secreTRAP: a system for monitoring and quantifying protein secretion from single cells

Summary

Current research methods for measuring protein release rely on quantifying bulk levels in serum and lack the ability to determine temporal and cell-specific release patterns. Oregon Health & Science University researchers have developed a novel technique to allow for visualization and quantification of protein and peptide release in real-time for in vitro and ex vivo applications.   

Technology Overview

Accurately measuring protein or peptide release can be difficult due to pulsatile release patterns and low concentrations in serum and cerebral spinal fluid. The laboratory of Carsten Schultz Ph.D. has developed a novel technique to measure protein and peptide release in real-time, increasing the ability to study the regulation of secretory events.

Features of this method include:

• A dimerization-based system to trap secreted proteins or peptides to the external cell membrane;
• Simple fluorescence read-out of secretion using standard laboratory equipment;
• An optogenetic switch to quickly reset the optical signal to baseline, allowing for multiple experiments in the same preparation;
• Broad applicability for any protein or neuropeptide of interest; and
• Demonstrated proof-of-concept studies measuring insulin, glucagon and kisspeptin release in vitro, including dose-responsiveness and confirmation of released hormone activity via calcium imaging.

This technique could allow for the quantification of stimuli-evoked protein and peptide secretion at a single-cell level with real-time temporal resolution, and could potentially be adapted in future applications to detect hormone secretion in awake freely-moving animals.

Licensing Opportunity

Available for licensing and co-development.