Binding to carboxypeptidase M mediates protective effects of fibrinopeptide Bβ

November 01, 2019

Intro

https://doi.org/10.1016/j.trsl.2019.07.008, Translational Research Volume 213, Sörensen-Zender et al.

Abstract

A 28-amino-acid fibrinopeptide (Bb15-42) was studied for kidney protection using human HK-2 tubular cells. The LRC-TriCEPS platform enabled the discovery of carboxypeptidase M (CBPM) as a novel cell surface receptor for Bb15-42, revealing a new protective mechanism independent of endothelial VE-cadherin. This work is important as it identifies CBPM as a therapeutic target for renal injury, illustrating the unique power of LRC-TriCEPS to uncover receptor-ligand interactions directly on living cells.

Author

Inga Sörensen-Zender soerensen.inga@mh-hannover.deRongjun Chen ∙ Song Rong ∙ Sascha David ∙ Anette Melk ∙ Hermann HallerRoland Schmitt from Hannover Medical School