Endoteliinipeptidit

Endoteliinipeptidit, also known as endothelin peptides, are a group of potent vasoconstrictive peptides that are produced by endothelial cells. These peptides play a crucial role in various physiological processes, including blood pressure regulation, vascular tone, and vascular permeability. The most well-known endotheliinipeptidit are endothelin-1 (ET-1), endothelin-2 (ET-2), and endothelin-3 (ET-3), which are derived from a common precursor protein, big endothelin.

ET-1 is the most potent and biologically active of the endothelin peptides, with a half-life of only a few seconds in the circulation. It is synthesized as a 21-amino acid precursor, big endothelin, which is then cleaved by endothelin-converting enzyme (ECE) to form ET-1. ET-1 binds to specific G-protein-coupled receptors, ET(A) and ET(B), which are expressed on various cell types, including vascular smooth muscle cells, platelets, and endothelial cells.

The endotheliinipeptidit have been implicated in several pathological conditions, such as hypertension, heart failure, and atherosclerosis. They also play a role in the development of pulmonary hypertension and certain types of cancer. The endotheliinipeptidit system is a target for various therapeutic interventions, including the development of endothelin receptor antagonists and endothelin-converting enzyme inhibitors. However, the use of these therapies is limited by their potential side effects and the complexity of the endothelin system. Further research is needed to fully understand the role of endotheliinipeptidit in health and disease and to develop more selective and effective therapies.