Transport of Biologically Active Ultrashort Peptides Using POT and LAT Carriers.

This review highlights the importance of POT and LAT transporters in the cellular transport of ultrashort peptides, but lacks specific data to support clinical applications.

Summary and findings

This review examines the transport mechanisms of ultrashort peptides (USPs) via POT and LAT carriers in various tissues. It highlights the role of these transporters in regulating biological functions under normal and pathological conditions. No specific quantitative findings or treatment claims are made.

Abstract

Ultrashort peptides (USPs), consisting of 2-7 amino-acid residues, are a group of signaling molecules that regulate gene expression and protein synthesis under normal conditions in various diseases and ageing. USPs serve as a basis for the development of drugs with a targeted mechanism of action. The purpose of this review is to systematize the available data on USP transport involving POT and LAT transporters in various organs and tissues under normal, pathological and ageing conditions. The carriers of the POT family (PEPT1, PEPT2, PHT1, PHT2) transport predominantly di- and tripeptides into the cell. Methods of molecular modeling and physicochemistry have demonstrated the ability of LAT1 to transfer not only amino acids but also some di- and tripeptides into the cell and out of it. LAT1 and 2 are involved in the regulation of the antioxidant, endocrine, immune and nervous systems' functions. Analysis of the above data allows us to conclude that, depending on their structure, di- and tripeptides can be transported into the cells of various tissues by POT and LAT transporters. This mechanism is likely to underlie the tissue specificity of peptides, their geroprotective action and effectiveness in the case of neuroimmunoendocrine system disorders.

Key findings

• Not reported in abstract.

Limitations

• Not reported in abstract.

Elsewhere in the Cartalax (AED peptide) corpus