Transforming growth factor‐β1 induces collagen synthesis and accumulation via p38 mitogen‐activated protein kinase (MAPK) pathway in cultured L6E9 myoblasts

FEBS Letters

Yuste, L³  López-Novoa, J.M¹  Rodrı́guez-Peña, A¹  Obreo, J¹  Montero, J.C³  Rodrı́guez-Barbero, A¹  Bernabéu, C²  Pandiella, A³ 

[1] Instituto ‘Reina Sofı́a’ de Investigación Nefrológica, Departamento de Fisiologı́a y Farmacologı́a, Universidad de Salamanca, Salamanca, Spain;Centro de Investigaciones Biológicas, Consejo Superior de Investigaciónes Cientı́ficas (CSIC), Velázquez 144, 28006 Madrid, Spain;Instituto de Microbiologı́a y Bioquı́mica, Consejo Superior de Investigaciones Cientı́ficas, Universidad de Salamanca, Edificio Departamental, Campus Miguel de Unamuno, Avda. Campo Charro s/n, 37007 Salamanca, Spain

关键词: Extracellular matrix;    Fibrosis;    Signaling;    Transforming growth factor-β1;   

DOI  :  10.1016/S0014-5793(02)02337-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Transforming growth factor-β (TGF-β) plays a pivotal role in the extracellular matrix accumulation observed in chronic progressive tissue fibrosis, but the intracellular signaling mechanism by which TGF-β stimulates this process remains poorly understood. We examined whether mitogen-activated protein kinase (MAPK) routes were involved in TGF-β1-induced collagen expression in L₆E₉ myoblasts. TGF-β1 induced p38 and extracellular signal-regulated kinase (ERK) 1/2 phosphorylation whereas no effect on Jun N-terminal kinase phosphorylation was observed. Biochemical blockade of p38 but not of the ERK MAPK pathway abolished TGF-β1-induced α₂(I) collagen mRNA expression and accumulation. These data indicate that TGF-β1-induced p38 activation is involved in TGF-β1-stimulated collagen synthesis.

【 授权许可】

Unknown