Kudla A J, John M L, Bowen-Pope D F, Rainish B, Olwin B B
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Mol Cell Biol. 1995 Jun;15(6):3238-46. doi: 10.1128/MCB.15.6.3238.
The distinct effects of cytokines on cellular growth and differentiation suggest that specific signaling pathways mediate these diverse biological activities. Fibroblast growth factors (FGFs) are well-established inhibitors of skeletal muscle differentiation and may operate via activation of specific signaling pathways distinct from recently identified mitogen signaling pathways. We examined whether platelet-derived growth factor (PDGF)-activated signaling pathways are sufficient to mediate FGF-dependent repression of myogenesis by introducing the PDGF beta receptor into a mouse skeletal muscle cell line. Addition of PDGF-BB to cells expressing the PDGF beta receptor activated the PDGF beta receptor tyrosine kinase, stimulated mitogen-activated protein (MAP) kinase, and increased the steady-state levels of junB and c-fos mRNAs. Despite the activation of these intracellular signaling molecules, PDGF beta receptor activation elicited no detectable effect on cell proliferation or differentiation. In contrast to PDGF-BB, addition of FGF-2 to myoblasts activated signaling pathways that resulted in DNA synthesis and repression of differentiation. Because of the low number of endogenous FGF receptors expressed, FGF-stimulated signaling events, including tyrosine phosphorylation and activation of MAP kinase, could be detected only in cells expressing higher levels of a transfected FGF receptor cDNA. As the PDGF beta receptor- and FGF receptor-stimulated signaling pathways yield different biological responses in these skeletal muscle cells, we hypothesize that FGF-mediated repression of skeletal muscle differentiation activates signaling pathways distinct from those activated by the PDGF beta receptor. Activation of PDGF beta receptor tyrosine kinase activity, stimulation of MAP kinase, and upregulation of immediate-early gene expression are not sufficient to repress skeletal muscle differentiation.
细胞因子对细胞生长和分化的独特影响表明,特定的信号通路介导了这些多样的生物学活性。成纤维细胞生长因子(FGFs)是公认的骨骼肌分化抑制剂,可能通过激活与最近发现的丝裂原信号通路不同的特定信号通路发挥作用。我们通过将血小板衍生生长因子(PDGF)β受体导入小鼠骨骼肌细胞系,研究了PDGF激活的信号通路是否足以介导FGF依赖的肌生成抑制作用。向表达PDGFβ受体的细胞中添加PDGF-BB可激活PDGFβ受体酪氨酸激酶,刺激丝裂原活化蛋白(MAP)激酶,并增加junB和c-fos mRNA的稳态水平。尽管这些细胞内信号分子被激活,但PDGFβ受体激活对细胞增殖或分化未产生可检测到的影响。与PDGF-BB相反,向成肌细胞中添加FGF-2可激活导致DNA合成和分化抑制的信号通路。由于内源性FGF受体表达数量较少,FGF刺激的信号事件,包括酪氨酸磷酸化和MAP激酶的激活,仅在表达较高水平转染FGF受体cDNA的细胞中才能检测到。由于PDGFβ受体和FGF受体刺激的信号通路在这些骨骼肌细胞中产生不同的生物学反应,我们推测FGF介导的骨骼肌分化抑制激活了与PDGFβ受体激活的信号通路不同的信号通路。PDGFβ受体酪氨酸激酶活性的激活、MAP激酶的刺激以及早期即刻基因表达的上调不足以抑制骨骼肌分化。