Regulation
Post-translational modifications include tyrosine phosphorylation, which is carried out by protein tyrosine kinases (PTKs). Five members of the Tec kinases subfamily of non-receptor PTKs were first identified in the hematopoietic system: Tec, Btk, Itk/Emt/Tsk, Etk/Bmx, and Txk/Rlk. As modern research has advanced, it has been discovered that some members of the Tec family of kinases are expressed outside the hematological system and are involved in the onset and development of a number of disorders. More research is being done on the involvement of Tec family kinases in cardiovascular disease. Ischemic heart disease, atherosclerosis, sepsis-associated cardiac dysfunction, atrial fibrillation, myocardial hypertrophy, coronary atherosclerotic heart disease, myocardial infarction, and post-myocardial necrosis are all caused by and progressed by tec kinases.
The function of Tec kinases in the cardiovascular system hasn’t, however, been thoroughly explained in any reviews. Consequently, this review highlights research on the function of Tec kinases in cardiovascular disease, offering fresh perspectives on its prevention and treatment.
Difference between RTK and NRTK
|
RTK |
NRTK |
|---|---|
| The transmembrane domain is typically present in the receptor kinase protein. | The non-receptor tyrosine kinase, however, is transmembrane domain-deficient. |
| Have growth factors | Inhibition of cell growth |
| Mediates the movement of the phosphate group to tyrosine residues of the target protein. | Non-receptor TKs are intracellular cytoplasmic proteins that relay intracellular signals. |
| RTKs are a group of 90 families. | It is a group of 9 subfamilies. |
Non-Receptor Tyrosine Kinase Signaling
Non-receptor tyrosine kinases (NRTKs), which can activate intracellular signals generated from external receptors, are a subset of tyrosine kinases, intracellular cytoplasmic proteins, or tethered to the cell membrane. Based mostly on similarities in the kinase domain sequences, they can be divided into nine subfamilies. These are the kinases from the ABL, FES, JAK, ACK, SYK, TEC, FAK, SRC, and CSK families.
NRTKs, which have a great deal of structural variety, don’t have receptor-like characteristics such as an extracellular ligand-binding domain or a transmembrane-spanning domain. They are made up of a large cytoplasmic C-terminal region and an N-terminal section of a common kinase domain that spans around 300 residues. Additionally, they frequently contain a number of extra SH2, SH3, and PH domains, which are signaling or protein-protein interaction domains. The protein substrate’s tyrosine sequence interacts with the residues of the C terminal domain by the binding of the ATP molecule between the two domains.
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