Contrasting effect of transforming growth factor type beta 1 (TGF-β1) on proliferation and interleukin-2 receptor expression in activated and rapidly cycling immature (CD3−CD4−CD8−) thymocytes

1993 ◽  
Vol 154 (1) ◽  
pp. 44-52 ◽  
Author(s):  
Arnaud Dupuy d'Angeac ◽  
Thierry Rème ◽  
Serge Monier ◽  
Qinglin Gao ◽  
Christophe Duperray ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Interleukin 2 ◽  
Receptor Expression ◽  
Interleukin 2 Receptor ◽  
Contrasting Effect ◽  
Factor Type ◽  
Tgf Β1

Transforming growth factor type beta 1 (TGF-?1) down-regulates interleukin-2 production and up-regulates interleukin-2 receptor expression in a thymoma cell line

1991 ◽  
Vol 147 (3) ◽  
pp. 460-469 ◽  
Author(s):  
Arnaud Dupuy D'Angeac ◽  
Jacques Dornand ◽  
Xavier Emonds-Alt ◽  
Pierre Jullien ◽  
Jose A. Garcia-Sanz ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Transforming Growth Factor ◽  
Interleukin 2 ◽  
Receptor Expression ◽  
Interleukin 2 Receptor ◽  
Factor Type

scholarly journals Angiotensin-(1-7) Prevents Skeletal Muscle Atrophy Induced by Transforming Growth Factor Type Beta (TGF-β) via Mas Receptor Activation

2016 ◽  
Vol 40 (1-2) ◽  
pp. 27-38 ◽  
Author(s):  
Johanna Ábrigo ◽  
Felipe Simon ◽  
Daniel Cabrera ◽  
Claudio Cabello-Verrugio
Keyword(s):  
Skeletal Muscle ◽  
Growth Factor ◽  
Western Blot ◽  
Muscle Atrophy ◽  
Transforming Growth Factor ◽  
Fibre Diameter ◽  
Skeletal Muscle Atrophy ◽  
Mas Receptor ◽  
Factor Type ◽  
Tgf Β1

Background: Transforming growth factor type beta 1 (TGF-β1) produces skeletal muscle atrophy. Angiotensin-(1-7) (Ang-(1-7)), through the Mas receptor, prevents the skeletal muscle atrophy induced by sepsis, immobilization, or angiotensin II (Ang-II). However, the effect of Ang-(1-7) on muscle wasting induced by TGF-β1 is unknown. Aim: To evaluate whether Ang-(1-7)/Mas receptor axis could prevent the skeletal muscle atrophy induced by TGF-β1. Methods: This study assessed the atrophic effect of TGF-β1 in C2C12 myotubes and mice in absence or presence of Ang-(1-7), and the receptor participation using A779, an antagonist of the Mas receptor. The levels of myosin heavy chain (MHC), polyubiquitination, and MuRF-1 were detected by western blot. Myotube diameter was also evaluated. In vivo analysis included the muscle strength, fibre diameter, MHC and MuRF-1 levels by western blot, and ROS levels by DCF probe detection. Results: The results showed that Ang-(1-7) prevented the increase in MuRF-1 and polyubiquitined protein levels, the decrease of MHC levels, the myotubes/fibre diameter diminution, and the increased production of reactive oxygen species (ROS) induced by TGF-β1. Utilizing A779 inhibited the anti-atrophic effect of Ang-(1-7). Conclusion: The preventive effect of Ang-(1-7) on skeletal muscle atrophy induced by TGF-β1 is produced through inhibition of ROS production and proteasomal degradation of MHC.

Transforming growth factor type-β inhibits Mas receptor expression in fibroblasts but not in myoblasts or differentiated myotubes; Relevance to fibrosis associated to muscular dystrophies

BioFactors ◽  
2015 ◽  
Vol 41 (2) ◽  
pp. 111-120 ◽  
Author(s):  
Catalina Cofre ◽  
María José Acuña ◽  
Osvaldo Contreras ◽  
María Gabriela Morales ◽  
Cecilia Riquelme ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Receptor Expression ◽  
Muscular Dystrophies ◽  
Mas Receptor ◽  
Factor Type

scholarly journals Transforming Growth Factor-β Inhibits Lipopolysaccharide-Stimulated Expression of Inflammatory Cytokines in Mouse Macrophages through Downregulation of Activation Protein 1 and CD14 Receptor Expression

2000 ◽  
Vol 68 (5) ◽  
pp. 2418-2423 ◽  
Author(s):  
Kenichi Imai ◽  
Akira Takeshita ◽  
Shigemasa Hanazawa
Keyword(s):  
Septic Shock ◽  
Growth Factor ◽  
Inflammatory Cytokines ◽  
Transforming Growth Factor ◽  
Inflammatory Responses ◽  
Consensus Sequence ◽  
Receptor Expression ◽  
Necrosis Factor Alpha ◽  
Mouse Macrophages ◽  
Tgf Β1

ABSTRACT The septic shock that occurs in gram-negative infections is caused by a cascade of inflammatory cytokines. Several studies showed that transforming growth factor-β1 (TGF-β1) inhibits this septic shock through suppression of expression of the lipopolysaccharide (LPS)-induced inflammatory cytokines. In this study, we investigated whether TGF-β1 inhibition of LPS-induced expression of inflammatory cytokines in the septic shock results from downregulation of LPS-stimulated expression of CD14, an LPS receptor. TGF-β1 markedly inhibited LPS stimulation of CD14 mRNA and protein levels in mouse macrophages. LPS-stimulated expression of CD14 was dramatically inhibited by addition of antisense, but not sense, c-fosand c-jun oligonucleotides. Since TGF-β1 pretreatment inhibited LPS-stimulated expression of c-fos and c-jun genes and also the binding of nuclear proteins to the consensus sequence of the binding site for activation protein 1 (AP-1), a heterodimer of c-Fos and c-Jun, in the cells, TGF-β1 inhibition of CD14 expression may be a consequence of downregulation of AP-1. LPS-stimulated expression of interleukin-1β and tumor necrosis factor alpha genes in the cells was inhibited by addition of CD14 antisense oligonucleotide. Also, TGF-β1 inhibited the LPS-stimulated production of both inflammatory cytokines by the macrophages. In addition, TGF-β1 inhibited expression of the two cytokines in several organs of mice receiving LPS. Thus, our results suggest that TGF-β1 inhibition of LPS-stimulated inflammatory responses resulted from downregulation of CD14 and also may be a possible mechanism of TGF-β1 inhibition of LPS-induced septic shock.

scholarly journals Erratum for: Transforming growth factor type-β inhibits Mas receptor expression in fibroblasts but not in myoblasts or differentiated myotubes; Relevance to fibrosis associated to muscular dystrophies

BioFactors ◽  
2015 ◽  
Vol 41 (3) ◽  
pp. 209-209
Author(s):  
Catalina Cofre ◽  
María José Acuña ◽  
Osvaldo Contreras ◽  
María Gabriela Morales ◽  
Cecilia Riquelme ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Receptor Expression ◽  
Muscular Dystrophies ◽  
Mas Receptor ◽  
Factor Type

scholarly journals Proteinases are isoform-specific regulators of the binding of transforming growth factor β to α2-macroglobulin

1996 ◽  
Vol 320 (2) ◽  
pp. 551-555 ◽  
Author(s):  
Donna J. WEBB ◽  
Alissa M. WEAVER ◽  
Tara L. ATKINS-BRADY ◽  
Steven L. GONIAS
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Serine Proteinase ◽  
Transforming Growth Factor Β ◽  
Cell Types ◽  
Receptor Expression ◽  
Α2 Macroglobulin ◽  
Kd Values ◽  
Factor Α ◽  
Tgf Β1

α2-Macroglobulin (α2M) regulates growth and gene expression in many cell types by binding and neutralizing transforming growth factor β (TGF-β). In this study we characterized the effects of the serine proteinase, plasmin, on the interaction of α2M with TGF-β1 and TGF-β2. Binding of both TGF-β isoforms to purified α2M–plasmin complex was primarily non-covalent and reversible. The binding affinity of α2M for TGF-β1 was increased by plasmin; the Kd values were 320 and 84 nM for native α2M and α2M–plasmin respectively. In contrast the affinity of α2M for TGF-β2 was decreased by plasmin; the Kd values were 14 and 80 nM for native α2M and α2M–plasmin respectively. Thrombin decreased the affinity of α2M for TGF-β2 in a similar manner to plasmin. In assays of DNA synthesis in fetal bovine heart endothelial cells, native α2M neutralized the activity of exogenously added TGF-β2, whereas α2M–plasmin, at equivalent concentrations, had almost no effect. Native α2M and methylamine-modified α2M increased platelet-derived growth factor α-receptor expression in vascular smooth-muscle cells, an activity attributed to the neutralization of autocrine TGF-β activity, whereas α2M–plasmin was less effective at the same concentration. These studies demonstrate that the effects of proteinases on the cytokine-binding and cytokine-neutralizing activities of α2M are cytokine-dependent. By reacting with α2M, proteinases might regulate not only the availability of cytokines in the extracellular spaces but also the composition of the cytokine milieu.

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