# Kallikrein 14 activates the chemoattractant protein chemerin in human skin

## TL;DR

This study identifies KLK14 as the enzyme that activates chemerin in human skin, which is important for skin homeostasis.

## Contribution

The study reveals KLK14 as a novel chemerin-processing enzyme in human skin.

## Key findings

- KLK14 activates chemerin by generating the 156F and 158S isoforms.
- Gene-edited keratinocytes confirmed KLK14's role in chemerin processing.
- KLK14 is a rapid and stable activator of chemerin in the skin.

## Abstract

Chemerin is a multifunctional protein that requires limited carboxyl-terminal proteolysis to manifest its chemotactic, antimicrobial, and metabolic activities. The role of chemerin in the maintenance of skin homeostasis has recently been demonstrated. The main enzymes responsible for processing chemerin in the skin, however, remain elusive. Due to their abundance in the skin and epidermis in particular, kallikreins (KLKs) are promising candidates. Here, using recombinant inactive chemerin, several isolated KLKs, and human primary keratinocytes gene-edited to silence KLK14, we demonstrate that KLK14 is a chemerin-processing enzyme in the skin, rapidly and stably activating this chemoattractant by generating the chemerin 156F and 158S isoforms.