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Diagnosis of brain cancer using proteomic approaches

Brain cancer (also known as malignant brain tumor, in medical definitions), is the most threatening cancer among all cancers in humans. By using various proteomic approaches, we can easily detect and analyze the effect of specific genetic events involved in the progression of malignant brain cancer.

In proteomics, we generally study proteomes. A proteome can be called the protein complement of a genome.

Malignant brain tumors are generally classified into four grades, based on their complexity or their physical appearance under a microscope.

Grade 1, a term generally used when brain cells show their physical appearance similar to normal cells. It’s just like benign tissue or cells.

In grade 2, more malignant cells begin to proliferate. At grade 3, they are likely to grow rapidly and begin to invade almost localized normal cells. This situation is called anaplastic, in medical terminology.

In grade 4 (generally referred to as most abnormal cells), cancer cells can break away from tumors and begin to spread, possibly to other parts of the brain or to the spinal cord.

Brain cancer cells generally have a wide range of abnormal proteins. They express the altered genetic potential of a cancer cell. These are the relevant examples of genetically modified proteins, as well as proteins regulated after their synthesis.

Interpretation of gene level modification in various types of brain cancers, ie, brain stem glioma, ependymoma, astrocytoma, medulloblastoma, oligodendroglioma, meningioma, can be easily performed using various proteomics tools. These different techniques basically act on the modification property of that abnormal cancer protein, that is, extracted from a particular malignant tumor cell.

These modifications are abundant in the post-translational mechanism, such as the cleavage of the proenzyme and the precursor part of abnormal proteins; phosphorylation activities interfere with biophysical appearance and signaling; hydroxylation changes in the atmosphere of H bonds; glycosylation involves molecular recognitions (or cell-cell recognition) and acetylation alters the binding affinity for DNA.

High-throughput proteomics tests or tools are available to circumvent some of the above caveats. For example, advanced proteomics tools and techniques, i.e., two-dimensional gel electrophoresis (2D PAGE), matrix-assisted laser desorption/ionization (MALDI), mass spectroscopy (MS), enzymes (ELISA), can adequately address the complexities of the proteome arise because most proteins appear to be modified.

New bioengineered proteomic approaches have enabled the analysis of several brain cancer biomarkers. A thorough interpretation of the relevance of each brain cancer biomarker will be very helpful in detecting the variant level or context of that particular malignant cell.

Research on cancer biomarkers will explore new ways to obtain options related to various therapeutic alternatives. Eventually, it will represent new biologic approaches in the next era of clinical research or rapid detection of brain cancer.

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