endoteliinia

Endoteliinia is a peptide hormone that plays a significant role in various physiological processes, particularly in the regulation of vascular tone, cell growth, and inflammation. It was first identified in the endothelial cells lining the blood vessels, hence the name, which is derived from "endothelium" and the suffix "-in" denoting a peptide.

The hormone is encoded by the EDN1 gene in humans and is synthesized as a precursor molecule called preproendothelin. This precursor undergoes cleavage to form big endothelin, which is then further processed by endothelin-converting enzymes to produce the active form, endothelin-1. There are three known isoforms of endothelin: endothelin-1, endothelin-2, and endothelin-3, each with distinct but overlapping functions.

Endothelin-1 is the most well-studied and is known for its potent vasoconstrictor properties. It exerts its effects by binding to two types of receptors, endothelin receptor type A (ET_A) and endothelin receptor type B (ET_B). Activation of ET_A receptors primarily mediates vasoconstriction, while ET_B receptors can mediate both vasodilation and vasoconstriction, depending on their location and the context.

In addition to its role in vascular tone, endoteliinia is involved in the regulation of cell proliferation, differentiation, and inflammation. It has been implicated in various pathological conditions, including hypertension, heart failure, pulmonary arterial hypertension, and endothelial dysfunction. Research is ongoing to explore the potential therapeutic applications of endothelin receptor antagonists in the treatment of these conditions.