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Results show that Spry1a, 2 and 4 have partially overlapping expression in developing and regenerating Xenopus limbs, which correspond with known areas of Fgf signaling.
Data show that the intracellular domain of PAPC interacts with Sprouty (Spry), and upon binding to PAPC, Spry function is inhibited and PCP signaling is enhanced.
Here we show that Xenopus laevis Sprouty2 (XSpry2) controls the duration of ERK activity and thereby contributes to the establishment of dorsoventral patterning during mesoderm formation.
Overexpression of miR-592 promotes GC proliferation, migration, and invasion and induces the EMT via the PI3K/AKT and MAPK/ERK signaling pathways by inhibiting Spry2, suggesting a potential therapeutic target for Gastric cancer.
nuclear Spry2 acts as a molecular link which co-ordinates airway and vascular growth of the cardiopulmonary system.
activation of ERK1/2 signaling was required for hCG-induced up-regulation of SPRY2 expression. Further, SPRY2 knockdown attenuated the AREG-induced COX-2 expression and PGE2 production by inhibiting AREG-activated ERK1/2 signaling.
Result demonstrated that SPRY2 low-expression was significantly associated with unfavorable prognosis of gastric adenocarcinoma and that SPRY2 could inhibit FGFR2-induced ERK phosphorylation and suppress FGFR2-elicited gastric cancer cell proliferation and invasion.
Sprouty2 inhibits amphiregulin-induced down-regulation of E-cadherin and cell invasion in human ovarian cancer cells.
Sprouty2 (Spry2), a negative regulator of the extracellular signal regulated kinase/mitogen-activated protein kinase (Erk/MAPK) signalling pathway, was a downstream target of miR-122-5p possibly involved in regulating the keratinocyte proliferation.
results shows the involvement of Spry2 in regulation of FosB and Runx2 genes, MAPK signaling and proliferation of mesenchymal stem cells.
MYB acts on MAPK signaling by directly regulating transcription of the gene encoding the negative modulator SPRY2.
ZEB1 upregulation by SPRY2 results from the combined induction of ETS1 transcription factor and the repression of microRNAs (miR-200 family, miR-150) that target ZEB1 RNA. Moreover, SPRY2 increased AKT activation by epidermal growth factor, whereas AKT and also Src inhibition reduced the induction of ZEB1.
upregulated in human CRC. Suppression of SPRY2 repressed AKT2 and EMT-inducing transcription factors and significantly increased E-cadherin expression. Concurrent downregulation of SPRY1 and SPRY2 also increased E-cadherin and suppressed mesenchymal markers in colon cancer cells.
In cells harbouring a K-Ras mutation the serine conversion weakens the reduction of migration velocity indicating that dependent on the status of K-Ras the serine influences Sprouty2 functions differently.
Increased nuclear localization of p21(WAF1/CIP1) in SPRY2 downregulated colon cancer cells may explain the inhibition of cell proliferation in colon cancer cells.
Data suggest a common mechanism by which DNA methyltransferase1 (DNMT1) and hypoxia inducible factors HIF1alpha/HIF2alpha regulate Sprouty2 (Spry2) transcription.
We showed that Spry2 is a novel unfolded protein response target and its upregulation is dependent on PERK.
has an inhibitory role in TGFbeta signaling pathway in lens epithelial cells
these results establish SPRY2 as a critical negative regulator of BCR-mediated MAPK-Erk signaling in chronic lymphocytic leukemia , thereby providing one of the molecular mechanisms to explain the clinical heterogeneity of chronic lymphocytic leukemia.
spry2 can inhibit MM cell growth and survival with a concomitant reduction in phosphorylation of extracellular signal-regulated kinases 1 and 2 in vitro and in vivo.
data suggest that Spry2 acts as a scaffold to bring more pVHL/associated E3 ligase in proximity of HIF1alpha and increase its ubiquitylation and degradation. This represents a novel action for Spry2 in modulating biological processes regulated by HIFalpha subunits.
MiR-122 could act as a tumor promoter and potentially target Sprouty2. MiR-122 promotes renal cell carcinoma cell proliferation, migration, and invasion.
miR27b promotes the migration and invasion of gastric cancer cells via inhibition of SPRY2mediated ERK signaling.
This gene encodes a protein belonging to the sprouty family. The encoded protein contains a carboxyl-terminal cysteine-rich domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to fibroblast growth factor two. This protein is indirectly involved in the non-cell autonomous inhibitory effect on fibroblast growth factor two signaling. The protein interacts with Cas-Br-M (murine) ectropic retroviral transforming sequence, and can function as a bimodal regulator of epidermal growth factor receptor/mitogen-activated protein kinase signaling. This protein may play a role in alveoli branching during lung development as shown by a similar mouse protein.
protein sprouty homolog 2
, sprouty 2