{"title":"Comparison studies of IGFBP-5 binding to osteoblasts and osteoblast-derived extracellular matrix","authors":"Dennis L. Andress","doi":"10.1016/0955-2235(95)00008-9","DOIUrl":"10.1016/0955-2235(95)00008-9","url":null,"abstract":"<div><p>Recent studies have identified a specific membrane protein in osteoblast-like cells which binds intact and carboxy-truncated IGFBP-5 with high affinity. The purpose of the present study was to evaluate the IGFBP-5 binding properties of osteoblast-derived extracellular matrix (ECM), with special interest in determining whether ECM proteoglycans were necessary for IGFBP-5 binding. Neonatal mouse osteoblasts and the ECM of these cells both bound intact [<sup>125</sup>I]IGFBP-5 and [<sup>125</sup>I]IGFB_-5<sup>1–169</sup>, though the ECM bound both forms with lower affinity when compared to their cellular binding. Treatment of the ECM with heparinase or chondroitinase, to remove glycosaminoglycan (GAG) side-chains of proteoglycans, resulted in 20–34% enhanced binding of intact [<sup>125</sup>I]IGFBP-5 and a 92–100% enhancement of [<sup>125</sup>I]IGFBP-5<sup>1–169</sup> binding. Similar enzymatic treatment of osteoblast monolayers had no effect on the binding of either form of [<sup>125</sup>I]IGFBP-5. These results indicate that GAGs within ECM secreted by neonatal mouse osteoblasts do not mediate the binding of IGFBP-5. This study also shows that intact and carboxy-truncated IGFBP-5 preferentially bind to the osteoblast surface, but that removal of GAGs from osteoblast-derived ECM can increase IGFBP-5 localization to this pericellular space, particularly the carboxy-truncated form of IGFBP-5.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 337-344"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(95)00008-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19785984","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The role of growth factors in preimplantation development","authors":"Peter L. Kaye , Mark B. Harveyt","doi":"10.1016/0955-2235(95)00001-1","DOIUrl":"10.1016/0955-2235(95)00001-1","url":null,"abstract":"<div><p>It has become clear that the mammalian embryo participates in a complex dialogue with the maternal physiology. The language of the dialogue is growth factor signalling. The embryo expresses receptors for insulin, IGFs, GH, EGF and cytokines including LIF, and CSFs; whilst ligands are secreted by the supporting tissues of the oviduct and uterus, and in some cases, the embryo itself. In the preimplantation period when the embryo is travelling to the uterus and passing through its first differentiation, these ligands affect embryonic physiology, apparently in ways that optimise developmental potential and synchronise embryonic and maternal physiologies. It is not yet clear in most cases whether this is by autocrine, paracrine or endocrine mode. In the crucial peri-implantation phase the embryo is preparing to invade the maternal system for which extensive uterine remodelling is necessary. A model is proposed in which a cascade of growth factor activities, orchestrated by the ovarian steroid patterns, choreographs the biochemical players (ECM proteinases and their inhibitors) which initiate this activity.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 1","pages":"Pages 1-24"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(95)00001-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19688771","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Moira S. Lewitt , Fergus P. Scott , Nicole M. Clarke , Robert C. Baxter
{"title":"Developmental regulation of circulating insulin-like growth factor-binding proteins in normal pregnancies and in pre-eclampsia","authors":"Moira S. Lewitt , Fergus P. Scott , Nicole M. Clarke , Robert C. Baxter","doi":"10.1016/0955-2235(95)00030-5","DOIUrl":"10.1016/0955-2235(95)00030-5","url":null,"abstract":"<div><p>The insulin-like growth factors (IGFs) and their binding properties (IGFBPs) are believed to play important roles in the growth and development of the human fetus. They have been implicated in the pathophysiology of pre-eclampsia. In this study we have characterized the developmental regulation, in normal and pre-eclamptic pregnancies, of IGFs and IGFBPs in maternal serum, neonatal serum and amniotic fluid. In neonatal cord serum IGFBP-1, -2 and -6 decreased with increasing gestational age. In contrast, the ternary complex and its components, IGF-I, IGFBP-3 and ALS increased with gestation. We show that while ALS is an important limiting factor for ternary complex formation in the fetal circulation, there is a fraction of IGFBP-3 which is unable to form this complex. IGFs and IGFBPs in the maternal and fetal circulation were similar in normal and pre-eclamptic pregnancies.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 475-480"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(95)00030-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786569","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Eric Neau , Daniel Chambéry , Ghislaine Schweizer-Groyer , Françoise Cadepond , Nicole Jibard , André Groyer
{"title":"Multiple liver-enriched trans-acting factors interact with the glucocorticoid- (GRU) and cAMP-(CRU) responsive units within the h-IGFBP-1 promoter","authors":"Eric Neau , Daniel Chambéry , Ghislaine Schweizer-Groyer , Françoise Cadepond , Nicole Jibard , André Groyer","doi":"10.1016/0955-2235(95)00039-9","DOIUrl":"10.1016/0955-2235(95)00039-9","url":null,"abstract":"<div><p>In response to hormonal control, serum concentrations of insulin-growth factor-binding protein-1 (IGFBP-1) may vary as much as 10-fold, owing to strict control of its gene's expression in hepatocytes. IGFBP-1 gene transcription is increased by gluco-corticoids and cAMP and inhibited by insulin. The effect of insulin is dominant since it suppresses constitutive and both glucocorticoid- and cAMP-stimulated transcription. Close examination of the human (h) IGFBP-1 promoter sequences showed that the glucocorticoid (GRE, nt −88 to −102) and cAMP (CRE, nt −259 to −264) response elements are 5′-flanked by an A/T-rich imperfect palindrome (nt −102 to −117 and −265 to −285, respectively). These A/T-rich motifs are putative <em>cis</em>-elements for liver-enriched <em>trans</em>-acting factors.</p><p>Competition experiments in electrophoretic mobility shift assay were carried out using rat liver nuclear extracts and a set of synthetic oligonucleotides designed from hIGFBP-1 Glucorticoid and cAMP Response Units (GRU and CRU), the rat transthyretin HNF3 <em>cis</em>-element and the ‘D-site’ of the mouse albumin promoter.</p><p>The nucleotide motifs located between nt −108 and −121 of the GRU, interacted with the HNF3 family of <em>rans</em>-acting factors (α,β,γ), whereas those encompassing nt −181 to −104 bound DBP and/or nuclear proteins sharing similar sequence specificity (i.e. from the C/EBP family of bZIP proteins). We have also shown that the hIGFBP-1-GRE binds glucocorticoid receptor homodimers.</p><p>In the case of the CRU, the <em>cis</em>-elements located between nt −249 and −285 bound DBP and/or nuclear proteins sharing similar sequence specificities. In addition, the nucleotide stretch lying between nt −256 and −275 was able to interact with the HNF3 family of <em>trans</em>-acting factors.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 103-117"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(95)00039-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ch. Schmid, I. Schläpfer, M.A. Gosteli-Peter, E.R. Froesch, J. Zapf
{"title":"Expression, effects, and fate of IGFBP-5 are different in normal and malignant osteoblastic cells","authors":"Ch. Schmid, I. Schläpfer, M.A. Gosteli-Peter, E.R. Froesch, J. Zapf","doi":"10.1016/0955-2235(95)00037-2","DOIUrl":"10.1016/0955-2235(95)00037-2","url":null,"abstract":"<div><p>Normal osteoblasts from newborn rat calvaria and human osteosarcoma (Saos-2) cells express IGFBP-5 mRNA. IGF I increases IGFBP-5 mRNA levels in both cell types, whereas retinoic acid stimulates IGFBP-5 mRNA expression in calvaria but suppresses it in Saos-2 cells. IGFBP-5 mRNA expression is stimulated in normal bone cells by parathyroid hormone. 30 nM IGFBP-5 stimulates <sup>3</sup>H-thymidine incorporation in calvaria (which produce IGF I contributing to basal proliferation in serum-free medium) but not in Saos-2 cells which produce little IGF I and IGF II. Among the 5 rhIGFBPs tested (IGFBP-2 to -6), only IGFBP-5 stimulates DNA synthesis in calvaria cells, and only IGFBP-6 in Saos-2 cells.</p><p>RhIGFBP-5 displays a short half-life (∼30 min) in serum-free medium of calvaria cells and a long half-life (∼15 h) in the medium of Saos-2 cells. Fragments of 20 and 14 kDa accumulate in the media of both cell types. Intact (31 kDa) IGFBP-5 is associated and remains with the extracellular matrix of mature calvaria osteoblasts but not of Saos-2 cells.</p><p>Among the IGFBPs produced IGFBP-5 is unique with regard to its marked affinity to matrix of normal bone cells, its short half-life when released, and its stimulatory effects on DNA synthesis.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 167-173"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(95)00037-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786812","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Growth factors in CNS repair and regeneration","authors":"Ann Logan , James J Oliver , Martin Berry","doi":"10.1016/0955-2235(94)00008-9","DOIUrl":"10.1016/0955-2235(94)00008-9","url":null,"abstract":"<div><p>Traumatic central nervous system (CNS) injury is a significant clinical problem in the developed world. After injuries that penetrate into either the mature brain or spinal cord, damaged neurons initially begin to regrow, but this regeneration is aborted as a fibrotic scar is laid down within the wound. Reconnection of severed neuronal pathways does not occur. Functional recovery from such injuries is therefore poor and morbidity severe, particularly for those patients with spinal cord damage. Although palliative measures are available to improve the quality of life, there is no accepted treatment to restore impaired sensory or motor function, so patients remain significantly and permanently debilitated. However, the rapid recent advances that have been made in our understanding of the underlying cellular and trophic pathology of such injuries offer the potential for development of novel therapies to control scarring, enhance neuron survival and stimulate axon regeneration, thereby promoting functional recovery.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 4","pages":"Pages 379-391, 393-405"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(94)00008-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18780285","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Regulatory issues in clinical applications of cytokines and growth factors","authors":"Karen D. Weiss, Jay P. Siegel, Theresa L. Gerrard","doi":"10.1016/0955-2235(94)90006-X","DOIUrl":"10.1016/0955-2235(94)90006-X","url":null,"abstract":"<div><p>This article describes the drug approval process at the Center for Biologics Evaluation and Research (CBER), FDA, for cytokines and growth factors that would be licensed for clinical use in the U.S.A. CBER is responsible for setting policy, providing guidance to industry and to academic investigators as they develop and evaluate these new products, and for recommendations about the approvability of license applications. Product development generally parallels clinical development, and the expectations at each stage of the IND (Investigational New Drug) process are discussed. FDA involvement continues beyond licensure to the post marketing phase. The goal is to assure that new cytokines and growth factors are safe and effective and available in a timely manner.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 2","pages":"Pages 213-222"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(94)90006-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18916000","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Growth factors in mouse primordial germ cell migration and proliferation","authors":"Massimo De Felici, Maurizio Pesce","doi":"10.1016/0955-2235(94)90001-9","DOIUrl":"10.1016/0955-2235(94)90001-9","url":null,"abstract":"<div><p>Information obtained mainly from in vitro culture studies and genetic analysis of mouse mutants <em>White</em> spotting and <em>Steel</em> indicate a pivotal role of growth factors in the development of mouse primordial germ cells (PGCs). While stem cell factor (SCF) and TGFβ1 seem to have a role in PGC migration (as an adhesion factor and a chemoattractant, respectively), the former is certainly required for PGC survival <em>in vitro</em> and probably <em>in vivo</em> as well. Recent findings suggest that the mechanism by which SCF supports PGC survival is by preventing PGC apoptosis. A similar action appears to be exerted by leukemia inhibitory factor (LIF), a further growth factor influencing PGC growth in culture.</p><p>PGC proliferation seems to be mainly induced by cAMP dependent mechanisms, but futther investigations are needed to clarify the interrelationships among the different molecular pathways activated by SCF, LIF, cAMP and other putative PGC growth factors (i.e. bFGF). Stimulation of long-term proliferation of PGCs, leading to derivation of ES-like cells (embryonal germ cells) obtained by using a combination of growth factors (bFGF, SCF and LIF), opens new intriguing perspectives for such studies and transgenic technology.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 2","pages":"Pages 135-143"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(94)90001-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18916798","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Are fibroblast growth factors regulators of myogenesis in vivo?","authors":"Bradley B. Olwin, Kevin Hannon, Arthur J. Kudla","doi":"10.1016/0955-2235(94)90002-7","DOIUrl":"10.1016/0955-2235(94)90002-7","url":null,"abstract":"<div><p>Recent advances in understanding of skeletal muscle differentiation implicate fibroblast growth factors (FGFs) as regulators of myogenesis; however, the identity and actions of factors that repress myogenesis <em>in vivo</em> remain to be established. This review will focus on the fibroblast growth factor family and the evidence for its role in regulating myogenesis in culture and <em>in vivo</em>.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 2","pages":"Pages 145-158"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(94)90002-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18916799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}