The role of fibroblast growth factor receptor1 in human ESC adhesion signalling and proliferation

MATULKA, Kamil, Michaela KUNOVÁ, Aleš HAMPL, Yuh-Man SUN a Petr DVOŘÁK. The role of fibroblast growth factor receptor1 in human ESC adhesion signalling and proliferation. Online. In ISSCR 10th Annual Meeting, 13.-.16.6.2012, Yokohama, Japonsko. 2012, [citováno 2024-04-23]

Základní údaje

• Originální název: The role of fibroblast growth factor receptor1 in human ESC adhesion signalling and proliferation
• Autoři: MATULKA, Kamil, Michaela KUNOVÁ, Aleš HAMPL, Yuh-Man SUN a Petr DVOŘÁK
• Vydání: ISSCR 10th Annual Meeting, 13.-.16.6.2012, Yokohama, Japonsko, 2012.

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Konferenční abstrakt
• Stát vydavatele: Japonsko
• Utajení: není předmětem státního či obchodního tajemství
• Organizační jednotka: Lékařská fakulta
• Příznaky: Mezinárodní význam

Anotace

Basic fibroblast growth factor (FGF-2) promotes self-renewal, survival, and adhesion of human ESCs. The diverse functions of FGF-2 may be attributed to its interactions with various fibroblast growth factor receptors (FGFRs), which in turn lead to different signalling cascades. Our study explores the role of FGFR1 in the human ESC adhesion, signalling and proliferation. FGFRs are tyrosine kinase receptors involved in a broad range of developmental processes, but their functions or expression often is dysregulated in developmental malignancies and cancers. Our data showed that hESCs express all types of FGFRs (1, 2, 3 and 4), to which FGFR1 is the most abundant. Intriguingly, the phosphorylation induced by FGF-2 treatment in FGFR1 is the least amongst the FGFRs. Our results suggest that the tepid reaction of FGFR1 to FGF-2 in phosphorylation implicates the action of FGFR1 in non-canonical FGF pathway. We also observed that FGFR1 localises mainly in the cell membranes where the cell-to-cell contacts occur. We also found that FGFR1 co-stains with ZO-1 protein, which is involved in tight junction assembly. Interestingly, in lower density cultures, we observed that FGFR1 and ZO-1 co-localise in nucleus in addition to the location in the cell membrane. Our data suggest that FGFR1 may play a role in cell adhesion and contact inhibition. Herein, we propose a potential novel role of FGFR1 in the microenvironment of human ESC interactions.