Proteomics Approach to Identify Serum Glycoproteins as Biomarkers in Human Lung Adenocarcinoma
Date Issued
2007
Date
2007
Author(s)
Yao, Jheng-Liang
DOI
zh-TW
Abstract
Lung cancer is the most common cancer in the world and has the highly lethal ratio from cancer. The survival rates of 5-year patient are very low at about 8-14%. The low survival rate is caused by that disease diagnosis is usually late, and prognosis is poor. To diagnose effectively in the early stage of cancer formation is important for increasing survival rate. Detection in the early stage of lung cancer is critical for successful clinical therapy.
Presently, many reports discuss the glycosylation changes in several cancer cases such as liver cancer, lung cancer, ovarian cancer etc. The differences are including fucosylation, sialylation, and high branches formation. They approach the subject matter from gene level to discuss the glycosyltransferase expression, and from the glycan and protein level to discuss the glycoform difference.
The aim of our study is to setup methods and attempts to identify serum biomarker of lung cancer. According to several reports, they did not discuss that the difference in glycoprotein resulted from protein level or glycan level. In the experiment, we combine the application of lectin and the method of proteomics for researching in serum biomarker of glycoprotein. Even if the difference is in protein level, it also has the potential to be a biomarker for cancer diagnosis. If the difference is in glycan level, we can discuss the different site and the effect in physiology.
First, we use several kinds of letin to screen serum. There are some differences in the result of Con A lectin staining. The affinity column of Con A was used to separate the protein which can be bound by Con A. Then the bound protein was separated by 2-D electrophoresis or direct identified by mass.
In the result, we find that several identified proteins were in immune response and were reported before in other cancer like liver cancer or gastric cancer. It is needed to discuss that the possibility of smoking and some factors inducing lung inflammation lead to lung cancer. We use Con A in the experiment. Because Con A can bind almost all proteins with N-glycosylation, the differences of identified proteins were in protein level. If we use other kinds of lectin, we can identify protein differences in glycan level. In the other side, we find the difference in the fragments of complement C3. It is needed to discuss what causes the result, cancer or not.
Subjects
肺腺癌
醣蛋白
生物標記
蛋白質體學
補體C3
lung adenocarcinoma
glycoprotein
biomarker
proteomics
complement C3
SDGs
Type
other
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