The antiproliferative effect of suramin on the cancer cell line sw-13 is mediated by the inhibition of transforming growth factor β1 (TGF-β1)☆

1992 ◽  
Vol 25 ◽  
pp. 17-18 ◽  
Author(s):  
R DANESI ◽  
C AGEN ◽  
N BERNARDINI ◽  
M COSTA ◽  
M DELTACCA
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Cancer Cell ◽  
Transforming Growth Factor ◽  
Cancer Cell Line ◽  
Transforming Growth Factor Β1 ◽  
Antiproliferative Effect ◽  
Tgf Β1

scholarly journals Transforming growth factor-β1-induced N-cadherin drives cell–cell communication through connexin43 in osteoblast lineage

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Yueyi Yang ◽  
Wenjing Liu ◽  
JieYa Wei ◽  
Yujia Cui ◽  
Demao Zhang ◽  
...  
Keyword(s):  
Growth Factor ◽  
Gap Junction ◽  
Cell Line ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1 ◽  
Cx43 Expression ◽  
Mc3t3 Cell ◽  
Primary Osteoblasts ◽  
Tgf Β1 ◽  
Cell Cell

AbstractGap junction (GJ) has been indicated to have an intimate correlation with adhesion junction. However, the direct interaction between them partially remains elusive. In the current study, we aimed to elucidate the role of N-cadherin, one of the core components in adhesion junction, in mediating connexin 43, one of the functional constituents in gap junction, via transforming growth factor-β1(TGF-β1) induction in osteoblasts. We first elucidated the expressions of N-cadherin induced by TGF-β1 and also confirmed the upregulation of Cx43, and the enhancement of functional gap junctional intercellular communication (GJIC) triggered by TGF-β1 in both primary osteoblasts and MC3T3 cell line. Colocalization analysis and Co-IP experimentation showed that N-cadherin interacts with Cx43 at the site of cell–cell contact. Knockdown of N-cadherin by siRNA interference decreased the Cx43 expression and abolished the promoting effect of TGF-β1 on Cx43. Functional GJICs in living primary osteoblasts and MC3T3 cell line were also reduced. TGF-β1-induced increase in N-cadherin and Cx43 was via Smad3 activation, whereas knockdown of Smad3 signaling by using siRNA decreased the expressions of both N-cadherin and Cx43. Overall, these data indicate the direct interactions between N-cadherin and Cx43, and reveal the intervention of adhesion junction in functional gap junction in living osteoblasts.

scholarly journals Restoration of RUNX3 enhances transforming growth factor-?-dependent p21 expression in a biliary tract cancer cell line

2007 ◽  
Vol 98 (6) ◽  
pp. 838-843 ◽  
Author(s):  
Kazunori Hasegawa ◽  
Shujiro Yazumi ◽  
Manabu Wada ◽  
Toshiharu Sakurai ◽  
Masaya Kida ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Cancer Cell ◽  
Biliary Tract ◽  
Biliary Tract Cancer ◽  
Transforming Growth Factor ◽  
Cancer Cell Line ◽  
Tract Cancer

scholarly journals TGF-β1 Increases GDNF Production by Upregulating the Expression of GDNF and Furin in Human Granulosa-Lutein Cells

Cells ◽  
2020 ◽  
Vol 9 (1) ◽  
pp. 185 ◽  
Author(s):  
Jingwen Yin ◽  
Hsun-Ming Chang ◽  
Yuyin Yi ◽  
Yuanqing Yao ◽  
Peter C.K. Leung
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Kinase Inhibitors ◽  
Transforming Growth Factor ◽  
Biological Response ◽  
Follicular Development ◽  
Transforming Growth Factor Β1 ◽  
Type I ◽  
High Level ◽  
Tgf Β1

Glial cell line-derived neurotrophic factor (GDNF) is expressed at a high level in the human ovary and GDNF signaling is involved in the direct control of follicular activation and oocyte maturation. Transforming growth factor-β1 (TGF-β1) plays an important role in the regulation of various ovarian functions. Furin is an intracellular serine endopeptidase of the subtilisin family that is closely associated with the activation of multiple protein precursors. Despite the important roles of GDNF and TGF-β1 in the regulation of follicular development, whether TGF-β is able to regulate the expression and production of GDNF in human granulosa cells remains to be determined. The aim of this study was to investigate the effect of TGF-β1 on the production of GDNF and its underlying mechanisms in human granulosa-lutein (hGL) cells. We used two types of hGL cells (primary hGL cells and an established immortalized hGL cell line, SVOG cells) as study models. Our results show that TGF-β1 significantly induced the expression of GDNF and furin, which, in turn, increased the production of mature GDNF. Using a dual inhibition approach combining RNA interference and kinase inhibitors against cell signaling components, we showed that the TβRII type II receptor and ALK5 type I receptor are the principal receptors that mediated TGF-β1-induced cellular activity in hGL cells. Additionally, Sma- and Mad-related protein (SMAD)3 and SMAD4 are the downstream signaling transducers that mediate the biological response induced by TGF-β1. Furthermore, furin is the main proprotein convertase that induces the production of GDNF. These findings provide additional regulatory mechanisms by which an intrafollicular factor influences the production of another growth factor through a paracrine or autocrine interaction in hGL cells.

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