Cited by 536Growth Hormone and Insulin-like Growth FactorsFibroblast Growth Factor ResearchLiver physiology and pathology

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Insulin-like Growth Factor Binding Protein-1: Recent Findings and New Directions

Lee, P. D. K., Giudice, L. C., Conover, C. A., Powell, D. R.·1997·Experimental Biology and Medicine

DOI 10.3181/00379727-216-44182

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Abstract

In 1988, insulin-like growth factor-binding protein-1 (IGFBP-1) became the first characterized member of a group of structurally related soluble proteins which specifically bind and modulate the actions of the IGFs. Since then, a wealth of information has accumulated regarding the physiology of this dynamic serum protein. In this review, we update our 1993 summary (Lee PDK et al. Proc Soc Exp Biol Med 204:4-29) of the status of IGFBP-1 research. The IGFBP-1 protein sequence contains 12 N-terminal and 6 C-terminal cysteine residues which are conserved in other mammalian IGFBP-1 sequences and amongst other IGFBPs; both of the cysteine-rich regions are required for optimal IGF binding. The nonconserved IGFBP-1 midregion may act as both a hinge which defines ligand binding characteristics and as a specific target for protease activity. Integrin-binding and phosphorylation sites within the IGFBP-1 sequence have functional significance in vitro, but their physiologic relevance in vivo have not been defined. The human IGFBP-1 and IGFBP-3 genes are contiguous and located in close proximity to the homeobox A (HOXA) gene cluster on chromosome 7. The other IGFBP genes, located on chromosomes 2, 12, and 17, are also associated with HOX clusters, suggesting evolutionary linkage of the IGFBP and HOX gene families. Similarities between the hlGFBP-1 and phosphoenolpyruvate kinase (PEPCK) promoters, including regions conferring insulin, glucocorticoid, and cyclic adenosine-monophosphate responses, are consistent with our previous hypothesis that IGFBP-1 is involved in regulation of glucose metabolism. The tissue-specific patterns of IGFBP-1 gene expression in liver, kidney, decidua, and ovary may be due to stimulation of IGFBP-1 transcription by hepatic nuclear factor 1 (HNF1) proteins. Clinical and basic studies of IGFBP-1 physiology have been aided by several recently developed assay methods. Numerous investigations have confirmed that insulin, via inhibition of IGFBP-1 transcription, is the primary determinant of IGFBP-1 expression both in vitro and in viva IGF-I and IGF-II also have specific inhibitory effects on IGFBP-1 expression. Glucocorticoids and cAMP stimulate IGFBP-1 transcription, but these effects are observed only in conditions of low or absent insulin effect. Other stimulants of IGFBP-1 expression include thyroid hormones and epidermal growth factor. Phorbol ester stimulation of IGFBP-1 expression can supersede the effects of insulin in vitro; however, the mechanism and in vivo correlates of this effect have not been determined. Cytokines and, perhaps, growth hormones may affect IGFBP-1 expression, perhaps by altering the regulatory actions of insulin; this effect may have important clinical relevance. IGFBP-1 expression is upregulated in liver and (nonhuman) kidney during postinjury regeneration. The IGF-inhibitory actions of IGFBP-1 has been confirmed by numerous in vitro studies and several in vivo animal investigations, including administration of recombinant IGFBP-1 and IGFBP-1 transgenic models. IGFBP-1 has been shown to inhibit somatic linear growth, weight gain, tissue growth, and glucose metabolism. Moreover, IGFBP-1 appears to be a primary determinant of free IGF-I levels in serum. Excess levels of IGFBP-1 may contribute to growth failure in intrauterine growth restriction and in pediatric chronic renal failure, while low IGFBP-1 levels are associated with obesity and with cardiovascular risk factors in insulin resistance syndromes. Serum IGFBP-1 measurements may be useful biochemical marker in these pathologic conditions. IGFBP-1 is expressed in decidualized stromal cells of the uterine endometrium and in ovarian granulosa cells. IGFBP-1, together with IGFs, insulin, ovarian steroids, cytokines, and other factors, is involved in a complex system which regulates menstrual cycles, ovulation, decidualization, blastocyst implantation, and fetal growth. Models for the role of IGFBP-1 in female reproductive physiology are presented, and evidence for pathophysiologic roles in pre-eclampsia, polycystic ovarian syndrome, and uterine malignancy are reviewed. Very recent data indicates that IGFBP-1 undergoes regulated expression in human osteoblasts. Limited information also suggests that IGFBP-1 may be present in peripheral neurons, and that serum IGFBP-1 may increase during exercise and in critical ilIness. In summary, two major roles for IGFBP-1 in normal physiology can be constructed from current data: (i) As an “endocrine” factor, IGFBP-1 regulates the bio-availability of serum IGF-I, thereby modulating IGF-mediated tissue metabolism. The dominant regulation of IGFBP-1 expression by meal-related changes in hepatic insulin concentrations provides a dynamic link to substrate availability. (ii) As an autocrine/paracrine factor, IGFBP-1 appears to play a crucial role in the female reproductive system and, in particular, the sequence of events leading from ovulation to implantation to successful fetal outcom

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“(2000) demonstrated that oral administration of estradiol increases circulating levels of IGFBP-1, and it is also up-regulatedduring catabolic states, such as insulin-dependent diabetes mellitus and after stress conditions in mammals and fish (Lee et al., 1997; Kelley et al., 2001).”
Background
Duplication and Diversification of the Hypoxia-Inducible IGFBP-1 Gene in Zebrafish
Kamei, H., Lu, L., Jiao, S., Li, Y., Gyrup, C., Laursen, L. S., Oxvig, C., Zhou, J., & Duan, C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003091 · Cited by 112
“In the L-domain of mammalian IGFBP-1, there is a proline, glutamine, serine, and threonine (PEST) motif, known to contribute to its susceptibility to proteolysis [15].”
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Evolution of Ancient Functions in the Vertebrate Insulin-Like Growth Factor System Uncovered by Study of Duplicated Salmonid Fish Genomes
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“…al. 2002, 2006; Ren et al. 2008), whereas IGFBP-1 and -2 generally inhibit the growth-promoting functions of IGF in both mammals and fish (Gockerman et al. 1995; Lee et al. 1997; Duan et al. 1999; Firth and Baxter 2002; Kiepe et al. 2002; Kajimura et al. 2005; Zhou et al. 2008; Kamei et al. 2008).”
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Sustained Antidiabetic Effects of a Berberine-Containing Chinese Herbal Medicine Through Regulation of Hepatic Gene Expression
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Elevated Serum Levels of Free Insulin-Like Growth Factor I in Polycystic Ovary Syndrome1
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Self-citation
Massive hepatic apoptosis associated with TGF-β1 activation after Fas ligand treatment of IGF binding protein-1–deficient mice
Leu, J. I.-J., Crissey, M. A. S., & Taub, R. A. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200316712 · Cited by 108
Developmental response to hypoxia
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“minute availability of free IGF-I in the circulation (6, 7).”
BackgroundSelf-citation
Regulation of Insulin-Like Growth Factor Binding Protein-1 Promoter Activity by FKHR and HOXA10 in Primate Endometrial Cells1
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“Insulin-like growth factor binding protein-1 (IGFBP-1) is expressed primarily in the liver, kidney, decidualized endometrium, and luteinizing granulosa cells [1].”
Background
Paternal effect on embryo quality in diabetic mice is related to poor sperm quality and associated with decreased glucose transporter expression
Kim, S. T., & Moley, K. H. (2008) · Reproduction · doi:10.1530/rep-08-0167 · Cited by 107
“Oxidation of lipids, proteins, and other macromolecules such as DNA occurs during the development of diabetes (Ohkawa et al. 1979), and mitochondrial DNA mutations have also been reported in diabetic tissues, suggesting oxidative stress-related mitochondrial damage (Lee et al. 1997).”
Background
The Role of Endocrine Insulin-Like Growth Factor-I and Insulin in Breast Cancer
Lann, D. E., & LeRoith, D. (2008) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-008-9100-x · Cited by 104
“Hyperinsulinemia, the hallmark of type 2 diabetes, can lead to the repression of IGFBP-1 hepatic production and therefore decreased release into circulation [80, 81].”
Background
Serum levels of C‐peptide, IGFBP‐1 and IGFBP‐2 and endometrial cancer risk; Results from the European prospective investigation into cancer and nutrition
Cust, A. E., Allen, N. E., Rinaldi, S., Dossus, L., Friedenreich, C. M., Olsen, A., Tjønneland, A. M., Overvad, K., Clavel‐Chapelon, F., Boutron‐Ruault, M., et al. (2007) · International Journal of Cancer · doi:10.1002/ijc.22578 · Cited by 101
“Lower IGFBP-1 and IGFBP-2 levels may lead to increased IGF-I bioavailability in the circulation and endometrial tissue,(2,11,13,41,43) because contrary to IGFBP-3, IGFBP-1 and IGFBP-2 can combine with IGF-I to form a small complex that can cross the capillary endothelium and prevent IGF-I receptor binding.(11,12,14,40…”
BackgroundResult
Changes in the circulating IGF system during short-term fasting and refeeding in rats
Frystyk, J., Delhanty, P. J. D., Skjærbæk, C., et al. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.2.e245 · Cited by 102
“In fact, because the liver is the primary source of circulating IGFBP-1, serum IGFBP-1 has been suggested to reflect portal rather than peripheral insulin levels (3, 15).”
BackgroundInfluential
Comparative Biology of the IGF System in Endometrium, Decidua, and Placenta, and Clinical Implications for Foetal Growth and Implantation Disorders
Nayak, N. R., & Giudice, L. C. (2003) · Placenta · doi:10.1053/plac.2002.0906 · Cited by 101
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Relationships between serum IGF1 levels, blood pressure, and glucose tolerance: an observational, exploratory study in 404 subjects
Colao, A., Somma, C. D., Cascella, T., Pivonello, R., Vitale, G., Grasso, L. F. S., Lombardi, G., & Savastano, S. (2008) · European Journal of Endocrinology · doi:10.1530/eje-08-0201 · Cited by 101
Hepatic IGFBP1 is a prosurvival factor that binds to BAK, protects the liver from apoptosis, and antagonizes the proapoptotic actions of p53 at mitochondriaPreprint
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“However, many recent studies have documented that these IGFBP proteins also have important intracellular functions that are independent of, and unrelated to, their secretion and interactions with the IGFs (Lee et al. 1997; Duan and Xu 2005).”
BackgroundInfluential
Oxidative stress occurs early in Down syndrome pregnancy: A redox proteomics analysis of amniotic fluid
Perluigi, M., di Domenico, F., Fiorini, A., Cocciolo, A., Giorgi, A., Foppoli, C., Butterfield, D. A., Giorlandino, M., Giorlandino, C., Eugenia Schininà, M., et al. (2011) · PROTEOMICS – Clinical Applications · doi:10.1002/prca.201000121 · Cited by 97
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Background
Paracrine actions of insulin-like growth factors and IGF binding protein-1 in non-pregnant human endometrium and at the decidual–trophoblast interface
Giudice, L. C., Mark, S., & Irwin, J. C. (1998) · Journal of Reproductive Immunology · doi:10.1016/s0165-0378(98)00018-7 · Cited by 97
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“Circulating levels of IGFBP-1 are generally inversely related to those of insulin after meals, and insulin treatment inhibits IGFBP-1 both at the mRNA and protein levels (Lee et al., 1993, 1997).”
Background
The role of IGF‐I and its binding proteins in the development of type 2 diabetes and cardiovascular disease
Ezzat, V., Duncan, E. R., Wheatcroft, S. B., & Kearney, M. T. (2007) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2007.00709.x · Cited by 91
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Authors: Lee, P. D. K., Giudice, L. C., Conover, C. A., & Powell, D. R.
Affiliations: Mayo Clinic (US)
ORCID: Lee, P. D. K.
Giudice, L. C.
Conover, C. A.
Powell, D. R.
Venue: Experimental Biology and Medicine
Publisher: Frontiers Media SA
Published: 1997-12-01
Volume: 216
Issue: 3
Pages: 319-357
ISSN: 0071-3384 (ISSN-L)
1535-3702
1535-3699
DOI: 10.3181/00379727-216-44182
OpenAlex: W2036466897
Cited by: 523
References: 0
Citations by year: 2026: 1 · 2025: 4 · 2024: 8 · 2023: 4 · 2022: 6 · 2021: 10 · 2020: 8 · 2019: 11 · 2018: 10 · 2017: 19 · 2016: 16 · 2015: 16 · 2014: 11 · 2013: 17 · 2012: 14
FWCI: 16.84
Type: journal article
Language: en
Open access: closed
Locations: Experimental Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Growth Hormone and Insulin-like Growth Factors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
Health Sciences › Medicine › Hepatology › Liver physiology and pathology
Keywords: IGFBP-1, insulin-like growth factor, IGF binding, cysteine-rich region, protease cleavage, integrin binding, phosphorylation sites, IGFBP-3, chromosome 7, glucose metabolism, glucocorticoids, cyclic AMP, tissue-specific gene expression
MeSH terms: Amino Acid Sequence, Animals, Bone and Bones, Cartilage, Connective Tissue, Female, Gene Expression Regulation, Genitalia, Female, Genitalia, Male, Humans, Kidney, Liver, Male, Molecular Sequence Data, Organ Specificity, Substrate Specificity, Insulin-Like Growth Factor Binding Protein 1, Evolution, Molecular

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Insulin-like Growth Factor Binding Protein-1: Recent Findings and New Directions

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