垂体瘤是临床最常见的神经系统肿瘤之一，对患者的生长、发育、劳动能力和生育功能等产生严重影响。VEGFR2（KDR）在血管生成和肿瘤形成中起主要作用。我们发现在KDR的229位丝氨酸为细胞周期素依赖激酶5（Cdk5）潜在的特异性磷酸化位点。前期实验表明垂体瘤组织样本中有丰富的磷酸化KDR表达，KDR的Ser229位磷酸化水平在侵袭性垂体瘤、非侵袭性垂体瘤、正常垂体瘤中依次递减，将KDR 229位丝氨酸突变后可能影响受体从高尔基体到细胞膜的膜转运，同时发现该位点的突变降低了垂体瘤细胞的迁移和侵袭能力。这些研究提示该位点磷酸化水平对于受体及受体后信号转导发挥重要作用。本研究主要探讨KDR 229位丝氨酸磷酸化对受体功能及后续信号转导的影响，并将在大规模垂体瘤样本中筛查KDR229位丝氨酸磷酸化水平与垂体瘤分子分类、侵袭、复发与预后的关系，并期望以此为线索探寻垂体瘤的个性化诊疗中有效的分子靶点。

Pituitary adenomas make up a significant number of intracranial tumors. The space-occupying lesions and hormone disorder could have heavy consequences for patients about growth, development, labor ability and fertility function. VEGF receptor 2 (KDR) is critical for the process of angiogenesis a tumor formation. Based on sequence analysis, we identified Ser-229 as the only consensus phosphorylation site for Cyclin dependent kinase 5 (Cdk5). In the Preliminary experiments, we detected abundant phosphorylated KDR protein in pituitary adenomas. pSer-229 KDR expression increased with differentiation from normal pituitary tissue, to noninvasive and to invasive prolactin pituitary adenomas. The expression of functional KDR Ser229A was significantly less than that of WT-DOR on cell surface in pituitary cell lines. This mutation is thought to prevent KDR from moving efficiently through the Golgi apparatus to the cell surface and mutation of KDR at Ser-229 impairs the invasiveness ability of pituitary cell lines. The present study indicates Cdk5 may regulate membrane trafficking of KDR through phosphorylation at Ser-229, but the mechanisms involved still need to be studied intensively. In the present study, through further investigation the effect of phosphorylation of KDR on Ser-229 on the function of receptor and its signal transduction pathway in pituitary adenomas, reveal the regulation mechanisms of phosphorylation of the KDR Ser229 in pituitary adenomas and provide new potential specific biomarkers of molecular diagnosis and molecular therapy of pituitary adenomas.