Phosphorylation status of ROCKII molecules after PI3Kδ suppression in glioblastoma multiforme cell line

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Phosphorylation status of ROCKII molecules after PI3Kδ suppression in glioblastoma multiforme cell line

 

Author: Tong, Yu Leong
Title: Phosphorylation status of ROCKII molecules after PI3Kδ suppression in glioblastoma multiforme cell line
Degree: M.Sc.
Year: 2015
Subject: Glioblastoma multiforme.
Phosphoinositides.
Protein kinases.
Hong Kong Polytechnic University -- Dissertations
Department: Dept. of Health Technology and Informatics
Pages: ix, 89 leaves : illustrations ; 30 cm
Language: English
InnoPac Record: http://library.polyu.edu.hk/record=b2778329
URI: http://theses.lib.polyu.edu.hk/handle/200/7837
Abstract: Glioblastoma multiforme (GBM) is a Grade IV tumor which is the most malignant type tumor according to WHO guidelines. The prognosis of GBM is very poor with frequent recurrence after surgery. Treatment for GBM is effective in extending patients' life. The poor prognosis of GBM is mainly due to its high invasion rate to nearby brain tissue which made total removal of tumor cells impossible. A previous study showed that PI3Kδ, a signaling molecule, is upregulated in glioma cell lines and its suppression by si-RNA treatment leads to decrease in glioma cell invasion. The result indicated that PI3Kδ plays an important role in the malignancy of glioma cell. Proteomic analysis revealed the phosphorylation changes in a group of signaling molecules after PI3Kδ suppression in the glioma cell line (U-87MG). Results showed that phosphorylation of ROCKII, a downstream signaling molecule involved in cell movement, at S1136 site was 2 fold increased after PI3Kδ suppression. The aim of this project is to verify the proteomic result in terms of phosphorylation change in ROCKII after PI3Kδ suppression by western blotting and, thus, identify the relationship between PI3Kδ and ROCKII in order to know more on the high invasion mechanism of GBM cell. Results showed that phosphorylation of ROCKII on T249 site was decreased in PI3Kδ suppressed glioma cell which contradicted to the status of S1136 phosphorylation from proteomic study. Therefore, further study by investigating ROCKII activity after PI3Kδ suppression as well as identification of the role of T249 phosphorylation on ROCKII can be carried out for better understanding the relationship of PI3Kδ and ROCKII.

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