PMID: 27438154 RLIMS-P 5 eFIP 0 miRTex 0 eGARD 0 Issue Report
Title
| 1. | Phosphorylation of kinase insert domain receptor by cyclin-dependent kinase 5 at serine 229 is associated with invasive behavior and poor prognosis in prolactin pituitary adenomas. |
Abstract
| 2. | Pituitary adenomas constitute 15-20% of intracranial neoplasms. |
| 3. | Previously we reported that cyclin-dependent kinase 5 (CDK5) is upregulated in pituitary tumors associated with activating protein p35, and plays an essential role in pituitary adenomas progression. |
| 4. | Here we explored the mechanisms of CDK5 signaling in prolactin pituitary adenomas. |
| 5. | Our data indicate that p35 expression and CDK5 activity are both significantly increased in human invasive prolactin pituitary adenomas as compared to noninvasive forms of pituitary adenomas. |
| 6. | Inhibition of CDK5 activity suppressed cell migration and invasive ability in GH3 rat pituitary cells. |
| 7. | We identified that CDK5 phosphorylates serine 229 residue (Ser-229) of kinase insert domain receptor (KDR), also known as VEGFR-2, in prolactin pituitary adenomas. |
| 8. | Phosphorylation of Ser-229 is required for proper KDR surface localization. |
| 9. | Phosphorylated Ser-229 in KDR (pSer-229) levels are significantly higher in noninvasive and invasive prolactin pituitary adenomas compared to normal pituitary tissues. |
| 10. | In addition, our data indicated that higher KDR pSer-229 correlates with worse prognosis in patients with prolactin pituitary adenomas. |
| 11. | In summary, our results illustrated that CDK5-mediated KDR phosphorylation controls prolactin pituitary adenoma progression and KDR pSer-229 serves as a potential prognostic biomarker for both noninvasive and invasive pituitary adenomas. |
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