in IGFBP-4 mRNA levels was seen in diabetic compared with non-diabetic rats. When serum was analysed by ligand blotting the major finding was a reduction in the 39–42kDa binding protein. No increase in 29–30kDa IGFBP in the serum was detected in the diabetic rats. From these studies we conclude that the major change in IGFBPs in mildly hyperglycaemic spontaneously diabetic rats is a decrease in IGFBP-3. The changes in hepatic IGFBP-1 and -2 mRNA do not appear to be of sufficient magnitude to result in an increase in serum concentrations of these binding proteins.

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Gargosky, SE, KF Wilson, PJ Fielder, MA Vaccarello, FB Diamond, RC Baxter, AL Rosenbloom, J. Guevara-Aguirre, and RG Rosenfeld. "Effects of insulin-like growth factor I treatment on the molecular distribution of insulin-like growth factors among different binding proteins." Acta Paediatrica 83, s399 (April 1994): 159–62. http://dx.doi.org/10.1111/j.1651-2227.1994.tb13316.x.

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48

Ooi, G. T., and A. C. Herington. "Recognition of insulin-like-growth-factor-binding proteins in serum and amniotic fluid by an antiserum against a low-molecular-mass insulin-like-growth-factor-inhibitor/binding protein." Biochemical Journal 267, no. 3 (May 1, 1990): 615–20. http://dx.doi.org/10.1042/bj2670615.

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An antiserum (R8) raised against a purified specific low-Mr (16,000-18,000) insulin-like-growth-factor (IGF)-inhibitor/binding protein, which is immunologically related to the native growth hormone (GH)-dependent Mr-150,000 IGF-binding protein in serum, has been used to probe a possible additional relationship to the predominant non-GH-dependent IGF-binding protein (Mr approximately 30,000) of human amniotic fluid. Amniotic-fluid fractions and an IGF-inhibitory fraction of serum were analysed by covalent cross-linking, ligand-blotting and immunoblotting techniques. Western blotting of the serum fraction using the R8 antiserum gave five immunoreactive (ir) bands, of which at least three (Mr 38,000, 34,000 and 23,000) possessed IGF-binding activity, as indicated by ligand (125I-IGF-I) blotting. Western blotting of two differently prepared amniotic-fluid fractions, which both showed potent IGF-inhibitory bioactivity, gave several (Mr range 14,500-73,000) ir bands, of which two (Mr 28,000 and 17,000) were most prominent. Ligand-blotting analysis gave a single intensely labelled band at Mr 28,000, consistent with the major presence of the Mr-28,000-30,000 amniotic-fluid IGF-binding protein. Covalent cross-linking of the amniotic-fluid fractions to 125I-IGF-I gave three specifically cross-linked complexes (Mr 36,000, 32,000 and 23,000), which, assuming a 1:1 binding stoichiometry with IGF (Mr 7500), represent binding proteins of Mr 28,500, 24,500 and 15,500 respectively. The Mr-15,500 binding protein, very similar to the Mr-17,000 ir band, in all likelihood represents the IGF-inhibitor protein. Our results indicate that inhibitor-sized binding proteins and IGF-inhibitor bioactivity are present in human amniotic fluid, and that the IGF-inhibitor protein (Mr 16,000) and amniotic-fluid IGF-binding protein (Mr 28,000) are immunologically related. Since the IGF-inhibitor protein is also immunologically and structurally related to the native, GH-dependent, Mr-150,000 binding protein in serum, our data suggest a heretofore-unrecognized immunological similarity between the Mr-150,000 binding protein and the amniotic-fluid binding protein and its serum analogue, the Mr approximately 30,000, non-GH-dependent, binding protein.

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49

Beattie, James, Kirsten Phillips, John H. Shand, Malgorzata Szymanowska, David J. Flint, and Gordon J. Allan. "Molecular recognition characteristics in the insulin-like growth factor (IGF)-insulin-like growth factor binding protein -3/5 (IGFBP-3/5) heparin axis." Journal of Molecular Endocrinology 34, no. 1 (February 2005): 163–75. http://dx.doi.org/10.1677/jme.1.01656.

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Insulin-like growth factor binding proteins (IGFBPs) -3 and -5 are known to interact with various components of the extracellular matrix (ECM; e.g. heparin and heparan sulphate) and this interaction is believed to affect the affinity of both IGFBP species for their cognate ligands – IGF-I and -II. There is little detail on the nature of the molecular complex formed between ECM components, IGFBPs and IGFs although the glycosaminoglycan (GAG) heparin has been reported to reduce the affinity of IGFBP-5 for IGF-I. In order to investigate this phenomenon further, we have undertaken an extensive surface plasmon resonance based biosensor study to report the affinity of IGFBP-3 and -5 for binding heparin (22 and 7 nM respectively). We have also shown that pre-complexation of IGFBP with IGF-I and -II inhibits the subsequent association of IGFBP with heparin and conversely that heparin complexation of IGFBP-3 and -5 inhibits IGFBP binding to biosensor surfaces containing immobilised IGF-I. In addition we have used both IGF-I and heparin coated biosensor surfaces in an attempt to build ternary IGF–IGFBP–heparin complexes in order to gain some insight into the nature of inhibition by heparin of IGFI–IGFBP complex formation. Our data lead us to conclude that the inhibition by heparin is partly competitive in nature, and that ternary complexes of IGF–IGFBP–heparin are either unable to form, or only form unstable transient complexes. The potential biological significance of our data is highlighted by the demonstration that IGF-I and IGF-II can displace endogenous IGFBP-5 from monolayer cultures of the mouse mammary epithelial cell line HC11.

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50

Molnar, P., and L. J. Murphy. "Effects of oestrogen on rat uterine expression of insulin-like growth factor-binding proteins." Journal of Molecular Endocrinology 13, no. 1 (August 1994): 59–67. http://dx.doi.org/10.1677/jme.0.0130059.

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ABSTRACT Previous studies have established that the IGFs are involved in oestrogen-induced uterine proliferation. IGF-binding proteins (IGFBPs) are present in most biological fluids and tissues and may modulate the actions of the IGFs. We examined uterine, hepatic and renal expression of the IGFBPs throughout the oestrous cycle and investigated the effects of oestradiol (OE2) on IGFBP expression in ovariectomized (ovx) rats. Uterine expression of IGFBPs-1 and -3 showed a definite variation throughout the oestrous cycle with highest levels during dioestrus. In the liver and kidney the changes in IGFBP-1 and IGFBP-3 mRNA abundance were the opposite of those observed in the uterus, with the highest levels observed during oestrus. Administration of OE2 to ovx rats decreased uterine IGFBP-3 mRNA and increased IGFBP-4 mRNA levels. In these rats there were no consistent changes in renal IGFBP-1 or IGFBP-3 mRNAs; however, a significant increase in IGFBP-4 mRNA was observed in this tissue, as in the uterus. In the liver an increase in IGFBP-1 mRNA and a decrease in IGFBP-3 mRNA levels were observed in rats treated with OE2. Despite changes in uterine, hepatic and renal IGFBP mRNA levels, no significant variation was seen in serum IGFBPs as determined by ligand blotting of sera. These data demonstrate that there is a cyclical variation in the expression of the IGFBPs in the uterus, kidney and liver, and that OE2 is able to modulate differentially IGFBP expression in these tissues.

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