Background[1-3]
Phosphorylated epidermal growth factor receptor antibody is a type of polyclonal antibody that can specifically bind to phosphorylated epidermal growth factor receptor. It is mainly used to detect phosphorylated epidermal growth factor receptor in Western Blot, IHC-P, and IF. , ELISA, Co-IP and other immunological experiments.
EGFR (Epidermal Growth Factor Receptor) is a receptor for epithelial growth factor (EGF) cell proliferation and signaling. EGFR belongs to the ErbB receptor family, which includes EGFR (ErbB-1), HER2/c-neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4). EGFR is also known as HER1 and ErbB1, and mutations or overexpression generally cause tumors. EGFR is a glycoprotein, a tyrosine kinase receptor, with a cell membrane penetration and a molecular weight of 170KDa. EGFR is located on the surface of the cell membrane and is activated by binding to ligands, including EGF and TGFα (transforming growth factorα). Upon activation, EGFR converts from a monomer to a dimer, although there is evidence that dimers also exist before activation. EGFR may also be activated by polymerizing with other members of the ErbB receptor family, such as ErbB2/Her2/neu.
EGFR can activate its intracellular kinase pathway after dimerization, including activation sites such as Y992, Y1045, Y1068, Y1148 and Y1173. This autophosphorylation can guide downstream phosphorylation, including MAPK, Akt and JNK pathways, inducing cell proliferation. Receptor activation is important for immunity in the skin.
After the ligand binds to the epidermal growth factor receptor (EGFR), the receptor undergoes dimerization. Dimerization includes both the binding of two receptor molecules of the same type (homodimerization) and Involves the binding (heterodimerization) of different members of the human EGF-related receptor (HER) tyrosine kinase family. Dimerization is followed by autophosphorylation of tyrosine residues. These phosphorylated residues serve as binding sites for recruitment of adapter proteins and additional tyrosine kinase substrates. Protein interactions in activated receptor complexes stimulate ras proteins, leading to the onset of a phosphorylation cascade and activation of mitogen-activated protein (MAP) kinase. Alternatively, transcriptional signaling and activation, phosphatidylinositol kinase-3 (PI3K)-Akt, and stress-activated protein kinase (SAPK) signaling pathways will be activated. These signaling pathways in turn trigger gene transcription, while pathways controlling cell proliferation, differentiation, and survival are activated.
Apply[4][5]
For research on the expression of epidermal growth factor receptor and transforming growth factor-α in lung cancer tissues and their clinical significance
Study the expression of epidermal growth factor receptor (EGFR) and transforming growth factor-alpha (TGF-α) in lung cancer tissues, and explore the relationship between EGFR and TGF-α and the occurrence, development and prognosis of lung cancer.
Methods: 36 lung cancer tissue specimens and 12 non-malignant tissue specimens from thoracic surgery and respiratory department fiberoptic bronchoscopy were selected, and the expression of EGFR and TGF-α in lung cancer tissue and non-malignant lung tissue was detected by immunohistochemistry S-P method. expression in.
Results: The tissue specimens were divided into lung cancer group and non-malignant tumor group according to pathological diagnosis. The positive expression rate of EGFR in the Dow reverse osmosis membrane lung cancer group was 55.56%, and the positive expression rate of EGFR in the non-malignant tumor group was 8.33. %, there is a significant difference between the two (P<0.01); the positive expression rate of TGF-α in the lung cancer group is 47.22%, and TGF-α is negatively expressed in the non-malignant tumor group, there is a significant difference between the two (P <0.01).
The expression rates of EGFR and TGF-α in non-small cell carcinoma (EGFR 78.57%; TGF-α 57.14%) were significantly higher than that in small cell undifferentiated carcinoma (P<0.05).
The expression of EGFR and TGF-α has nothing to do with TNM stage (P>0.05); there is no significant difference in the one-year survival rate of lung cancer patients with positive and negative expression of EGFR and TGF-α (P>0.05).
The cases with simultaneous expression of EGFR and TGF-α accounted for 30.56% of the total number of lung cancer patients. The one-year survival rate of lung cancer cases with simultaneous expression of EGFR and TGF-α was 27.27%. EGFR and TGF-α were not expressed simultaneously or were negative. The one-year survival rate of lung cancer cases was 72%, and there was a significant difference between the two (P<0.05).
