Signal Transduction
Application of Enzyme-Linked Immunosorbent Assay (ELISA) in Signal Transduction Research
Signal transduction is a process in which extracellular factors bind to receptors to trigger a series of intracellular biochemical reactions and protein interactions, followed by the expression of genes required for cell physiological responses and the formation of various biological effects. Through the interaction of signal proteins between cells, various signaling pathways form a highly ordered and complex regulatory network in the body. In the human body, signal transduction pathways are usually composed of specific cells that secrete and release information substances, information substances, and target cells. Intercellular information substances, namely the first messenger, can be divided into neurotransmitters, endocrine hormones, and local chemical mediators and so on. The information substance in the cell, that is, the second messenger, can be divided into Ca2+, cAMP, cGMP and so on. Failure of signal transduction pathways may cause disease and even cancer. To study the important role of each link in the signal transduction pathway, and to detect diseases caused by signal transduction failure, ELISA as an efficient immunoassay technology is widely used in signal transduction research.
Common Targets in Signal Transduction Research
- Adropin
- Aggrecan
- Beta Actin
- Bridging Integrator 1
- Calcyclin Binding Protein
- Calnexin
- Calreticulin
- Desmoglein 2
- Diablo Homolog
- Eomesodermin
- Fibrillin 1
- Focal Adhesion Kinase
- Glucuronidase Beta
- Heat Shock Protein 27
- Luteinizing Hormone
Advantages of ELISA in Signal Transduction Research
- Help to study all aspects of the signal transduction pathway
- Help detect malfunctions in signal transduction pathways
- Help to study the relationship between information substances and diseases
Common Targets Detected by ELISA in Signal Transduction Research
Heat Shock Protein
Heat Shock Proteins (HSPs) refer to a group of proteins produced by cells under the induction of stressors, especially environmental high temperatures. HSPs are divided into five categories, namely HSP110, HSP90, HSP70, HSP60 and small Heat Shock Proteins. HSP is a protective protein that can improve the stress ability of cells, especially heat resistance. HSP also breaks down damaged proteins and helps cells achieve normal physiological functions. And HSP also participates in the innate immune response.
Histone
Histone refers to the general term for basic proteins that bind to DNA in the nucleus of all eukaryotes. Histone plays a role in gene regulation, and its genes are very conservative. Histones can be modified by several types such as methylation, acetylation and phosphorylation. The correlation between histone modification and chromatin structure changes and gene activity control is a hot research topic. Studies have found that abnormal histone methylation is associated with many human diseases such as tumor.
Actin
Actin is a kind of globular multifunctional protein that forms microfilaments, which is basically present in all eukaryotic cells. It interacts with a large number of other proteins and is highly conserved during evolution. Actin is a kind of muscle structural protein and plays an important role in muscle movement. It is present in the filaments of striated muscle myofibrils and also in smooth muscle. Actin filaments are connected to α-actin and the membrane through vinculin.
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References
- Zininga, T.; et al. Heat Shock Proteins as Immunomodulants. Molecules. 2018, 23(11): 2846.
- Strahl, B.D.; Allis C.D. The language of covalent histone modifications. Nature. 2000, 403(6765): 41-45.
- Pollard, T.D. Actin and Actin-Binding Proteins. Cold Spring Harb Perspect Biol. 2016, 8(8): a018226.
