Suppression of Keratin 15 Expression by Transforming Growth Factor β in Vitro and by Cutaneous Injury in Vivo

2000 ◽  
Vol 254 (1) ◽  
pp. 80-90 ◽  
Author(s):  
Silke Werner ◽  
Sabine Werner ◽  
Barbara Munz
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Cutaneous Injury

scholarly journals Estrogen Protects Lenses against Cataract Induced by Transforming Growth Factor-β (TGFβ)

1997 ◽  
Vol 185 (2) ◽  
pp. 273-280 ◽  
Author(s):  
Angela M. Hales ◽  
Coral G. Chamberlain ◽  
Christopher R. Murphy ◽  
John W. McAvoy
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Hormone Replacement ◽  
Transforming Growth Factor Β ◽  
Epidemiological Studies ◽  
Female Rats ◽  
World Population ◽  
Damaging Effects

Cataract, already a major cause of visual impairment and blindness, is likely to become an increasing problem as the world population ages. In a previous study, we showed that transforming growth factor-β (TGFβ) induces rat lenses in culture to develop opacities and other changes that have many features of human subcapsular cataracts. Here we show that estrogen protects against cataract. Lenses from female rats are more resistant to TGFβ-induced cataract than those from males. Furthermore, lenses from ovariectomized females show increased sensitivity to the damaging effects of TGFβ and estrogen replacement in vivo, or exposure to estrogen in vitro, restores resistance. Sex-dependent and estrogen-related differences in susceptibility to cataract formation, consistent with a protective role for estrogen, have been noted in some epidemiological studies. The present study in the rat indicates that estrogen provides protection against cataract by countering the damaging effects of TGFβ. It also adds to an increasing body of evidence that hormone replacement therapy protects postmenopausal women against various diseases.

scholarly journals NIM811 downregulates transforming growth factor-β signal transduction in vivo and in vitro

2015 ◽  
Vol 13 (1) ◽  
pp. 522-528 ◽  
Author(s):  
JING CHEN ◽  
DIAN-GANG LIU ◽  
HUI WANG ◽  
XIAO-NING WU ◽  
MIN CONG ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β

scholarly journals Transforming Growth Factor β and Immunosuppression in Experimental Visceral Leishmaniasis

1998 ◽  
Vol 66 (3) ◽  
pp. 1233-1236 ◽  
Author(s):  
Virmondes Rodrigues ◽  
João Santana da Silva ◽  
Antonio Campos-Neto
Keyword(s):  
T Cells ◽  
Growth Factor ◽  
Visceral Leishmaniasis ◽  
Leishmania Donovani ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Spleen Cells ◽  
Immunohistochemical Studies

ABSTRACT Hamsters infected with Leishmania donovani develop a disease similar to human kala-azar. They present hypergammaglobulinemia, and their T cells do not respond to parasite antigens. This unresponsiveness has been primarily ascribed to defects in antigen-presenting cells (APCs), because these cells are unable to stimulate proliferation of parasite-specific T cells from immunized animals. In this study, we show that APCs (adherent spleen cells) fromL. donovani-infected hamsters produce high levels of the inhibitory cytokine transforming growth factor β (TGF-β). Immunohistochemical studies with an anti-TGF-β monoclonal antibody (MAb) showed that this cytokine is abundantly produced in vivo by the spleen cells of infected animals. In addition, high levels of TGF-β are produced in vitro by infected hamster cells, either spontaneously or after stimulation with parasite antigen or lipopolysaccharide. Furthermore, in vivo-infected adherent cells obtained from spleens ofL. donovani-infected hamsters caused profound inhibition of the in vitro antigen-induced proliferative response of lymph node cells from hamsters immunized with leishmanial antigens. Moreover, this inhibition was totally abrogated by the anti-TGF-β MAb. These results suggest that the immunosuppression observed in visceral leishmaniasis is, at least in part, due to the abundant production of TGF-β during the course of the infection.

scholarly journals Role of the Latent Transforming Growth Factor β-Binding Protein 1 in Fibrillin-Containing Microfibrils in Bone Cells In Vitro and In Vivo

2000 ◽  
Vol 15 (1) ◽  
pp. 68-81 ◽  
Author(s):  
Sarah L. Dallas ◽  
Douglas R. Keene ◽  
Scott P. Bruder ◽  
Juha Saharinen ◽  
Lynn Y. Sakai ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Bone Cells ◽  
Binding Protein ◽  
Transforming Growth Factor Β

scholarly journals Transforming Growth Factor-β Mediates Intestinal Healing and Susceptibility to Injury in Vitro and in Vivo Through Epithelial Cells

2003 ◽  
Vol 162 (2) ◽  
pp. 597-608 ◽  
Author(s):  
Paul L. Beck ◽  
Ian M. Rosenberg ◽  
Ramnik J. Xavier ◽  
Theodore Koh ◽  
Josée F. Wong ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β

scholarly journals Induction of Sonic Hedgehog Mediators by Transforming Growth Factor-β: Smad3-Dependent Activation of Gli2 and Gli1 Expression In vitro and In vivo

2007 ◽  
Vol 67 (14) ◽  
pp. 6981-6986 ◽  
Author(s):  
Sylviane Dennler ◽  
Jocelyne André ◽  
Ismini Alexaki ◽  
Allen Li ◽  
Thierry Magnaldo ◽  
...  
Keyword(s):  
Growth Factor ◽  
Sonic Hedgehog ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Gli1 Expression

scholarly journals Transforming Growth Factor-β Receptors Interact with AP2 by Direct Binding to β2 Subunit

2002 ◽  
Vol 13 (11) ◽  
pp. 4001-4012 ◽  
Author(s):  
Diying Yao ◽  
Marcelo Ehrlich ◽  
Yoav I. Henis ◽  
Edward B. Leof
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Type I ◽  
Coated Pits ◽  
Wide Range ◽  
Cytoplasmic Tails ◽  
Direct Binding

Transforming growth factor-β (TGF-β) superfamily members regulate a wide range of biological processes by binding to two transmembrane serine/threonine kinase receptors, type I and type II. We have previously shown that the internalization of these receptors is inhibited by K+ depletion, cytosol acidification, or hypertonic medium, suggesting the involvement of clathrin-coated pits. However, the involvement of the clathrin-associated adaptor complex AP2 and the identity of the AP2 subunit that binds the receptors were not known. Herein, we have studied these issues by combining studies on intact cells with in vitro assays. Using fluorescence photobleaching recovery to measure the lateral mobility of the receptors on live cells (untreated or treated to alter their coated pit structure), we demonstrated that their mobility is restricted by interactions with coated pits. These interactions were transient and mediated through the receptors' cytoplasmic tails. To measure direct binding of the receptors to specific AP2 subunits, we used yeast two-hybrid screens and in vitro biochemical assays. In contrast to most other plasma membrane receptors that bind to AP2 via the μ2 subunit, AP2/TGF-β receptor binding was mediated by a direct interaction between the β2-adaptin N-terminal trunk domain and the cytoplasmic tails of the receptors; no binding was observed to the μ2, α, or ς2 subunits of AP2 or to μ1 of AP1. The data uniquely demonstrate both in vivo and in vitro the ability of β2-adaptin to directly couple TGF-β receptors to AP2 and to clathrin-coated pits, providing the first in vivo evidence for interactions of a transmembrane receptor with β2-adaptin.

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