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Journal articles on the topic 'Receptors fibroblast growth factor'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Chen, Gregory, and Reza Forough. "Fibroblast Growth Factors, Fibroblast Growth Factor Receptors, Diseases, and Drugs." Recent Patents on Cardiovascular Drug Discovery 1, no. 2 (2006): 211–24. http://dx.doi.org/10.2174/157489006777442478.

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2

Li, Y., C. Basilico, and A. Mansukhani. "Cell transformation by fibroblast growth factors can be suppressed by truncated fibroblast growth factor receptors." Molecular and Cellular Biology 14, no. 11 (1994): 7660–69. http://dx.doi.org/10.1128/mcb.14.11.7660.

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Ligand-induced dimerization and transphosphorylation are thought to be important events by which receptor tyrosine kinases generate cellular signals. We have investigated the ability of signalling-defective, truncated fibroblast growth factor (FGF) receptors (FGFR-1 and FGFR-2) to block the FGF response in cells that express both types of endogenous FGF receptors. When these dominant negative receptors are expressed in NIH 3T3 cells transformed by the secreted FGF-4, the transformed properties of the cells can be reverted to various degrees, with better reversion phenotype correlating with hig

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3

Li, Y., C. Basilico, and A. Mansukhani. "Cell transformation by fibroblast growth factors can be suppressed by truncated fibroblast growth factor receptors." Molecular and Cellular Biology 14, no. 11 (1994): 7660–69. http://dx.doi.org/10.1128/mcb.14.11.7660-7669.1994.

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Ligand-induced dimerization and transphosphorylation are thought to be important events by which receptor tyrosine kinases generate cellular signals. We have investigated the ability of signalling-defective, truncated fibroblast growth factor (FGF) receptors (FGFR-1 and FGFR-2) to block the FGF response in cells that express both types of endogenous FGF receptors. When these dominant negative receptors are expressed in NIH 3T3 cells transformed by the secreted FGF-4, the transformed properties of the cells can be reverted to various degrees, with better reversion phenotype correlating with hig

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4

Wang, Shuwei, and Zhongyang Ding. "Fibroblast growth factor receptors in breast cancer." Tumor Biology 39, no. 5 (2017): 101042831769837. http://dx.doi.org/10.1177/1010428317698370.

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Fibroblast growth factor receptors are growth factor receptor tyrosine kinases, exerting their roles in embryogenesis, tissue homeostasis, and development of breast cancer. Recent genetic studies have identified some subtypes of fibroblast growth factor receptors as strong genetic loci associated with breast cancer. In this article, we review the recent epidemiological findings and experiment results of fibroblast growth factor receptors in breast cancer. First, we summarized the structure and physiological function of fibroblast growth factor receptors in humans. Then, we discussed the common

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5

Green, Paula J., Frank S. Walsh, and Patrick Doherty. "Promiscuity of fibroblast growth factor receptors." BioEssays 18, no. 8 (1996): 639–46. http://dx.doi.org/10.1002/bies.950180807.

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6

Hsu, Pi-en, Fu Yu, François Féron, James O. Pickles, Kyra Sneesby, and Alan Mackay-Sim. "Basic fibroblast growth factor and fibroblast growth factor receptors in adult olfactory epithelium." Brain Research 896, no. 1-2 (2001): 188–97. http://dx.doi.org/10.1016/s0006-8993(01)02173-4.

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7

Galzie, Zoya, Anne R. Kinsella, and John A. Smith. "Fibroblast growth factors and their receptors." Biochemistry and Cell Biology 75, no. 6 (1997): 669–85. http://dx.doi.org/10.1139/o97-091.

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Fibroblast growth factors (FGFs) represent a group of polypeptide mitogens eliciting a wide variety of responses depending upon the target cell type. The knowledge of the cell surface receptors mediating the effects of FGFs has recently expanded remarkably. The complexity of the FGF family and the FGF-induced responses is reflected in the diversity and redundancy of the FGF receptors. In this review, a number of biochemical characteristics and biological properties of the FGF family and its receptors are described and their expression both in normal tissues and in tumours is discussed. Finally

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8

Malot, Michel, Edith Browaeys-Poly, Franck Foumiertjt, Katia Cailliaul, and Jean Pierre Vilain. "Ca2+Oscillations induced by fibroblast growth factor 2 inXenopusoocytes expressing fibroblast growth factor receptors." Molecular Membrane Biology 14, no. 4 (1997): 205–10. http://dx.doi.org/10.3109/09687689709048183.

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9

Klint, Peter. "Signal transduction by fibroblast growth factor receptors." Frontiers in Bioscience 4, no. 1-3 (1999): d165. http://dx.doi.org/10.2741/klint.

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10

Fedyanin, M. Yu, D. N. Hmel’kova, T. S. Serebriyskaya, T. A. Nikol’skaya, and S. A. Tyulyandin. "Fibroblast growth factor receptors in malignant tumors." Malignant tumours, no. 4 (May 21, 2015): 19. http://dx.doi.org/10.18027/2224-5057-2014-4-19-34.

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11

Liang, Guang, Zhiguo Liu, Jianzhang Wu, Yuepiao Cai, and Xiaokun Li. "Anticancer molecules targeting fibroblast growth factor receptors." Trends in Pharmacological Sciences 33, no. 10 (2012): 531–41. http://dx.doi.org/10.1016/j.tips.2012.07.001.

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12

Claesson-Welsh, Lena. "Signal transduction by fibroblast growth factor receptors." Frontiers in Bioscience 4, no. 4 (1999): d165–177. http://dx.doi.org/10.2741/a419.

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13

Yu, Xijie, and Kenneth E. White. "Fibroblast Growth Factor 23 and Its Receptors." Therapeutic Apheresis and Dialysis 9, no. 4 (2005): 308–12. http://dx.doi.org/10.1111/j.1744-9987.2005.00287.x.

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14

Eswarakumar, V. P., I. Lax, and J. Schlessinger. "Cellular signaling by fibroblast growth factor receptors." Cytokine & Growth Factor Reviews 16, no. 2 (2005): 139–49. http://dx.doi.org/10.1016/j.cytogfr.2005.01.001.

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15

Lappi, Douglas A. "Tumor targeting through fibroblast growth factor receptors." Seminars in Cancer Biology 6, no. 5 (1995): 279–88. http://dx.doi.org/10.1006/scbi.1995.0036.

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16

Jimenez-Pascual, Ana, and Florian A. Siebzehnrubl. "Fibroblast Growth Factor Receptor Functions in Glioblastoma." Cells 8, no. 7 (2019): 715. http://dx.doi.org/10.3390/cells8070715.

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Glioblastoma is the most lethal brain cancer in adults, with no known cure. This cancer is characterized by a pronounced genetic heterogeneity, but aberrant activation of receptor tyrosine kinase signaling is among the most frequent molecular alterations in glioblastoma. Somatic mutations of fibroblast growth factor receptors (FGFRs) are rare in these cancers, but many studies have documented that signaling through FGFRs impacts glioblastoma progression and patient survival. Small-molecule inhibitors of FGFR tyrosine kinases are currently being trialed, underlining the therapeutic potential of

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17

Yamakage, A., K. Kikuchi, E. A. Smith, E. C. LeRoy, and M. Trojanowska. "Selective upregulation of platelet-derived growth factor alpha receptors by transforming growth factor beta in scleroderma fibroblasts." Journal of Experimental Medicine 175, no. 5 (1992): 1227–34. http://dx.doi.org/10.1084/jem.175.5.1227.

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Transforming growth factor beta (TGF-beta), a multifunctional cytokine, is an indirect mitogen for human fibroblasts through platelet-derived growth factor (PDGF), particularly the A ligand-alpha receptor arm of that system. TGF-beta effects on PDGF alpha receptor expression were studied in vitro using ligand binding techniques in three human dermal fibroblast strains: newborn foreskin, adult skin, and scleroderma (systemic sclerosis, SSc). Each cell strain responded differently to TGF-beta. In newborn foreskin fibroblasts, PDGF alpha receptor number decreased in a dose-dependent manner after

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18

Panossian, Vah??, Stephen H. Liu, Joseph M. Lane, and Gerald A. M. Finerman. "Fibroblast Growth Factor and Epidermal Growth Factor Receptors in Ligament Healing." Clinical Orthopaedics and Related Research 342 (September 1997): 173???180. http://dx.doi.org/10.1097/00003086-199709000-00025.

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19

Wiedłocha, A., P. O. Falnes, A. Rapak, R. Muñoz, O. Klingenberg, and S. Olsnes. "Stimulation of proliferation of a human osteosarcoma cell line by exogenous acidic fibroblast growth factor requires both activation of receptor tyrosine kinase and growth factor internalization." Molecular and Cellular Biology 16, no. 1 (1996): 270–80. http://dx.doi.org/10.1128/mcb.16.1.270.

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U2OS Dr1 cells, originating from a human osteosarcoma, are resistant to the intracellular action of diphtheria toxin but contain toxin receptors on their surfaces. These cells do not have detectable amounts of fibroblast growth factor receptors. When these cells were transfected with fibroblast growth factor receptor 4, the addition of acidic fibroblast growth factor to the medium induced tyrosine phosphorylation, DNA synthesis, and cell proliferation. A considerable fraction of the cell-associated growth factor was found in the nuclear fraction. When the growth factor was fused to the diphthe

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20

Dvorakova, Dana, Stanislava Koskova, Martina Vodinska, Ales Hampl, Jiri Mayer, and Petr Dvorak. "Fibroblast Growth Factor Receptors in Human Embryonic Stem Cells." Blood 104, no. 11 (2004): 4168. http://dx.doi.org/10.1182/blood.v104.11.4168.4168.

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Abstract Signals via fibroblast growth factor receptors (FGFRs) are involved in mesoderm induction events and may be also critical for early hematopoietic specification and proliferation of the hemangioblast. In vitro differentiated embryonic stem cells represent excellent system for the study of early hematopoietic commitment, particularly for understanding signals regulating the onset of hematopoietic differentiation. We have used human embryonic stem cells (hESCs) to study the expression of FGFR1, 2, 3, and 4 in undifferentiated cells and their differentiated progeny. Culturing hESCs i/ in

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21

Greulich, Heidi, and Pamela M. Pollock. "Targeting mutant fibroblast growth factor receptors in cancer." Trends in Molecular Medicine 17, no. 5 (2011): 283–92. http://dx.doi.org/10.1016/j.molmed.2011.01.012.

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22

Ertl, Iris E., Shahrokh F. Shariat, Hadi Mostafaei, Dafina Ilijazi, and Yohann Loriot. "Fibroblast growth factor receptors across urothelial carcinoma landscape." Current Opinion in Urology 30, no. 4 (2020): 557–65. http://dx.doi.org/10.1097/mou.0000000000000782.

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23

Burke, David, David Wilkes, Tom L. Blundell, and Sue Malcolm. "Fibroblast growth factor receptors: lessons from the genes." Trends in Biochemical Sciences 23, no. 2 (1998): 59–62. http://dx.doi.org/10.1016/s0968-0004(97)01170-5.

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24

Haugsten, Ellen Margrethe, Antoni Wiedlocha, Sjur Olsnes, and Jørgen Wesche. "Roles of Fibroblast Growth Factor Receptors in Carcinogenesis." Molecular Cancer Research 8, no. 11 (2010): 1439–52. http://dx.doi.org/10.1158/1541-7786.mcr-10-0168.

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25

COUTTS, JACQUELINE C., and JOHN T. GALLAGHER. "Receptors for fibroblast growth factors." Immunology and Cell Biology 73, no. 6 (1995): 584–89. http://dx.doi.org/10.1038/icb.1995.92.

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26

HU, Z. "Expression of transforming growth factor-alpha/epidermal growth factor receptor, hepatocyte growth factor/c-met, acidic fibroblast growth factor/fibroblast growth factor receptors during hepatocarcinogenesis." Hepatology 18, no. 4 (1993): A160. http://dx.doi.org/10.1016/0270-9139(93)92170-5.

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27

M. Rusnati and M. Presta. "Fibroblast Growth Factors/Fibroblast Growth Factor Receptors as Targets for the Development of Anti-Angiogenesis Strategies." Current Pharmaceutical Design 13, no. 20 (2007): 2025–44. http://dx.doi.org/10.2174/138161207781039689.

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28

Isaacson, Marisa K., Adam L. Feire, and Teresa Compton. "Epidermal Growth Factor Receptor Is Not Required for Human Cytomegalovirus Entry or Signaling." Journal of Virology 81, no. 12 (2007): 6241–47. http://dx.doi.org/10.1128/jvi.00169-07.

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ABSTRACT Human cytomegalovirus (HCMV) can bind, fuse, and initiate gene expression in a diverse range of vertebrate cell types. This broad cellular tropism suggests that multiple receptors and/or universally distributed receptors mediate HCMV entry. Our laboratory has recently discovered that certain β1 and β3 integrin heterodimers are critical mediators of HCMV entry into permissive fibroblasts (A. L. Feire, H. Koss, and T. Compton, Proc. Natl. Acad. Sci. USA 101:15470-15475, 2004). It has also been reported that epidermal growth factor receptor (EGFR) is necessary for HCMV-mediated signaling

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29

Wang, J. K., G. Gao, and M. Goldfarb. "Fibroblast growth factor receptors have different signaling and mitogenic potentials." Molecular and Cellular Biology 14, no. 1 (1994): 181–88. http://dx.doi.org/10.1128/mcb.14.1.181.

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Fibroblast growth factor (FGF) receptors (FGFRs) are structurally related receptor protein tyrosine kinases encoded by four distinct genes. Activation of FGFR-1, -2, and -3 by FGFs induces mitogenic responses in various cell types, but the mitogenic potential of FGFR-4 has not been previously explored. We have compared the properties of BaF3 murine lymphoid cells and L6 rat myoblast cells engineered to express FGFR-1 or FGFR-4. Acidic FGF binds with high affinity to and elicits tyrosine phosphorylation of FGFR-1 or FGFR-4 receptors displayed on BaF3 cells, but only FGFR-1 activation leads to c

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30

Wang, J. K., G. Gao, and M. Goldfarb. "Fibroblast growth factor receptors have different signaling and mitogenic potentials." Molecular and Cellular Biology 14, no. 1 (1994): 181–88. http://dx.doi.org/10.1128/mcb.14.1.181-188.1994.

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Fibroblast growth factor (FGF) receptors (FGFRs) are structurally related receptor protein tyrosine kinases encoded by four distinct genes. Activation of FGFR-1, -2, and -3 by FGFs induces mitogenic responses in various cell types, but the mitogenic potential of FGFR-4 has not been previously explored. We have compared the properties of BaF3 murine lymphoid cells and L6 rat myoblast cells engineered to express FGFR-1 or FGFR-4. Acidic FGF binds with high affinity to and elicits tyrosine phosphorylation of FGFR-1 or FGFR-4 receptors displayed on BaF3 cells, but only FGFR-1 activation leads to c

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31

Weinreich, Michael A., Ingrid Lintmaer, Linlin Wang, H. Denny Liggitt, Michael A. Harkey, and C. Anthony Blau. "Growth factor receptors as regulators of hematopoiesis." Blood 108, no. 12 (2006): 3713–21. http://dx.doi.org/10.1182/blood-2006-01-012278.

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AbstractNearly 15 years have elapsed since the US Food and Drug Administration last approved a major new hematopoietic cytokine. Promiscuous binding to multiple receptors, or to receptors expressed by multiple tissues, reduces growth factor specificity and promotes side effects. Here we show that hematopoiesis can be differentially regulated using receptors rather than ligands. Conditional derivatives of both fibroblast growth factor receptor-1 (F36VFGFR1) and the thrombopoietin receptor (F36VMpl) induced a sustained expansion of mouse marrow cells ex vivo, and erythroid cells in vivo. Only F3

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32

Inokuchi, Mikito, Yoshitaka Fujimori, Sho Otsuki, Yuya Sato, Masatoshi Nakagawa, and Kazuyuki Kojima. "Therapeutic Targeting of Fibroblast Growth Factor Receptors in Gastric Cancer." Gastroenterology Research and Practice 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/796380.

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Chemotherapy has become the global standard treatment for patients with metastatic or unresectable gastric cancer (GC), although outcomes remain unfavorable. Many molecular-targeted therapies inhibiting signaling pathways of various tyrosine kinase receptors have been developed, and monoclonal antibodies targeting human epidermal growth factor receptor 2 (HER2) have become standard therapy for HER2-positive GC. An inhibitor of vascular endothelial growth factor receptor 2 or MET has also produced promising results in patients with GC. Fibroblast growth factor receptors (FGFR) play key roles in

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33

Klingenberg, O., A. Wiedlocha, A. Rapak, D. Khnykin, L. Citores, and S. Olsnes. "Requirement for C-terminal end of fibroblast growth factor receptor 4 in translocation of acidic fibroblast growth factor to cytosol and nucleus." Journal of Cell Science 113, no. 10 (2000): 1827–38. http://dx.doi.org/10.1242/jcs.113.10.1827.

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The ability of COS cells to bind and internalise acidic fibroblast growth factor (aFGF) was studied after transient transfection of the cells with wild-type and mutated fibroblast growth factor receptor 4. In one case the tyrosine kinase of the receptor was inactivated by a point mutation in the active site, whereas in other cases parts of the receptor were deleted to remove various parts of the cytoplasmic domain. In all cases the receptors were expressed at the cell surface at a high level and the cells bound labelled growth factor efficiently and internalised it by endocytosis. Translocatio

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34

Wakulich, Candice, Linda Jackson-Boeters, Tom D. Daley, and George P. Wysocki. "Immunohistochemical localization of growth factors fibroblast growth factor-1 and fibroblast growth factor-2 and receptors fibroblast growth factor receptor-2 and fibroblast growth factor receptor-3 in normal oral epithelium, epithelial dysplasias, and squamous cell carcinoma." Oral Surgery, Oral Medicine, Oral Pathology, Oral Radiology, and Endodontology 93, no. 5 (2002): 573–79. http://dx.doi.org/10.1067/moe.2002.124461.

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35

Takahashi, Hiroaki. "STUDIES ON THE EXPERSSION OF FIBROBLAST GROWTH FACTORS AND FIBROBLAST GROWTH FACTOR RECEPTORS IN HUMAN PROSTATE CANCER." Japanese Journal of Urology 89, no. 10 (1998): 836–45. http://dx.doi.org/10.5980/jpnjurol1989.89.836.

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36

Cancilla, Belinda, Miriam D. Ford-Perriss, and John F. Bertram. "Expression and localization of fibroblast growth factors and fibroblast growth factor receptors in the developing rat kidney." Kidney International 56, no. 6 (1999): 2025–39. http://dx.doi.org/10.1046/j.1523-1755.1999.00781.x.

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37

Chen, Yunliang, David J. Abraham, Xu Shi-wen, et al. "CCN2 (Connective Tissue Growth Factor) Promotes Fibroblast Adhesion to Fibronectin." Molecular Biology of the Cell 15, no. 12 (2004): 5635–46. http://dx.doi.org/10.1091/mbc.e04-06-0490.

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In vivo, CCN2 (connective tissue growth factor) promotes angiogenesis, osteogenesis, tissue repair, and fibrosis, through largely unknown mechanisms. In vitro, CCN2 promotes cell adhesion in a variety of systems via integrins and heparin sulfate proteoglycans (HSPGs). However, the physiological relevance of CCN2-mediated cell adhesion is unknown. Here, we find that HSPGs and the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase cascade are required for adult human dermal fibroblasts to adhere to CCN2. Endogenous CCN2 directly b

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38

Ivey, Malina J., Jill T. Kuwabara, Kara L. Riggsbee та Michelle D. Tallquist. "Platelet-derived growth factor receptor-α is essential for cardiac fibroblast survival". American Journal of Physiology-Heart and Circulatory Physiology 317, № 2 (2019): H330—H344. http://dx.doi.org/10.1152/ajpheart.00054.2019.

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Platelet-derived growth factor receptor α (PDGFRα), a receptor tyrosine kinase required for cardiac fibroblast development, is uniquely expressed by fibroblasts in the adult heart. Despite the consensus that PDGFRα is expressed in adult cardiac fibroblasts, we know little about its function when these cells are at rest. Here, we demonstrate that loss of PDGFRα in cardiac fibroblasts resulted in a rapid reduction of resident fibroblasts. Furthermore, we observe that phosphatidylinositol 3-kinase signaling was required for PDGFRα-dependent fibroblast maintenance. Interestingly, this reduced numb

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39

Putnins, Edward E., Ali-Reza Sanaie, Qiang Wu, and James D. Firth. "Induction of Keratinocyte Growth Factor 1 Expression by Lipopolysaccharide Is Regulated by CD-14 and Toll-Like Receptors 2 and 4." Infection and Immunity 70, no. 12 (2002): 6541–48. http://dx.doi.org/10.1128/iai.70.12.6541-6548.2002.

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ABSTRACT Periodontal disease is a chronic inflammatory condition that is associated with increased concentrations of gram-negative pathogenic bacteria and epithelial cell proliferation. Regulation of this proliferation is poorly understood but is most likely controlled by locally expressed growth factors. Keratinocyte growth factor 1, an epithelium-specific growth factor, is expressed by gingival fibroblasts, and its expression is regulated in a concentration-dependent manner by lipopolysaccharide. In this study, induction of keratinocyte growth factor 1 protein expression was dependent on gin

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40

Kaleko, M., W. J. Rutter, and A. D. Miller. "Overexpression of the human insulinlike growth factor I receptor promotes ligand-dependent neoplastic transformation." Molecular and Cellular Biology 10, no. 2 (1990): 464–73. http://dx.doi.org/10.1128/mcb.10.2.464.

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The human insulinlike growth factor I receptor was overexpressed in NIH 3T3 cells as well as human and rat primary fibroblast strains. The NIH 3T3 cells displayed a ligand-dependent, highly transformed phenotype. When exposed to insulinlike growth factor I or supraphysiologic levels of insulin, NIH 3T3 cells that expressed high levels of receptors formed aggregates in tissue culture dishes, colonies in soft agar, and tumors in nude mice. Expression of 1 million receptors per cell, a 40-fold increase above the base-line level, was required for anchorage-independent growth. Primary fibroblasts t

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41

Kaleko, M., W. J. Rutter, and A. D. Miller. "Overexpression of the human insulinlike growth factor I receptor promotes ligand-dependent neoplastic transformation." Molecular and Cellular Biology 10, no. 2 (1990): 464–73. http://dx.doi.org/10.1128/mcb.10.2.464-473.1990.

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The human insulinlike growth factor I receptor was overexpressed in NIH 3T3 cells as well as human and rat primary fibroblast strains. The NIH 3T3 cells displayed a ligand-dependent, highly transformed phenotype. When exposed to insulinlike growth factor I or supraphysiologic levels of insulin, NIH 3T3 cells that expressed high levels of receptors formed aggregates in tissue culture dishes, colonies in soft agar, and tumors in nude mice. Expression of 1 million receptors per cell, a 40-fold increase above the base-line level, was required for anchorage-independent growth. Primary fibroblasts t

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42

Britto, J. A., J. C. Chan, R. D. Evans, R. D. Hayward, P. Thorogood, and B. M. Jones. "FIBROBLAST GROWTH FACTOR RECEPTORS ARE EXPRESSED IN CRANIOSYNOSTOTIC SUTURES." Plastic and Reconstructive Surgery 101, no. 2 (1998): 540–43. http://dx.doi.org/10.1097/00006534-199802000-00052.

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43

Cohen, M. Michael. "Neoplasms associated with alterations in fibroblast growth factor receptors." American Journal of Medical Genetics 119A, no. 2 (2003): 97–100. http://dx.doi.org/10.1002/ajmg.a.10058.

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44

Kelleher, F. C., H. O'Sullivan, E. Smyth, R. McDermott, and A. Viterbo. "Fibroblast growth factor receptors, developmental corruption and malignant disease." Carcinogenesis 34, no. 10 (2013): 2198–205. http://dx.doi.org/10.1093/carcin/bgt254.

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45

Rohs, Patricia, Alicia M. Ebert, Ania Zuba, and Sarah McFarlane. "Neuronal expression of fibroblast growth factor receptors in zebrafish." Gene Expression Patterns 13, no. 8 (2013): 354–61. http://dx.doi.org/10.1016/j.gep.2013.06.006.

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46

Reilly, John F., та Pamela A. Maher. "Importin β–Mediated Nuclear Import of Fibroblast Growth Factor Receptor". Journal of Cell Biology 152, № 6 (2001): 1307–12. http://dx.doi.org/10.1083/jcb.152.6.1307.

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Although growth factor receptors are generally thought to carry out their role in signal transduction at the cell surface, many of these transmembrane proteins translocate to the nucleus after ligand stimulation. Here, we show that the nuclear translocation of fibroblast growth factor receptor (FGFR)1 occurs via a mechanism distinct from classical nuclear import but dependent on importin β, a component of multiple nuclear import pathways. Furthermore, we show that nuclear FGFR1 induces c-Jun and is involved in the regulation of cell proliferation. These data are the first description of a nucl

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47

Partanen, Juha, Satu Vainikka, Jaana Korhonen, Elina Armstrong, and Kari Alitalo. "Diverse receptors for fibroblast growth factors." Progress in Growth Factor Research 4, no. 1 (1992): 69–83. http://dx.doi.org/10.1016/0955-2235(92)90005-3.

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48

Bras, S. L., F. Miralles, A. Basmaciogullari, P. Czernichow, and R. Scharfmann. "Fibroblast Growth Factor 2 Promotes Pancreatic Epithelial Cell Proliferation Via Functional Fibroblast Growth Factor Receptors During Embryonic Life." Diabetes 47, no. 8 (1998): 1236–42. http://dx.doi.org/10.2337/diab.47.8.1236.

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49

Le Bras, S., F. Miralles, A. Basmaciogullari, P. Czernichow, and R. Scharfmann. "Fibroblast growth factor 2 promotes pancreatic epithelial cell proliferation via functional fibroblast growth factor receptors during embryonic life." Diabetes 47, no. 8 (1998): 1236–42. http://dx.doi.org/10.2337/diabetes.47.8.1236.

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50

Ball, Stephen G., C. Adrian Shuttleworth, and Cay M. Kielty. "Vascular endothelial growth factor can signal through platelet-derived growth factor receptors." Journal of Cell Biology 177, no. 3 (2007): 489–500. http://dx.doi.org/10.1083/jcb.200608093.

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Vascular endothelial growth factor (VEGF-A) is a crucial stimulator of vascular cell migration and proliferation. Using bone marrow–derived human adult mesenchymal stem cells (MSCs) that did not express VEGF receptors, we provide evidence that VEGF-A can stimulate platelet-derived growth factor receptors (PDGFRs), thereby regulating MSC migration and proliferation. VEGF-A binds to both PDGFRα and PDGFRβ and induces tyrosine phosphorylation that, when inhibited, results in attenuation of VEGF-A–induced MSC migration and proliferation. This mechanism was also shown to mediate human dermal fibrob

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