Presionin

Presionin is a hypothetical signaling peptide proposed in educational and theoretical discussions of cellular mechanotransduction. In these discussions, presionin functions as a paracrine or autocrine ligand that mediates cellular responses to mechanical pressure. The term is not widely used in peer-reviewed literature as a defined endogenous molecule; rather, it serves as a placeholder to illustrate how pressure signals might be transduced at the cellular level.

Origin of the name reflects its association with presión, the Spanish word for pressure. In typical hypothetical descriptions, presionin is a small peptide, around 6–12 amino acids, with no fixed sequence. Its activity is presumed to be regulated by mechanical stimulus and proteolytic processing of a larger precursor, yielding an active form.

Mechanistically, presionin is imagined to bind a putative presionin receptor (PRR) on mechanosensitive cells. Receptor engagement would trigger intracellular signaling cascades, such as calcium release and MAP kinase activation, and modulate ion channels to alter cellular excitability or contractility. These effects could influence gene expression and tissue remodeling under sustained load.

Use in teaching: presionin helps illustrate how a diffusible ligand might couple external pressure to intracellular responses. In research, analogous concepts are explored with real signaling peptides and with engineered synthetic systems; presionin itself has no established therapeutic or diagnostic use. Further reading should rely on peer-reviewed discussions of mechanotransduction and mechanosensitive signaling pathways.

See also: Mechanotransduction; Mechanosensitive channels; G protein-coupled receptors.