Progress in growth factor research最新文献

{"title":"Periconceptual undernutrition resets plasma IGFBP levels and alters the response of IGFBP-1, IGFBP-3 and IGF-1 to subsequent maternal undernutrition in fetal sheep","authors":"Brian W. Gallaher,&nbsp;Bernhard H. Breier,&nbsp;Jane E. Harding,&nbsp;Peter D. Gluckman","doi":"10.1016/0955-2235(96)00010-5","DOIUrl":"10.1016/0955-2235(96)00010-5","url":null,"abstract":"<div><p>Maternal undernutrition inhibits fetal growth and alters circulating levels of insulin-like growth factors (IGFs) and IGF binding proteins (IGFBPs). This study investigates whether the fetal IGF axis could be reprogrammed by maternal undernutrition and hence be a potential contributing factor to changes in fetal and postnatal metabolism. Ewes were either fed <em>ad lib.</em> or undernourished from day −60 to day 30 of gestation, and then both groups were fed <em>ad lib</em>. These groups were further divided at day 105, either being fed <em>ad lib</em> or undernourished until day 115. Fetal blood samples were obtained at day 105 and day 115. IGFBP-1 and IGFBP-3 levels were lower at day 105 in the periconceptually undernourished fetuses. Levels of IGFBP-1 were increased and IGFBP-3, IGFBP-4, IGF-1, glucose and insulin were reduced at day 115 after undernutrition. The degree of change in IGFBP-1, IGFBP-3 and IGF-I between day 105 and day 115 was greater in fetuses receiving low periconceptual nutrition. These results indicate that periconceptual undernutrition is able to reprogramme the fetal IGF axis such that the responses of IGF-I and the IGFBPs to undernutrition in late gestation are markedly altered.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 189-195"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(96)00010-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19785566","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":"Circulating and ovarian IGF binding proteins: Potential roles in normo-ovulatory cycles and in polycystic ovarian syndrome","authors":"L.C. Giudice ,&nbsp;H.J.H.M. ban Dessel ,&nbsp;N.A. Cataldo ,&nbsp;Y.A. Chandrasekher ,&nbsp;O.W.S. Yap ,&nbsp;B.C.J.M. Fauser","doi":"10.1016/0955-2235(95)00016-X","DOIUrl":"10.1016/0955-2235(95)00016-X","url":null,"abstract":"<div><p>IGFs function as co-gonadotropins in the ovary, facilitating steroidogenesis and follicle growth. IGFBP-1 to -5 are expressed in human ovary and mostly inhibit IGF action in <em>in vitro</em> ovarian cell culture systems. In the clinical disorder of polycystic ovarian syndrome (PCOS), which is characterized by hyperandrogenemia, polycystic ovaries and anovulation, follicles have a higher androgen : estradiol (A : E₂) content and growth is arrested at the small antral stage. In the PCOS follicle, follicle stimulating hormone (FSH) and IGF levels are in the physiologic range, and even in the face of abundant androstenedione (AD) substrate, aromatase activity and E₂ production are low. When PCOS granulosa are removed from their ovarian environment, they respond normally or hyperrespond to FSH. It has been postulated that an inhibitor of IGF's synergistic actions with FSH on aromatase activity may be one (or more) of the IGFBPs, which contributes to the arrested state of follicular development commonly observed in this disorder. High levels of IGFBP-2 and IGFBP-4 are present in follicular fluid (FF) from androgen-dominant follicles (FF_a) from normally cycling women and in women with PCOS. This is in marked contrast to the near absence of these IGFBPs in estrogen-dominant FF (FF_e), determined by Western ligand blotting. Regulation of granulosa-derived IGFBPs is effected by gonadotropins and insulin-like peptides. In addition, an IGFBP-4 metallo-serine protease is present in FF_e, but not in FF_a in ovaries from normally cycling women and those with PCOS, although the IGFBP-4 protease is present in PCOS follicles hyperstimulated for <em>in vitro</em> fertilization. Recent studies demonstrate that IGF-II in FF_e is higher than in FF_a, whereas IGF-I, IGFBP-3 and IGFBP-1 levels do not differ, underscoring the importance of local IGF-II production by the granulosa and the importance of IGFBP-4 and IGFBP-2 in regulation of IGF-II action within the follicle during its developmental pathway as an E₂- or A-dominant follicle. In the androgen-treated female-to-male transsexual (TSX) model for PCOS, IGF-I, IGF-II, IGFBP-3 and IGFBP-1 levels do not differ in A-dominant follicles in TSX ovaries, compared to A-dominant follicles from normally cycling women. Furthermore, TSX follicles do not contain IGFBP-4 protease, similar to A-dominant follicles from normally cycling women and those with PCOS. In summary, A-dominant follicles contain physiologic levels of IGF-I and IGF-II, high levels of inhibitory IGFBPs and low levels of IGFBP-4 protease, thereby favoring low levels of bioavailable IGFs in these follicles. In contrast, maximal IGF bioavailability is maintained in the E-dominant follicle by increased IGF-II production, decreased IGFBP production and increased IGFBP-degradation.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 397-408"},"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)00016-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19785990","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Proceedings of the third international symposium on IGF binding proteins","authors":"Kerstin Hall,&nbsp;Werner F. Blum","doi":"10.1016/0955-2235(96)88808-9","DOIUrl":"https://doi.org/10.1016/0955-2235(96)88808-9","url":null,"abstract":"","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Page 77"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(96)88808-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138274017","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":"Biochemical and mitogenic properties of the heparin-binding growth factor HARP","authors":"Khalid Laaroubi,&nbsp;Francis Vacherot,&nbsp;Jean Delbé,&nbsp;Daniéle Caruelle,&nbsp;Denis Barritault,&nbsp;José Courty","doi":"10.1016/0955-2235(95)00002-X","DOIUrl":"10.1016/0955-2235(95)00002-X","url":null,"abstract":"<div><p>Heparin affin regulatory peptide (HARP), also called Pleiotrophin (PTN), is a polypeptide that displays a high affinity for heparin and that shares approximately 50% sequence homology with Midkine (MK). According to this structural homology, these two molecules constitute a new family of heparin-binding proteins. The biological properties of HARP and MK remain largely a subject of debate. Both proteins have been described as neurite outgrowth promoting agents whereas until recently the mitogenic activity has been controversial. The aim of this review is to summarize the information on HARP with special focus on the recent data relating to its mitogenic properties.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 1","pages":"Pages 25-34"},"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)00002-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19687023","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 fibroblast growth factor-2 (FGF-2) in hematopoiesis","authors":"Michele Allouche ,&nbsp;Andreas Bikfalvi","doi":"10.1016/0955-2235(95)00041-0","DOIUrl":"10.1016/0955-2235(95)00041-0","url":null,"abstract":"<div><p>Basic fibroblast growth factor (bFGF or FGF-2) is an angiogenic and pleiotropic growth factor involved in the proliferation and differentiation of numerous cell types. It is expressed mostly in tissues of mesoderm and neuroectoderm origin, and is thought to play an important role in the mesoderm induction. Although hematopoietic cells derive from the mesoderm, relatively few studies have, until recently, addressed the role of FGF-2 in hematopoiesis. FGF-2 is expressed in cells of the bone marrow including stromal cells, and possibly cells from several hematopoietic cell lineages. It is stored in the bone marrow extra-cellular matrix and released by enzymes such as heparanase, plasmin, or phospholipase C and D. FGF-receptors (FGF-Rs) are expressed in leukemic cell lines and in hematopoietic cells. FGF-2 positively regulates hematopoiesis, by acting on stromal cells, on early and committed hematopoietic progenitors, and possibly on some mature blood cells. The action of FGF-2 is most likely indirect since its action, on megakaryocytopoiesis for example, is abrogated by anti-IL6 antibodies. It synergizes with hematopoietic cytokines, or antagonizes the negative regulatory effects of TGF-β Taken together, these results demonstrate that FGF-2 is a potent hematopoietic growth factor that is likely to play an important role in physiological and pathological hematopoiesis.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 1","pages":"Pages 35-48"},"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)00041-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19687024","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":"Genetic ablation of IGFBP-2 suggests functional redundancy in the IGFBP family","authors":"John E. Pintar ,&nbsp;Alwin Schuller ,&nbsp;Joseph A. Cerro ,&nbsp;Maureen Czick ,&nbsp;Anoop Grewal ,&nbsp;Barrett Green","doi":"10.1016/0955-2235(95)00029-1","DOIUrl":"10.1016/0955-2235(95)00029-1","url":null,"abstract":"<div><p>Gene targeting allows mutations to be introduced selectively into any mouse locus of interest. This approach has already been used to demonstrate that insulin-like growth factor (IGF) peptides and receptors are required <em>in vivo</em> for normal prenatal growth. One of the IGFBP genes, IGFBP-2, has also been disrupted using gene targeting, and homozygous null BP-2 mice are characterized by a decreased spleen size most apparent during early postnatal stages and increased adult circulating levels of several other IGFBPs. These alterations are considered less dramatic than the phenotypes initially predicted based on the fetal IGFBP-2 expression pattern, although several physiological paradigms can be envisioned that will provide additional tests for specific aspects of IGFBP function. Since all six IGFBP genes are expressed during prenatal rodent development, as well as in adult tissues, the IGFBP-2 null phenotype must also be compared with genetic ablations involving members of other gene families and in the context of the other IGFBP expression patterns in rodent embryonic, extraembryonic, and uterine tissues.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 437-445"},"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)00029-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786565","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":"A novel DNA/protein complex interacts with the insulin-like growth factor binding protein-1 (IGFBP-1) insulin response sequence and is required for maximal effects of insulin and glucocorticoids on promoter function","authors":"T. Unterman,&nbsp;D. Oehler,&nbsp;H. Ngyuen,&nbsp;P. Sengupta,&nbsp;R. Lacson","doi":"10.1016/0955-2235(95)00020-8","DOIUrl":"10.1016/0955-2235(95)00020-8","url":null,"abstract":"<div><p>Glucocorticoids stimulate and insulin inhibits hepatic production of IGFBP-1 at the level of gene transcription. We previously identified contiguous insulin and glucocorticoid response sequences in the proximal rat IGFBP-1 promoter. This insulin response sequence (IRS) is palindromic (<em>CAAAACAA</em>A<em>TTATTTTG</em>) and each half resembles an IRS in the phosphoenolpyruvate carboxykinase (PEPCK) gene. We have reported that both the IGFBP-1 and PEPCK IRSs bind hepatocyte nuclear factor-3 (HNF-3) proteins [1]. We now report that IRSs from the IGFBP-1 and PEPCK, as well as an IRS which also binds HNF-3 in the rat tyrosine aminotransferase (TAT) gene, also interact with another DNA/protein complex in gel shift studies. Further, methylation interferences studies, gel shift and transient transfection studies with site-specific mutations identified a single base in the first half of the IRS that is critical both for interactions with proteins in this complex, and for maximal effects of insulin and glucocorticoids, on promoter function. Of note, a 250-fold excess of an oligo containing a C/EBP binding site (but not other AT-rich sequences) inhibits the formation of this complex in gel shift assays. Nevertheless, interactions with this C/EBP site are negligible at lower titers (≤ 100-fold excess), and antibodies against known C/EBP proteins do not react with this complex. Similarly, preincubation with CHOP, a truncated member of the C/EBP family which contains a β-leucine zipper domain, does not prevent or alter the mobility of this novel DNA/protein complex, indicating that components of this complex do not form heterodimers with β-ZIP proteins. We conclude that HNF-3 proteins and this novel C/EBP-related DNA/protein complex may play an important role in mediating interactions between glucocorticoids and insulin in the regulation of IGFBP-1 and perhaps multiple hepatic genes.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 119-129"},"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)00020-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786807","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":"Dexamethasone stimulation of rat insulin-like growth factor binding protein-1 (IGFBP-1) promoter activity involves the interaction of multiple transcription factors","authors":"Dae-Shik Suh,&nbsp;Yuehua Zhou,&nbsp;Guck T. Ooi,&nbsp;Matthew M. Rechler","doi":"10.1016/0955-2235(95)00021-6","DOIUrl":"10.1016/0955-2235(95)00021-6","url":null,"abstract":"<div><p>Using an improved procedure for transient transfection of H4-II-E rat hepatoma cells, we characterized the <em>cis</em> elements in the proximal promoter of the rat insulin-like growth factor binding protein-1 (rat IGFBP-1) gene that are required for basal (unstimulated) and dexamethasone-stimulated promoter activity. Three sites are required for optimal basal promoter activity: an AP-2 site (nt −286 to −293), the M4 region of the insulin response element (nt −108 to −99), and a hepatocyte nuclear factor-1 (HNF-1) site (nt −62 to −50). In addition to the glucocorticoid response element (nt −91 to −77), participation of two of three accessory sites is required for optimal stimulation by dexamethasone: the M4 and HNF-1 sites, and a third site located between nt −252 and −236. Further study will focus on how the interactions of tissue-specific and hormonally-responsive transcription factors are integrated.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 131-140"},"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)00021-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786808","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":"Bibliographic update","authors":"","doi":"10.1016/0955-2235(95)90002-0","DOIUrl":"10.1016/0955-2235(95)90002-0","url":null,"abstract":"","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 1","pages":"Pages 49-76"},"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)90002-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19687025","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":"Insulin-like growth factors (IGF) and IGF binding proteins in children with chronic renal failure","authors":"Burkhard Tönshoff,&nbsp;Werner F. Blum ,&nbsp;Otto Mehls","doi":"10.1016/0955-2235(96)00003-8","DOIUrl":"10.1016/0955-2235(96)00003-8","url":null,"abstract":"<div><p>The pathomechanism of growth retardation and catabolism in children with chronic renal failure (CRF) is multifactorial. Recent evidence indicates that in particular disturbances of the somatotropic hormone axis play an important pathogenic role. In preterminal CRF serum insulin-like growth factor (IGF)-I and IGF-II levels are normal, while in end-stage renal disease (ESRD), IGF-I levels are slightly decreased and IGF-II levels slightly increased. In view of the prevailing elevated growth hormone levels in ESRD, these serum IGF-I levels appear as inadequately low. Indeed, there is both clinical and experimental evidence for a decreased hepatic IGF-I production rate in CRF. This hepatic insensitivity to the action of GH is partially owing to a reduced GH receptor expression. The action and metabolism of IGFs are modulated by specific high-affinity IGF binding proteins (IGFBPs), which bind ∼99% of circulating IGF. IGFBP-1, IGFBP-2, and low molecular weight IGFBP-3 fragments are increased in CRF serum in relation to the degree of renal dysfunction. Both decreased renal filtration, in particular of low molecular weight IGFBP-3 fragments, and increased hepatic production of IGFBP-1 and -2 contribute to high IGFBP serum levels. Experimental and clinical evidence suggests that these excessive high-affinity IGFBPs in CRF serum inhibit IGF action on target tissues by competition with the type 1 IGF receptor for IGF binding.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"6 2","pages":"Pages 481-491"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0955-2235(96)00003-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19786431","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}