Journal articles: 'Transforming growth factors'

1

Hsuan, J. Justin. "Transforming growth factors β." British Medical Bulletin 45, no. 2 (1989): 425–37. http://dx.doi.org/10.1093/oxfordjournals.bmb.a072332.

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2

Massagué, Joan. "The transforming growth factors." Trends in Biochemical Sciences 10, no. 6 (June 1985): 237–40. http://dx.doi.org/10.1016/0968-0004(85)90141-0.

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3

HELDIN, Carl-Henrik, and Bengt WESTERMARK. "Growth factors as transforming proteins." European Journal of Biochemistry 184, no. 3 (October 1989): 487–96. http://dx.doi.org/10.1111/j.1432-1033.1989.tb15041.x.

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4

Moses, Harold L., Jorma Keski-Oja, Robert J. Coffey, Russette M. Lyons, Nancy J. Sipes, and Charles C. Bascom. "Transforming growth factors and oncogenes." European Journal of Cancer and Clinical Oncology 23, no. 11 (November 1987): 1780. http://dx.doi.org/10.1016/0277-5379(87)90651-1.

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5

Lawrence, D. A. "Transforming growth factors-an overview." Biology of the Cell 53, no. 2 (1985): 93–98. http://dx.doi.org/10.1111/j.1768-322x.1985.tb00358.x.

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6

Stenn, Kurt S., Raymond L. Barnhill, and Yasmin Johnston. "Transforming growth factors and histopathologic interpretation." Journal of the American Academy of Dermatology 17, no. 1 (July 1987): 161–63. http://dx.doi.org/10.1016/s0190-9622(87)70185-6.

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7

Hammerman, M. R., S. A. Rogers, and G. Ryan. "Growth factors and metanephrogenesis." American Journal of Physiology-Renal Physiology 262, no. 4 (April 1, 1992): F523—F532. http://dx.doi.org/10.1152/ajprenal.1992.262.4.f523.

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The formation of all organs during embryogenesis, including kidney, is dependent on the timed and sequential expression of a number of polypeptide growth factors. Synthesis and actions of one or more members of the insulin-like growth factor, epidermal growth factor/transforming growth factor-alpha, transforming growth factor-beta, platelet-derived growth factor, fibroblast growth factor, and nerve growth factor families have been characterized in the developing metanephric kidney. Studies originating from a number of laboratories have defined the localization of growth factor mRNAs, receptors and peptides, have delineated patterns of growth factor synthesis, and have established the growth factor dependency of embryonic kidney development. The results of these investigations will be summarized in this editorial review and integrated within the broader context of growth factor cellular physiology and growth factor expression in nonrenal systems.

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8

Keski-Oja, Jorma, Edward B. Leof, Russette M. Lyons, Robert J. Coffey, and Harold L. Moses. "Transforming growth factors and control of neoplastic cell growth." Journal of Cellular Biochemistry 33, no. 2 (February 1987): 95–107. http://dx.doi.org/10.1002/jcb.240330204.

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9

Archer, J. R. "Ankylosing spondylitis, IgA, and transforming growth factors." Annals of the Rheumatic Diseases 54, no. 7 (July 1, 1995): 544–46. http://dx.doi.org/10.1136/ard.54.7.544.

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10

Gol-Winkler, R. "5 Paracrine action of transforming growth factors." Clinics in Endocrinology and Metabolism 15, no. 1 (February 1986): 99–115. http://dx.doi.org/10.1016/s0300-595x(86)80044-5.

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11

Salomon, D. S., F. Ciardiello, E. Valverius, T. Saeki, and N. Kim. "Transforming growth factors in human breast cancer." Biomedicine & Pharmacotherapy 43, no. 9 (January 1989): 661–67. http://dx.doi.org/10.1016/0753-3322(89)90084-x.

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12

IHLE, J. N. "Transforming Genes: Oncogenes, Genes, and Growth Factors." Science 237, no. 4818 (August 28, 1987): 1060–61. http://dx.doi.org/10.1126/science.237.4818.1060-a.

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13

Neal, Harold J. "Crescentic glomerulonephritis: associations and transforming growth factors." Journal and proceedings of the Royal Society of New South Wales 136, no. 1-4 (December 2003): 51–52. http://dx.doi.org/10.5962/p.361514.

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14

Mak, Robert H., and Wai W. Cheung. "Transforming growth factors and insulin-like growth factors in chronic kidney disease." Journal of Organ Dysfunction 5, no. 1 (January 2009): 59–64. http://dx.doi.org/10.1080/17471060701486225.

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15

Centrella, Michael, Thomas L. McCarthy, and Ernesto Canalis. "Effects of Transforming Growth Factors on Bone Cells." Connective Tissue Research 20, no. 1-4 (January 1989): 267–75. http://dx.doi.org/10.3109/03008208909023896.

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16

MADRI, JOSEPH A., OLIVIER KOCHER, JUNE R. MERWIN, LEONARD BELL, ADELINE TUCKER, and CRAIG T. BASSON. "Interactions of Vascular Cells with Transforming Growth Factors-?" Annals of the New York Academy of Sciences 593, no. 1 Transforming (June 1990): 243–58. http://dx.doi.org/10.1111/j.1749-6632.1990.tb16116.x.

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17

Rizzino, Angie, and Eric Ruff. "Parameters for optimizing detection of transforming growth factors." Journal of Tissue Culture Methods 10, no. 2 (June 1986): 109–15. http://dx.doi.org/10.1007/bf01404601.

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18

Krieglstein, Kerstin, Matthias Rufer, Clemens Suter-Crazzolara, and Klaus Unsicker. "Neural functions of the transforming growth factors β." International Journal of Developmental Neuroscience 13, no. 3-4 (June 1995): 301–15. http://dx.doi.org/10.1016/0736-5748(94)00062-8.

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19

Massagu�, Joan, Sela Cheifetz, Ronald A. Ignotz, and Frederick T. Boyd. "Multiple type-? transforming growth factors and their receptors." Journal of Cellular Physiology 133, S5 (1987): 43–47. http://dx.doi.org/10.1002/jcp.1041330409.

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20

Jingushi, S., S. P. Scully, M. E. Joyce, Y. Sugioka, and M. E. Bolander. "Transforming growth factor-?1 and fibroblast growth factors in rat growth plate." Journal of Orthopaedic Research 13, no. 5 (September 1995): 761–68. http://dx.doi.org/10.1002/jor.1100130516.

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21

Jankowski, J., R. McMenemin, D. Hopwood, J. Penston, and K. G. Wormsley. "Abnormal expression of growth regulatory factors in Barrett's oesophagus." Clinical Science 81, no. 5 (November 1, 1991): 663–68. http://dx.doi.org/10.1042/cs0810663.

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1. In order to assess potential abnormalities in the control of mucosal proliferation, 30 patients with Barrett's oesophagus were studied in order to evaluate the presence and distribution of epidermal growth factor, transforming growth factor-α and epidermal growth factor receptor to determine the Ki-67 labelling index in the affected oesophageal mucosa. Serial sections were analysed immunohistochemically. Ten of the patients had adenocarcinoma in the Barrett's mucosa and the other 20 had differing histological types of Barrett's mucosa (10, intestinal-type; 10, fundic-or cardiac-type). 2. The expression of transforming growth factor-α, epidermal growth factor and epidermal growth factor receptor was increased and the Ki-67 labelling index was higher in Barrett's mucosa compared with normal gastric mucosa. The ‘intestinal-type’ of Barrett's mucosa had the greatest expression of transforming growth factor-α, epidermal growth factor receptor and the highest Ki-67 labelling index compared with the other types of Barrett's metaplasia. Five cases of ‘intestinal-type’ Barrett's metaplasia had especially high Ki-67 labelling indices and these patients over-expressed both transforming growth factor-α and epidermal growth factor receptor. The patients with adenocarcinomas in the Barrett's mucosa also over-expressed transforming growth factor-α and epidermal growth factor receptor, but not epidermal growth factor, compared with normal gastric mucosa. 3. In conclusion, both normal gastric mucosa and Barrett's mucosa have potential autocrine growth regulatory mechanisms, but Barrett's mucosa has increased expression of both of the measured ligands and of the epidermal growth factor receptor.

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22

Hemmings, Robert, Jean Langlais, Tommaso Falcone, Louis Granger, Pierre Miron, and Harvey Guyda. "Human embryos produce transforming growth factors α activity and insulin-like growth factors II." Fertility and Sterility 58, no. 1 (July 1992): 101–4. http://dx.doi.org/10.1016/s0015-0282(16)55144-9.

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23

Haralson, Michael A. "Transforming growth factor-β, other growth factors, and the extracellular matrix." Journal of Laboratory and Clinical Medicine 130, no. 5 (November 1997): 455–58. http://dx.doi.org/10.1016/s0022-2143(97)90120-7.

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24

Massagué, J. "Transforming growth factor-alpha. A model for membrane-anchored growth factors." Journal of Biological Chemistry 265, no. 35 (December 1990): 21393–96. http://dx.doi.org/10.1016/s0021-9258(18)45745-6.

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25

Dart, Linda L., Diane M. Smith, Chester A. Meyers, Michael B. Sporn, and Charles A. Frolik. "Transforming growth factors from a human tumor cell: characterization of transforming growth factor .beta. and identification of high molecular weight transforming growth factor .alpha." Biochemistry 24, no. 21 (October 1985): 5925–31. http://dx.doi.org/10.1021/bi00342a035.

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26

Massagué, J. "Transforming growth factor-beta modulates the high-affinity receptors for epidermal growth factor and transforming growth factor-alpha." Journal of Cell Biology 100, no. 5 (May 1, 1985): 1508–14. http://dx.doi.org/10.1083/jcb.100.5.1508.

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The epidermal growth factor (EGF) receptor mediates the induction of a transformed phenotype in normal rat kidney (NRK) cells by transforming growth factors (TGFs). The ability of EGF and its analogue TGF-alpha to induce the transformed phenotype in NRK cells is greatly potentiated by TGF-beta, a polypeptide that does not interact directly with binding sites for EGF or TGF-alpha. Our evidence indicates that TGF-beta purified from retrovirally transformed rat embryo cells and human platelets induces a rapid (t 1/2 = 0.3 h) decrease in the binding of EGF and TGF-alpha to high-affinity cell surface receptors in NRK cells. No change due to TGF-beta was observed in the binding of EGF or TGF-alpha to lower affinity sites also present in NRK cells. The effect of TGF-beta on EGF/TGF-alpha receptors was observed at concentrations (0.5-20 pM) similar to those at which TGF-beta is active in promoting proliferation of NRK cells in monolayer culture and semisolid medium. Affinity labeling of NRK cells and membranes by cross-linking with receptor-bound 125I-TGF-alpha and 125I-EGF indicated that both factors interact with a common 170-kD receptor structure. Treatment of cells with TGF-beta decreased the intensity of affinity-labeling of this receptor structure. These data suggest that the 170 kD high-affinity receptors for EGF and TGF-alpha in NRK cells are a target for rapid modulation by TGF-beta.

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27

PITTELKOW, MARK R., ROBERT J. COFFEY, and HAROLD L. MOSES. "Keratinocytes Produce and Are Regulated by Transforming Growth Factors." Annals of the New York Academy of Sciences 548, no. 1 Endocrine, Me (December 1988): 211–24. http://dx.doi.org/10.1111/j.1749-6632.1988.tb18809.x.

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28

LYONS, Russette M., and Harold L. MOSES. "Transforming growth factors and the regulation of cell proliferation." European Journal of Biochemistry 187, no. 3 (February 1990): 467–73. http://dx.doi.org/10.1111/j.1432-1033.1990.tb15327.x.

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29

Visser, Jenny A., and Axel P. N. Themmen. "Downstream factors in transforming growth factor-β family signaling." Molecular and Cellular Endocrinology 146, no. 1-2 (November 1998): 7–17. http://dx.doi.org/10.1016/s0303-7207(98)00198-1.

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30

Konttinen, Y. T., P. Kemppinen, T. F. Li, E. Waris, H. Pihlajamäki, T. Sorsa, M. Takagi, S. Santavirta, G. S. Schultz, and M. G. Humphreys-Beher. "Transforming and epidermal growth factors in degenerated intervertebral discs." Journal of Bone and Joint Surgery. British volume 81-B, no. 6 (November 1999): 1058–63. http://dx.doi.org/10.1302/0301-620x.81b6.0811058.

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31

Madri, Joseph A., Leonard Bell, and June Rae Merwin. "Modulation of vascular cell behavior by transforming growth factors ?" Molecular Reproduction and Development 32, no. 2 (June 1992): 121–26. http://dx.doi.org/10.1002/mrd.1080320207.

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32

Bascom, Charles C., Nancy J. Sipes, Robert J. Coffey, and Harold L. Moses. "Regulation of epithelial cell proliferation by transforming growth factors." Journal of Cellular Biochemistry 39, no. 1 (January 1989): 25–32. http://dx.doi.org/10.1002/jcb.240390104.

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33

Coffey, Robert J., Carol M. McCutchen, Ramona Graves-Deal, and William H. Polk. "Transforming growth factors and related peptides in gastrointestinal neoplasia." Journal of Cellular Biochemistry 50, S16G (1992): 111–18. http://dx.doi.org/10.1002/jcb.240501120.

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34

Runser, S., and N. Cerletti. "Transforming growth factors beta: conformational stability and features of the denaturation of recombinant human transforming growth factors beta 2 and beta 3." Biotechnology and Applied Biochemistry 22, no. 1 (August 1995): 39–53. http://dx.doi.org/10.1111/j.1470-8744.1995.tb00342.x.

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Transforming growth factors beta (TGF‐beta) are cytokines with multiple biological activities. Their development as biopharmaceutical drugs targets the control of complex physiological processes such as osteogenesis and epithelial cell differentiation. We report here the first characterization of the recombinant human (rh) TGF‐beta 2 and rhTGF‐beta 3 isoforms in terms of their conformational stability and structural transitions induced by a chaotrope or temperature. The transitions detected by CD spectroscopy suggested that thermal denaturation of both TGF‐beta isoforms apparently fitted a simple two‐state (N<==>D) model. However, the ratios of calorimetric to van't Hoff enthalpies, significantly different from unity, indicated that these molecules most probably consist of independently denaturing subdomains. The complex transitions induced by guanidine hydrochloride, at pH 1.8 or 8.0, also suggested intermediately denatured structures. Thermodynamic stabilities under pH conditions useful for bioprocessing were derived from spectroscopic and calorimetric measurements. Treatment of thermal denaturation data by van't Hoff analysis yielded, for the beta 2 and beta 3 isoforms respectively, apparent delta G(25 degrees C, pH 1.8) of 20.4/17.2 kJ/mol and 17.5/18.6 kJ/mol (near‐UV CD/far‐UV CD data) in 20 mM hydrochloric acid, and apparent delta G (25 degrees C, pH 3.0) of 35.1 and 33.5 kJ/mol in 0.25 M acetic acid (calorimetric data). Neither low‐pH‐induced denatured states nor soluble aggregates were detected in both acidic solvents. The spectroscopic and thermodynamic data should be useful for assessing the homogeneity and proper folding of these recombinant molecules.

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35

Tremollieres, Florence A., Donna D. Strong, David J. Baylink, and Subburaman Mohan. "Insulin-like growth factor II and transforming growth factor β1 regulate insulin-like growth factor I secretion in mouse bone cells." Acta Endocrinologica 125, no. 5 (November 1991): 538–46. http://dx.doi.org/10.1530/acta.0.1250538.

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Abstract. Bone cells in culture produce and respond to growth factors, suggesting that local as well as systemic factors regulate bone volume. Previous studies have shown that IGF-I is the major mitogen produced by mouse bone cells and that its production is regulated by systemic agents such as PTH and estrogen. Because IGF-II and transforming growth factor β1 have been shown, respectively, to increase and decrease MC3T3-E1 cell proliferation, we tested the hypothesis that these two growth factors modulate the production of IGF-I in this cell line. In order to eliminate artifacts owing to IGF binding proteins, conditioned media samples were pretreated with IGF-II before measurement of IGF-I by RIA. After 24 h treatment at a density of 2.5× 104 cells/cm2, IGF-II (10 μg/l) induced a 2.2-fold increase compared with untreated control (9.5±1.5 vs 4.2±0.44 pg/μg protein, p<0.001), whereas transforming growth factor β1 (1 μg/l) caused a 66% decrease in IGF-I production (1.5±0.3 vs 4.2±0.44 pg/μg protein, p<0.001). Both IGF-II and transforming growth factor β1 regulated IGF-I production in a dose-, time- and cell density-dependent manner. The lowest effective doses for IGF-II and transforming growth factor β1 were 1 and 0.01 μg/l, respectively. These results support a role for IGF-II and transforming growth factor β1 as potent modulators of IGF-I secretion in mouse bone cells. Furthermore, regulation of IGF-I production in bone cells by IGF-II and transforming growth factor β1 in an autocrine/paracrine manner could represent a component part of the mechanism whereby the skeleton locally adapts in reponse to external stimuli.

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36

Peña-Ortiz, Miguel Ángel, Liliana Germán-Castelán, and Aliesha González-Arenas. "Growth factors and kinases in glioblastoma growth." Advances in Modern Oncology Research 2, no. 5 (October 19, 2016): 248. http://dx.doi.org/10.18282/amor.v2.i5.100.

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<p>Glioblastoma multiforme (GBM) is the most aggressive type of brain cancer, having the highest invasion, migration, proliferation, and angiogenesis rates. Several signaling pathways are involved in the regulation of these processes including growth factors and their tyrosine kinase receptors, such as vascular endothelial growth factor (VEGF), transforming growth factor beta (TGFβ), fibroblast growth factor (FGF), platelet-derived growth factor (PDGF), and insulin-like growth factor–I (IGF–I). Different kinases and regulators also participate in signaling pathways initiated by growth factors, such as mitogen-activated kinases (MAPK), protein kinases C (PKC), phosphatidylinositol-3 kinases (PI3K), protein kinase B (PKB or Akt), glycogen synthase kinase 3β (GSK3β), the mTOR complex, and Bcl-2. In this review, we will focus on the role of these proteins as possible therapeutic targets in GBM.</p>

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37

Keski-Oja, Jorma, Arnold E. Postlethwaite, and Harold L. Moses. "Transforming Growth Factors in the Regulation of Malignant Cell Growth and Invasion." Cancer Investigation 6, no. 6 (January 1988): 705–24. http://dx.doi.org/10.3109/07357908809078038.

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38

Wajeetongratana, Prateep. "Economic growth and its key factors: an alternative view on the factors stimulating agriculture growth." E3S Web of Conferences 175 (2020): 13028. http://dx.doi.org/10.1051/e3sconf/202017513028.

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This research study makes an attempt to study the impacts of natural resources as well as financial and labor factors on economic development of contemporary states. Also, it investigates the correlation between all these factors mentioned above, in the context of countries’ economic growth. The obtained here results have helped us determine the core reasons behind international migration as a global phenomenon applicable to all countries without exceptions. Indirectly, we also demonstrate the transforming role of the labour factor as applied to economic development of countries and regions. Finally, positive impacts of a set of manufacturing factors on both international and domestic markets are demonstrated.

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39

Metzler, Veronika Maria, Christian Pritz, Anna Riml, Angela Romani, Raphaela Tuertscher, Teresa Steinbichler, Daniel Dejaco, Herbert Riechelmann, and József Dudás. "Separation of cell survival, growth, migration, and mesenchymal transdifferentiation effects of fibroblast secretome on tumor cells of head and neck squamous cell carcinoma." Tumor Biology 39, no. 11 (November 2017): 101042831770550. http://dx.doi.org/10.1177/1010428317705507.

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Fibroblasts play a central role in tumor invasion, recurrence, and metastasis in head and neck squamous cell carcinoma. The aim of this study was to investigate the influence of tumor cell self-produced factors and paracrine fibroblast–secreted factors in comparison to indirect co-culture on cancer cell survival, growth, migration, and epithelial–mesenchymal transition using the cell lines SCC-25 and human gingival fibroblasts. Thereby, we particularly focused on the participation of the fibroblast-secreted transforming growth factor beta-1.Tumor cell self-produced factors were sufficient to ensure tumor cell survival and basic cell growth, but fibroblast-secreted paracrine factors significantly increased cell proliferation, migration, and epithelial–mesenchymal transition–related phenotype changes in tumor cells. Transforming growth factor beta-1 generated individually migrating disseminating tumor cell groups or single cells separated from the tumor cell nest, which were characterized by reduced E-cadherin expression. At the same time, transforming growth factor beta-1 inhibited tumor cell proliferation under serum-starved conditions. Neutralizing transforming growth factor beta antibody reduced the cell migration support of fibroblast-conditioned medium. Transforming growth factor beta-1 as a single factor was sufficient for generation of disseminating tumor cells from epithelial tumor cell nests, while other fibroblast paracrine factors supported tumor nest outgrowth. Different fibroblast-released factors might support tumor cell proliferation and invasion, as two separate effects.

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40

Bidey, SP, DJ Hill, and MC Eggo. "Growth factors and goitrogenesis." Journal of Endocrinology 160, no. 3 (March 1, 1999): 321–32. http://dx.doi.org/10.1677/joe.0.1600321.

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By combining data from studies of multinodular non-toxic goitre (MNTG) with data from rat models of goitre induction and in vitro models, a map of the growth factors involved in goitrogenesis has been constructed. We have addressed the roles of the insulin-like growth factors, transforming growth factors, fibroblast growth factors, endothelins, etc. We hypothesise that an imbalance in the interactions between the various growth factor axes exists in MNTG which favours cell replication. Thyrotrophin, although not significantly elevated in MNTG, exerts critical effects through interactions with autocrine and paracrine factors and their receptors. Expansion of the thyroidal vascular bed through angiogenesis is closely co-ordinated with follicular cell expansion and folliculoneogenesis, and while the integrated paracrine actions of fibroblast growth factors, vascular endothelial growth factor and endothelin probably play central roles, additional, as yet elusive, factors are probably involved. The combination of in vitro and in vivo approaches, designed to address specific questions, will undoubtedly continue to prove invaluable in dissecting further the complex interactions that exist between these growth factors, their binding proteins and receptors in goitrogenesis.

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41

Lee, G., L. R. Ellingsworth, S. Gillis, R. Wall, and P. W. Kincade. "Beta transforming growth factors are potential regulators of B lymphopoiesis." Journal of Experimental Medicine 166, no. 5 (November 1, 1987): 1290–99. http://dx.doi.org/10.1084/jem.166.5.1290.

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Members of the transforming growth factor beta (TGF-beta) family of polypeptides were found to be potent in vitro inhibitors of kappa light chain expression on normal bone marrow-derived and transformed cloned pre-B cells, and of the maturation of these cells to mitogen responsiveness. The inhibition by TGF-beta was selective in that Ia expression was not blocked. Together with the observations that LPS, IL-1, NZB serum factors, IL-4, and IFN-gamma preferentially induced either kappa or Ia, or both, on a pre-B cell line, these results further suggest that acquisition of Ig and class II molecules is independently controlled by different antagonists as well as agonists. In addition, kappa chain induction by IFN-gamma does not appear to be as sensitive to TGF-beta downregulation as that stimulated by other factors tested, and this raises the possibility that activation of the same gene may result from different transmembrane signaling pathways. In contrast to the inhibitory effects of TGF-beta on kappa acquisition by pre-B cells and on kappa increase after exposure of mature B cells to LPS, as measured by kappa RNA levels and/or surface fluorescence, no inhibition was observed on unstimulated spleen B cells or on two cloned B cell lines that constitutively produce kappa. Thus, TGF-beta may function during specific stages of B cell differentiation by inhibiting initiation of, or increased transcription of Ig genes, and therefore, may be an important negative regulator of B lymphopoiesis. It is the first natural substance found to have this effect.

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42

COMMISSIONG, JOHN W., TAKAO TAKESHIMA, JANE M. JOHNSTON, and KOTARO SHIMODA. "EFFECTS OF TRANSFORMING GROWTH FACTORS ON DOPAMINERGIC NEURONS IN CULTURE." Neurochemistry International 30, no. 4-5 (April 1997): 393–99. http://dx.doi.org/10.1016/s0197-0186(96)00074-5.

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43

Hamburger, A. W., C. P. White, and F. E. Dunn. "Secretion of transforming growth factors by primary human tumour cells." British Journal of Cancer 51, no. 1 (January 1985): 9–14. http://dx.doi.org/10.1038/bjc.1985.2.

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44

Castilla, Alberto, Jesús Prieto, and Nelson Fausto. "Transforming Growth Factors β1 and α in Chronic Liver Disease." New England Journal of Medicine 324, no. 14 (April 4, 1991): 933–40. http://dx.doi.org/10.1056/nejm199104043241401.

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45

Chang, E. B. "Transforming growth factors and intestinal epithelia: More questions than answers." Gastroenterology 97, no. 6 (December 1989): 1587–88. http://dx.doi.org/10.1016/0016-5085(89)90408-3.

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46

van der Kruijssen, C. M. M., A. Feijen, D. Huylebroeck, and A. J. M. van den Eijnden-van Raaij. "Modulation of Activin Expression by Type β Transforming Growth Factors." Experimental Cell Research 207, no. 2 (August 1993): 407–12. http://dx.doi.org/10.1006/excr.1993.1208.

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47

Leake, Robin. "Transforming growth factors alpha & beta — Positive and negative regulators of epithelial growth." European Journal of Cancer 33 (June 1997): S11. http://dx.doi.org/10.1016/s0959-8049(97)89359-8.

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48

Ellis, James S., Daniel J. Paull, Sumit Dhingra, Ashkan Khalili, Maria Notara, Steve Brocchini, and Peng T. Khaw. "Growth Factors and Ocular Scarring." European Ophthalmic Review 03, no. 02 (2009): 58. http://dx.doi.org/10.17925/eor.2009.03.02.58.

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Growth factors play a part in every stage of the wound healing process that leads to scar tissue formation. Ocular scarring can cause decreased vision or blindness by virtue of the opaque nature of the new matrix that is deposited as scar tissue (as in the lens or cornea). In addition, the contractile nature of the ocular scar tissue is the most common cause of failed retinal attachment. Scar formation after glaucoma surgery can lead to surgery failure. Growth factors, particularly the transforming growth factor (TGF-βs), play a major role in scar tissue formation in the eye and induce the synthesis of growth factors that control cell migration, proliferation, enzyme production and matrix deposition. Neurotrophins are also neuroprotective and can delay ganglion cell death, thus delaying scar formation in the retina if retinal attachment is restored promptly. Growth factors can be seen as a major target for preventing ocular scarring in the future.

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49

McWilliam, R., R. E. Leake, and J. R. T. Coutts. "Growth Factors in Human Ovarian Follicle Fluid and Growth Factor Receptors in Granulosa-Luteal Cells." International Journal of Biological Markers 10, no. 4 (October 1995): 216–20. http://dx.doi.org/10.1177/172460089501000405.

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The levels of oestradiol (E2), progesterone (P4), transforming growth factor a (TGFa), transforming growth factor β2 (TGFβ2), insulin-like growth factor I (IGF-I), platelet-derived growth factor AB (PDGF-AB) and epidermal growth factor (EGF) were measured in follicular fluids obtained from patients undergoing ovarian stimulation as part of an in vitro fertilisation program. Each of the substances was detected in all of the fluid samples tested, except TGFα (which was detected in 90% of samples tested), PDGF-AB (70%) and EGF (2%). Comparisons were made between each of these factors, follicular maturity, successful oocyte recovery and the outcome of fertilisation and embryo transfer. No statistically significant correlations were found. The presence of receptors for EGF, IGF-I and PDGF in extracts from granulosa-luteal cells isolated from follicular fluids was detected by means of Western blotting. The co-localisation of these growth factors and their receptors within the ovarian follicle suggests a likely role in control of follicular development.

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Rifkin, Daniel B., and Vesna Todorovic. "Bone matrix to growth factors: location, location, location." Journal of Cell Biology 190, no. 6 (September 20, 2010): 949–51. http://dx.doi.org/10.1083/jcb.201008116.

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The demonstration that fibrillin-1 mutations perturb transforming growth factor (TGF)–β bioavailability/signaling in Marfan syndrome (MFS) changed the view of the extracellular matrix as a passive structural support to a dynamic modulator of cell behavior. In this issue, Nistala et al. (2010. J. Cell Biol. doi: 10.1083/jcb.201003089) advance this concept by demonstrating how fibrillin-1 and -2 regulate TGF-β and bone morphogenetic protein (BMP) action during osteoblast maturation.

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Journal articles on the topic 'Transforming growth factors'

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