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Готові списки джерел за темами / Insulin-like growth factor-binding proteins Molecular aspects / Статті в журналах

Щоб переглянути інші типи публікацій з цієї теми, перейдіть за посиланням: Insulin-like growth factor-binding proteins Molecular aspects.

Статті в журналах з теми "Insulin-like growth factor-binding proteins Molecular aspects"

Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 8 лютого 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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Анотація:

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

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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, insu

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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 analyz

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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

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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 h

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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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Анотація:

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

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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 lnc

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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

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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 pr

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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

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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

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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-ri

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25

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

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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-t

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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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34

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 pheno

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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

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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 prot

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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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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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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.

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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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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 seru

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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 sur

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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 i

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