Progress in growth factor research最新文献_第7页

Are fibroblast growth factors regulators of myogenesis in vivo? 成纤维细胞生长因子是体内肌生成的调节因子吗?

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-15 DOI: 10.1016/0955-2235(94)90002-7

Bradley B. Olwin, Kevin Hannon, Arthur J. Kudla

引用次数: 47

Bibliographic update: Transforming growth factors 书目更新:转化生长因子

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-15 DOI: 10.1016/0955-2235(94)90012-4

引用次数: 0

Serine/threonine kinase receptors 丝氨酸/苏氨酸激酶受体

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-27 DOI: 10.1016/0955-2235(94)90017-5

Peter ten Dijke , Petra Franzén , Hidetoshi Yamashita , Hidenori Ichijo , Carl-Henrik Heldin , Kohei Miyazono

引用次数: 87

Cytokine control of cell motility: Modulation and mediation by the extracellular matrix 细胞因子对细胞运动的控制:细胞外基质的调节和调解

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-15 DOI: 10.1016/0955-2235(94)90007-8

Seth L. Schor

引用次数: 45

Vascular endothelial growth factor and its receptors 血管内皮生长因子及其受体

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-27 DOI: 10.1016/0955-2235(94)90019-1

Gera Neufeld , Shoshana Tessler , Hela Gitay-Goren , Tzafra Cohen , Ben-Zion Levi

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引用次数: 0

Regulation of cell proliferation and growth by angiotensin II 血管紧张素II对细胞增殖和生长的调控

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-15 DOI: 10.1016/0955-2235(94)90004-3

William R. Huckle , H.Shelton Earp

{"title":"Regulation of cell proliferation and growth by angiotensin II","authors":"William R. Huckle , H.Shelton Earp","doi":"10.1016/0955-2235(94)90004-3","DOIUrl":"10.1016/0955-2235(94)90004-3","url":null,"abstract":"<div><p>The peptide hormone angiotensin II (AngII) has clearly defined physiologic roles as a regulator of vasomotor tone and fluid homeostasis. In addition AngII has trophic or mitogenic effects on a variety of target tissues, including vascular smooth muscle and adrenal cells. More recent data indicate that AngII exhibits many characteristics of the ‘classical’ peptide growth factors such as <span><math><mtext>EGF</mtext><mtext>TGFα</mtext></math></span>, PDGF and IGF-1. These include the capacity for local generation (‘autocrine or paracrine’ action) and the ability to stimulate tyrosine phosphorylation, to activate MAP kinases and to increase expression of nuclear proto-oncogenes. The type 1 AngII receptor, which is responsible for all known physiologic actions of AngII, has been cloned. Activation of this receptor leads to elevated phosphoinositide hydrolysis, mobilization of intracellular Ca<sup>2+</sup> and diacylglycerol, and activation of <span><math><mtext>Ca</mtext><msup><mi></mi><mn>2+</mn></msup><mtext>calmodulin</mtext></math></span> and <span><math><mtext>Ca</mtext><msup><mi></mi><mn>2+</mn></msup><mtext>phospholipid</mtext><mtext>-</mtext><mtext>dependent</mtext></math></span><span><math><mtext>Ser</mtext><mtext>Thr</mtext></math></span> kinases, as well as Ca<sup>2+</sup> regulated tyrosine kinases. The existence of other AngII receptor subtypes has been postulated, but the function(s) of these sites remains unclear. In vascular smooth muscle, AngII can promote cellular hypertrophy and/or hyperplasia, depending in part on the patterns of induction of secondary factors that are known to stimulate (PDGF, IGF-1, basic FGF) or inhibit (TGF-β) mitosis. Together, these findings have suggested that AngII plays important roles in both the normal development and pathophysiology of vascular, cardiac, renal and central nervous system tissues.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 2","pages":"Pages 177-194"},"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)90004-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18915998","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}

引用次数: 106

Vascular endothelial growth factor and its receptors. 血管内皮生长因子及其受体。

Progress in growth factor research Pub Date : 1994-01-01 DOI: 10.1097/00006982-199515020-00025

G. Neufeld, S. Tessler, H. Gitay-Goren, T. Cohen, B. Levi

{"title":"Vascular endothelial growth factor and its receptors.","authors":"G. Neufeld, S. Tessler, H. Gitay-Goren, T. Cohen, B. Levi","doi":"10.1097/00006982-199515020-00025","DOIUrl":"https://doi.org/10.1097/00006982-199515020-00025","url":null,"abstract":"Vascular endothelial growth factor (VEGF) is a highly specific mitogen for vascular endothelial cells and an angiogenic factor that is structurally related to platelet derived growth factor (PDGF). It is also known as the vascular permeability factor (VPF) because it efficiently potentiates the permeabilization of blood vessels. Five types of VEGF mRNA encoding VEGF species which differ in their molecular mass and in their biological properties are transcribed from a single gene as a result of alternative splicing. VEGFs are produced and secreted by several normal cell types including smooth muscle, luteal and adrenal cortex cells. VEGFs are also produced by different tumorigenic cells, and appear to play a major role in tumour angiogenesis. Antibodies directed against VEGF can inhibit the growth of a variety of VEGF producing tumours. Of the various VEGF species, the best characterized is the 165 amino acid long form (VEGF165). VEGF165 is a heparin binding growth factor, and its interaction with VEGF receptors on the cell surface of vascular endothelial cells depends on the presence of heparin-like molecules. Several cell types which do not proliferate in response to VEGF such as bovine corneal endothelial cells, HeLa cells and human melanoma cells also express cell surface VEGF receptors, but the function of the VEGF receptors in these cells is unclear. Recently, the tyrosine-kinase receptors encoded by the flt and KDR/flk-1 genes were found to function as VEGF165 receptors.","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 1 1","pages":"89-97"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/00006982-199515020-00025","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61770018","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}

引用次数: 121

Signal transduction by the PDGF receptors PDGF受体的信号转导

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-27 DOI: 10.1016/0955-2235(94)90016-7

Lena Claesson-Welsh

{"title":"Signal transduction by the PDGF receptors","authors":"Lena Claesson-Welsh","doi":"10.1016/0955-2235(94)90016-7","DOIUrl":"10.1016/0955-2235(94)90016-7","url":null,"abstract":"<div><p>The three isoforms of PDGF bind with different affinities to two related tyrosine kinase receptors, denoted the PDGF α- and β-receptors. Ligand binding induces receptor dimerization, creating receptor homo- or heterodimers. Dimerization is accompanied by, and might be a prerequisite for, receptor autophosphorylation and kinase activation. Receptor autophosphorylation serves to regulate the kinase activity and to create binding sites on the receptor molecule for downstream signalling components. The activities of the signalling components are ultimately manifested as specific biological responses. All the currently described PDGF receptor-binding components, e.g. phospholipase C-γ, members of the src family of cytoplasmic tyrosine kinases, the rasGT-Pase activating protein and p85, the regulatory subunit of phosphatidylinositol 3′ kinase, contain a conserved src homology 2-domain, through which the association with the receptor takes place. The receptor-binding components appear to either possess an intrinsic enzymatic activity, or they function as adaptors, which may complex with catalytically active components. For most receptor-binding components, there is insufficient understanding of how binding to the receptor affects the catalytic function. Certain of these components become tyrosine-phosphorylated, i.e. they are substrates for the receptor tyrosine kinase. Moreover, the change in subcellular localization, which most of the receptor binding components undergo in conjunction with receptor binding, could play a critical role. The current efforts of many laboratories are aimed at delineating different PDGF receptor signal transduction pathways and what roles the different receptor-binding components play in the establishment of these pathways.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 1","pages":"Pages 37-54"},"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)90016-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19189220","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}

引用次数: 101

Fibroblast growth factors and their receptors: An information network controlling tissue growth, morphogenesis and repair 成纤维细胞生长因子及其受体:控制组织生长、形态发生和修复的信息网络

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-07-26 DOI: 10.1016/0955-2235(94)00007-8

David G Fernig , John T Gallagher

{"title":"Fibroblast growth factors and their receptors: An information network controlling tissue growth, morphogenesis and repair","authors":"David G Fernig , John T Gallagher","doi":"10.1016/0955-2235(94)00007-8","DOIUrl":"10.1016/0955-2235(94)00007-8","url":null,"abstract":"<div><p>The stimulation of cellular metabolism by the nine fibroblast growth factors (FGFs) is mediated by a dual-receptor system. This comprises a family of four receptor tyrosine kinases (FGFR) and heparan sulphate proteoglycans (HSPG). The stimulation of cell division by FGFs has an obligate requirement for both partners of the dual-receptor system. The binding of the nine FGFs to the FGFRs is marked by a pattern of overlapping specificity despite alternative splicing events generating a large number of FGFR proteins. Thus many of the FGFR isoforms bind several FGFs. It is likely that each FGF requires a different pattern of sulphation within the heparan sulphate chains for binding. Therefore, the HSPG receptors may provide additional specificity, allowing a cell to fine tune its response to the FGFs present in the extracellular milieu. The HSPG receptors also control the availability of FGFs and hence regulate the transport of FGFs within a tissue. FGF-stimulated cell division would appear to have a mandatory requirement for the FGFs to be translocated to the nucleus via the cytosol after interacting with the dual-receptor system. The consequences of the potential direct action of FGFs in stimulating cell division are examined in the light of current models of signal transduction.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 4","pages":"Pages 353-377"},"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)00007-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18780283","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}

引用次数: 208

Growth factors in Parkinson's disease 帕金森病的生长因子

Progress in growth factor research Pub Date : 1994-01-01 Epub Date: 2004-04-27 DOI: 10.1016/0955-2235(94)90018-3

Klaus Unsicker

{"title":"Growth factors in Parkinson's disease","authors":"Klaus Unsicker","doi":"10.1016/0955-2235(94)90018-3","DOIUrl":"10.1016/0955-2235(94)90018-3","url":null,"abstract":"<div><p>The etiology of Parkinson's disease, one of the most frequent neurodegenerative disorders in human, is unknown. New hopes concerning satisfactory therapies include transplants of autologous adrenal medullary chromaffin tissue, fetal mesencephalic dopaminergic neurons, and local application of growth factors with a neurotrophic capacity. A large body of evidence supports the notion that neurons require trophic support not only during a limited period of ontogenesis, but during their whole lifespan. Relevant molecules promote survival, transmitter synthesis and other differentiated properties, and become crucially important when a neuron is metabolically or toxically impaired. Several molecules, most of which occur in the striatum and the substantia nigra, have been identified that protect lesioned dopaminergic nigrostriatal neurons in culture or in animal models of Parkinson's disease. These include members of the neurotrophin, fibroblast growth factor, and insulin-like growth factor families as well as epidermal growth factor/transforming growth factor alpha, interleukins and ciliary neurotrophic factor. Whether their effects are merely pharmacological, or reflect a physiological role in the nigrostriatal system, is unclear as yet. This article reviews experiments that document the trophic effects of these factors on dopaminergic neurons and discusses their possible physiological and therapeutic relevance.</p></div>","PeriodicalId":77335,"journal":{"name":"Progress in growth factor research","volume":"5 1","pages":"Pages 73-87"},"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)90018-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19189222","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}

引用次数: 57