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Although the expression of SPRY1 was low when compared with other tumors, SPRY1 was variably expressed in primary Ewing sarcoma tumors and higher expression levels were significantly associated with improved outcome in a large patient cohort.
SPRY1 and SPRY2 (show SPRY2 Proteins) mRNA transcripts were significantly upregulated in human CRC (show CALR Proteins). Suppression of SPRY2 (show SPRY2 Proteins) repressed AKT2 (show AKT2 Proteins) and EMT (show ITK Proteins)-inducing transcription factors and significantly increased E-cadherin (show CDH1 Proteins) expression. Concurrent downregulation of SPRY1 and SPRY2 (show SPRY2 Proteins) also increased E-cadherin (show CDH1 Proteins) and suppressed mesenchymal markers in colon cancer cells.
Spry1 plays a selective role in at least a subset of triple-negative breast cancer to promote the malignant phenotype via enhancing EGF (show EGF Proteins)-mediated mesenchymal phenotype.
Suppression of SPRY1 by age-associated methylation inhibits the replenishment of the muscle stem cell pool.
Cosuppression of Sprouty and Sprouty-related negative regulators of FGF signalling in prostate cancer
There is an inverse correlation between the expression of Spry1 and growth, proliferation, invasion and migration of ovarian cancer cells.
A random population of LNCaP prostate cancer cells comprises a heterogeneous group of cells with different androgen-deprivation sensitivities and potential for invasiveness; expression levels of 2 genes known to be regulated by miR (show MLXIP Proteins)-21, an androgen-regulated microRNA, SPRY1 and JAG1 (show JAG1 Proteins) were lower in an androgen insensitive clone, than an androgen sensitive clone.
The Spry1 acts as a sensor of mitogenic activity that not only attenuates RTK signaling but also induces a cellular senescence response to avoid uncontrolled proliferation.
Spry1 and Spry4 have opposing roles in VSMC phenotypic modulation, and Spry1 maintains the VSMC differentiation phenotype in vitro in part through an Akt/FoxO/myocardin pathway.
Re-expression of SPRY1, a repressed target of BCL11B, limits the transformation capacity of Ewing sarcoma cells.
Here, we present a novel mouse model of pheochromocytoma consisting of double-heterozygous mice for Pten and Sprouty1 (Spry1), which leads to pheochromocytomas that appear at earlier onset and grow at a higher rate than those from Pten+/- mice.
Sprouty gain of function disrupts lens cellular processes and growth by restricting receptor tyrosine kinase (show ERBB3 Proteins) signaling.
In vivo analysis of thyroid glands from Spry1 knockout mice reveals that Spry1 induces a senescence-associated secretory phenotype via activation of the NFkappaB pathway.
showed that hSpry1 overexpression prevents VEGF secretion
Spry1 and Spry2 (show SPRY2 Proteins) coordination is required for normal development of the external genitalia in mice
conjunctival epithelial Spry1 and Spry2 (show SPRY2 Proteins) redundantly promote eyelid closure.
Findings demonstrate that Pokemon (show ZBTB7A Proteins) suppresses Sprouty1 expression through a miR (show MLXIP Proteins)-21-mediated mechanism, affecting the growth and proliferation of liver cancer cells.
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.
When Spry1 and Spry2 loss-of-function occurs in the context of heterozygosity for a null allele of the tumor suppressor gene Pten, there is a striking increase in prostatic intraepithelial neoplasia and evidence of neoplastic invasion.
May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis.
protein sprouty homolog 1
, sprouty, Drosophila, homolog of, 1 (antagonist of FGF signaling)
, sprouty 1 protein
, sprouty homolog 1, antagonist of FGF signaling (Drosophila)
, sprouty homolog 1, antagonist of FGF signaling
, sprouty 1
, sprouty homolog 1a, antagonist of FGF signaling
, sprouty homolog 1b, antagonist of FGF signaling
, inhibitor of receptor tyrosine kinases