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Separation and Identification of HSP27 Interacting Proteins from Human Hepatocellular Carcinoma Cells

Author: SunXueFeng
Tutor: HeSong
School: Chongqing Medical University
Course: Internal Medicine
Keywords: Heat shock protein 27 Hepatic carcinoma Co-immunoprecipitation Liquid chromatography - electrospray ionization ion trap Western blot Interacting protein
CLC: R735.7
Type: Master's thesis
Year: 2009
Downloads: 74
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Abstract


Purpose of liver cancer is one of the most common malignancy in the world, is not sensitive to chemotherapy and radiotherapy, the surgery cure rate of only 15%, the easy early metastasis and postoperative recurrence and metastasis. Metastasis and the tumor is the most important one of the malignant phenotype, is more than a molecule involved in highly complex and orderly process. The study found that over-expression of heat shock proteins in a wide range of human cancer and involved in tumor cell proliferation, differentiation, invasion and metastasis, death, and immune system recognizes. Heat shock protein 27 (HSP27) as an important one in the small heat shock protein subfamily, in recent years the relationship between the tumor increasingly valued by cell proliferation, differentiation and apoptosis, signal transduction regulation involved in some tumorigenesis and invasion and metastasis process, the specific mechanism is still not very clear, but more and more evidence to suggest that apoptosis and metastasis correlation. The experimental binding protein HSP27 and HSP27-interacting protein in HCC screened, provided the experimental basis and foundation for further exploration of the tumor and its metastasis gene therapy. Method 1. DMEM medium (containing 10% fetal calf serum) to develop hepatocellular carcinoma HepG2 .2215 cells. 2.M-PER protein lysates collected HepG2 .2215 total cellular protein. 3 by co-immunoprecipitation of total cellular protein from HepG2 .2215 corresponding HSP27-binding protein, directly digested liquid chromatography - electrospray ionization tandem mass spectrometry (LC-ESI-ITMS/MS), the corresponding peptide sequence tags (peptide sequence tags, PST). 4 Co-immunoprecipitation and Western blot analysis identified HSP27 one of the interacting proteins HSP90 verify. Results by searching the database in a hepatoma cell line for the first time identified seven HSP27-binding protein, heat shock protein 90 (HSP90), heat shock protein 70 (HSP70), specific downregulation of glucose-regulated protein 78 (GRP-78), lysyl hydroxylase (lysyl hydroxylase), cytokeratin (Keratin, of type I cytoskeletal 9), cytokeratin 10 (Keratin, type I cytoskeletal 10) and cytokeratin (Keratin, type Ⅱ cytoskeletal 1). The identification of seven-binding proteins can be divided into three role areas: molecular chaperones, cytoskeletal organization, and metabolic enzymes. Conclusion HSP27 in HCC tissues involved in the regulation of the related proteins, peptides or small molecule protein interactions involved in the regulation of tumor development.

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CLC: > Medicine, health > Oncology > Gastrointestinal Cancer > Liver tumors
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