The Expression Of SHP2 Between Normal Tissues And Cancer Samples

In the quantities of regulation mechanisms of cell signal transduction, the phosphorylation and dephosphorylation of proteins are of importance. Especially, phosphorylation of specific cellular proteins on tyrosyl residues is one of the most fundamental regulatory mechanisms in signal transduction that dictates cell-cell communication, cell growth and proliferation, regulation of cell cycle and differentiation, tumorogenesis and tumor metastasis, nero tranmission, angiogenesis, embryogeny, and kinds of hereditary and non-hereditary diseases. The research of protein tyrosine phophorylation has been hot spot in the field of biological science.SHP-2,a number of the PTPs family,has one domain with the function of catalysis,containing two SH2 domains at the N-terminal.It is widely express in cytoplasm with no catalysis,when combining with its substrate on membrane ,it could be stimulated. Though, the mechanism of SHP-2 action remains controversial and the critical downstream targets are largely unclear , there is no doubt that SHP-2 can influence FAK activity, celladhesion and motility.Several studies point to SHP-2being either a positive or a negative regulator of celladhesion and motility.Meanwhile,there are also some studies implicate that SHP-2 plays a positive role in insulinsignalling,and attributs to leukemia and cancer.Mutation of SHP-2 causes Noonan syndrome.For researching the expression of SHP-2 in cancer tissue,we extract total RNA from cancer and normal tissues by useing Trizol,and transcribe mRNA to cDNA,then amplify SHP-2 by Nested PCR.We divide the samples into different group accoding to their position,and detect the products by electrophoresis ,and sequencing the products.But we find no conspicuous difference between cancer and normal tissue ,but pseudo gene.