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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.
that Dyrk1A might promote fibroblast-like synoviocytes proliferation, migration and invasion by suppressing Spry2 expression and activating the ERK MAPK signaling pathway in rheumatoid arthritis
this study identified the association of a genetic polymorphism in the intergenic region of SPRY2 with a decreased incidence of thrombocytopenia after coronary artery bypass grafting surgery
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.
Loss of Spry1/2 enhances the survival of effector CD8+ T cells and results in the formation of more protective memory cells. Deleting Spry1/2 in antigen-specific CD8+ T cells may have therapeutic potential for enhancing the survival and functionality of effector and memory CD8+ T cells in vivo.
These results identify Spry2 as a critical regulator of endochondral bone formation that modulates signaling in both osteoblast and chondrocyte lineages.
Spry2 is a novel unfolded protein response target and its upregulation is dependent on PERK. Knockdown of Spry2 resulted in reduced expression of Serca2, reduced endoplasmic reticulum calcium levels, and induction of the UPR. Spry2 deletion in the adult mouse beta-cell caused hyperglycemia and hypoinsulinemia.
In the present study, it is demonstrated that Spry2 and -4 participate in KA induced neurodegeneration possibly through inhibition of ERK signaling.
Study revealed that suppression of Spry2 expression induced proliferation and differentiation of osteoblastic cells upon bFGF and EGF stimulation, whereas it diminished proliferation of gingival epithelial cells.
Cosuppression of Sprouty and Sprouty-related negative regulators of FGF signalling in prostate cancer
in embryos with lower Spry2;Spry4 gene dosages, we observed a non-fusion of original R2 and M1 Shh signaling domains with consequent formation of a supernumerary tooth primordium from the isolated R2 bud
The data showed enhanced axon outgrowth and improved long-distance axon regeneration in sprouty2 deficient mice
Sprouty2 acts as an inhibitor of CrkL-Rap1 signaling.
we reveal that SPRY2 expression is regulated by FOXO3a and beta-catenin nuclear activity in colon cancer
Spry1 and Spry2 coordination is required for normal development of the external genitalia in mice
We propose that Sprouty genes(Spry2 and Spry4) were implicated during evolution in reduction of the cheek teeth in Muridae, and their deletion can reveal ancestral stages of murine dental evolution.
conjunctival epithelial Spry1 and Spry2 redundantly promote eyelid closure.
Findings indicate that leukemia inhibitory factor (LIF)-induced Stat3 phosphorylation plays an important role in promoting the binding of phospho-Erk1/2 and Sprouty2, and thus inhibiting growth factor (FGF)-induced differentiation.
study thus reveals a novel Spry2 function, which mediates endothelial contact inhibition and barrier integrity
Sprouty2 signaling inhibits Akt activation and branch initiation in the developing mammary epithelium.
Inactivation of Spry2 accelerates AKT-induced hepatocarcinogenesis via activation of Ras/mitogen-activated protein kinase and pyruvate kinase M2 pathways.
ISG15 mRNA expression and IFN-dependent antiviral responses are enhanced in Spry1,2,4 triple knock-out mouse embryonic fibroblasts, consistent with negative feedback regulatory roles for Spry proteins in IFN-mediated 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