J C Chambard's research while affiliated with French National Centre for Scientific Research and other places

... For instance, the epidermal growth factor (EGF) is constitutively expressed in some cell types (Wong and Wright 1999 ). Cytokines typically exert several biological activities in multiple cell types and the overlapping activity from different cytokines is a common phenomenon called cross-talk (Paris et al. 1988 ;Sun et al. 1999 ). ...

... ETS2, a pivotal member of the ETS family of transcription factors, plays a crucial role in various cellular processes, including cell proliferation, differentiation, apoptosis, and tumorigenesis [3][4][5][6][7][8][9][10]. Understanding the regulatory mechanisms and identifying the interacting partners of ETS2 is of utmost importance due to its intricate involvement in these fundamental cellular events. ...

... Interestingly, the proteomics data reported an overall lower MyoD expression for myoblasts cultured on soft substrates (Fig. 7B), while desmin, a myogenic commitment marker, was expressed at a higher level on stiff substrate (Fig. 7B). Furthermore, JUNB, which has been previously reported to suppress myogenin expression (Li et al., 1992), was found to express at a higher level on soft substrate (Fig. 7B). Our immunocytochemical analysis suggests that there may not have been a major divergence in the Pax7/MyoD myogenic fate landscape across the two substrate stiffness levels at the 45-hour time-point post-seeding in growth medium. ...

... This type of mechanism has been convincingly demonstrated for LPA, ET-1, and thrombin (Daub et al., 1996;Arora et al., 2008). Independent of cross-talk, however, we have demonstrated that thrombin stimulates the proliferation of human glioblastoma cells through activation of G 12/13 and RhoA and subsequent regulation of the transcription factor, activating protein-1 (AP-1) and its target genes (Trejo et al., 1992;Aragay et al., 1995;Post et al., 1996;Majumdar et al., 1998;Walsh et al., 2008a). Our work and other studies examining the regulation of AP-1 through RhoA are discussed in this review. ...

... Of four PARs that have been described, three are activated by the protease thrombin (PAR-1, PAR-3 and PAR-4), whereas PAR-2 is sensitive to trypsin [3, 4]. PAR-1 has been found in various tissues and cells of species ranging from human to Xe- nopus5678. Tethered ligand peptides, mimicking the neo-aminoterminus, are capable of activating PAR-1 [9] . However, analysis of one of thrombin's most important functions, stimulation of platelet activation, has presented an interesting paradox and has initiated the search for additional thrombin receptors other than the original thrombin receptor, PAR-1. ...

... 51 There is also some evidence of HIF1α regulation of STAT3. 52 Additionally, STAT3 and HIF1α cooperatively activate HIF1 target genes in MDA-MB-231 and RCC4 cells. 53 As IL-2 appears to be integral to haNK cell resistance to hypoxia, it is reasonable to hypothesize that IL-2 influences STAT3 phosphorylation. ...

... Several GPCRs and heterotrimeric G proteins were found to control cellular proliferation and differentiation (Dhanasekaran et al., 1995; Lorenz et al., 2000; Moolenaar, 1991; Post and Brown, 1996; Pouyssegur et al., 1988; van Corven et al., 1989). Moreover, activated Gα proteins can cause malignant transformation of cultured cells and have been implicated in the formation of human cancer (Dhanasekaran et al., 1995). ...

... Although controversial data have been reported concerning the receptor subtype(s) that are responsible for the biphasic effects of ANG II on proximal tubular transport [87,88], some studies have clearly indicated that both luminal and basolateral AT1A receptors mediate the biphasic effects of Ang II on proximal transport [89][90][91]. It has been shown that at physiological concentrations, binding between ANG II and the AT1 receptor induces the rapid activation of PLC, which results in the release of IP3 and DAG, which are themselves involved in slightly increasing [Ca 2+ ]i by mobilizing Ca 2+ from intracellular storage and by activating PKC, respectively [92][93][94]. These processes may ultimately result in the activation of ERK [71,83,90]. ...

... To identify growth factors in 10ϫ hMSC-CM, we measured concentrations of 40 growth factors by using an antibody array chip (Table 1). Among them, we assessed involvement of FGF2, TGF-␤ 1 , and VEGF, which are known to enhance fibroblast proliferation (27,28,47), with each blocking antibody. Antibodies against FGF2, TGF-␤ 1 , and VEGF significantly suppressed hMSC-CM-induced proliferation of NHLFs that were not exposed to CSE (Fig. 10A). ...

... Traces of aluminum are present in food and in the organism, thus, in human studies with sodium fluoride and with fluoridated water, fluoroaluminate is also likely to be an active molecular species. Fluoroaluminate has been known to cell biologists as an agent that directly stimulates cellular heterotrimeric G proteins, and thereby mimics the signaling of G protein-coupled, seven-transmembrane receptors (19,20). Thus, fluoride, in the form of fluoroaluminate, could activate G proteins on osteoblasts and induce bone formation. ...