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- W2092824717 abstract "Background/Aims: Transforming growth factor-β1(TGF-β1) plays a pivotal role in the extracellular matrix accumulation observed in fibrotic diseases. Endoglin is an important component of the TGF-βreceptor complex highly expressed in tissues undergoing fibrotic processes. Endoglin expression regulates the effect of TGF-β on extracellular matrix synthesis. The purpose of our study has been to understand the molecular mechanism by which endoglin exerts its effects on fibrosis and the possible role of MAP kinases in these effects. Methods: We have assessed in mock and in endoglin-transfected L6E9 myoblasts the effect of TGF-β1 on collagen mRNA by Northern blot and effect of TGF-β1 on collagen content in the cultured medium by [3H]-Proline incorporation into collagen proteins. Total and activated MAPK and their role on collagen synthesis were assessed by Western blot. Results: TGF-β1 induced an increase on α2 (I) collagen mRNA expression and collagen accumulation in mock-transfected myoblasts,whereas the response was much lower in endoglintransfected cells. TGF-β1 activated the ERK1/2 and p38 MAPK pathways but not the JNK pathway in L6E9 myoblasts. TGF-β1-induced α2 (I) collagen mRNA expression and collagen accumulation were completely inhibited by SB203580, in either mock or endoglintransfected myoblasts. PD98059 increased TGF-β1 induced-collagen synthesis and accumulation in endoglin-transfected myoblasts but not in mock cells. Conclusion: Our studies demonstrate that TGF-β1-induced collagen synthesis is mediated by p38 MAPK activation in L6E9 myoblasts. Furthermore, endoglin expression reduces basal and TGF-β1 induced collagen synthesis when ERK1/2 pathway is operating." @default.
- W2092824717 created "2016-06-24" @default.
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- W2092824717 date "2006-01-01" @default.
- W2092824717 modified "2023-10-01" @default.
- W2092824717 title "Endoglin Modulation of TGF-ß1-Induced Collagen Synthesis is Dependent on ERK1/2 MAPK Activation" @default.
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- W2092824717 doi "https://doi.org/10.1159/000095181" @default.
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