2000
DOI: 10.1016/s0898-6568(00)00120-0
|View full text |Cite
|
Sign up to set email alerts
|

Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

8
78
0

Year Published

2004
2004
2016
2016

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 104 publications
(86 citation statements)
references
References 40 publications
8
78
0
Order By: Relevance
“…These observations suggest an important role of endocytosis induced by the T␤RII-p38 MAPK signaling pathway in activating endothelial proliferation and reducing endothelial apoptosis. Our results are in agreement with studies showing that p38 MAPK activation is a crucial determinant of cell proliferation (6,13).…”
Section: Discussionsupporting
confidence: 93%
“…These observations suggest an important role of endocytosis induced by the T␤RII-p38 MAPK signaling pathway in activating endothelial proliferation and reducing endothelial apoptosis. Our results are in agreement with studies showing that p38 MAPK activation is a crucial determinant of cell proliferation (6,13).…”
Section: Discussionsupporting
confidence: 93%
“…For example, ADAM12 cell signaling may positively influence myogenesis, because membrane-bound ADAM12 activates phosphatidylinositol (PI) 3-kinase by mediating its recruitment to the membrane , active PI 3-kinase being crucially involved in terminal differentiation of myogenic cells (Jiang et al, 1998;Li et al, 2000). Moreover, the ADAM12 cytoplasmic tail binds ␣-actinin 1 and 2 (Galliano et al, 2000;Cao et al, 2001), this binding being required for full-blown fusion of C2C12 myogenic cells (Galliano et al, 2000).…”
Section: Discussionmentioning
confidence: 99%
“…on April 7, 2019 by guest http://mcb.asm.org/ shown to be crucial for myogenesis (5,9,10,32,44,62,66). Both inactivation and hyperactivation of Cdc42 or Rac-1 result in inhibition of myogenesis (reference 36 and references therein), pointing to a complex regulation of myogenic differentiation and a delicate equilibrium between promyogenic and antimyogenic signaling pathways.…”
Section: Vol 24 2004 Rage Engagement Stimulates Myogenesis 4891mentioning
confidence: 99%
“…However, IGF I and IGF II were reported to promote or inhibit myogenic differentiation depending on the absence or presence of TNF-␣, respectively (16), and down-regulation of nerve growth factor low-affinity receptor was shown to be required for myoblast terminal differentiation (12). Signaling pathways implicated in the transduction of the effects of these agents acting on myoblasts include (i) the mitogen-activated protein (MAP) kinase (MAPK) p38 and Akt, the activation of which is required for myogenesis (5,9,10,17,32,44,55,57,62,66); (ii) an NF-B-dependent pathway activated by cytokines such as TNF-␣, which interferes with myogenesis (30); (iii) a PW1-dependent, NF-Bindependent activation of caspases in the absence of apoptosis (8); (iv) the Ras-MEK-extracellular signal-regulated kinase (ERK) pathway, which suppresses myogenesis (4,42,43,61) but is required at a later stage of muscle differentiation (4); and (v) activation of inducible nitric oxide synthase via NF-B, which results in stimulation of myogenesis (25).Recently, we found that S100B, a member of a multigenic family of Ca 2ϩ -modulated proteins of the EF-hand type with both intracellular and extracellular regulatory activities (11,19), inhibited myoblast differentiation and myotube formation when administered to the rat myoblast cell line L6 (51). Inhibition of myogenesis was registered at picomolar doses of S100B and was reversible, pointing to S100B binding to a cell surface receptor with a relatively high affinity.…”
mentioning
confidence: 99%