Comparative proteomic analysis of regenerative acellular matrices: The effects of tissue source and processing method

Abstract

AbstractAcellular tissue matrices are used in regenerative medicine from weak tissue re‐enforcement to cosmetic augmentation. However, proteomic signatures leading to different clinical outcomes among matrices are not well understood. In an attempt to investigate the effects of tissue source and processing method, we examined by liquid chromatography tandem mass spectrometry (LC–MS/MS) the proteomic profiles of 12 regulatory agency‐approved acellular matrices (AlloMax, AlloDerm, CollaMend, Heal‐All, JayyaLife, ReGen, Renov, Strattice, SurgiMend, Surgisis, UniTrump and Vidasis). The compositions of acellular matrices varied greatly with the number of identified proteins ranging from 7 to 106. The content of individual proteins was between 0.0001% and 95.8% according to their abundances measured by the M/Z signal intensities. Most acellular matrices still contained numerous cellular proteins. AlloMax, AlloDerm, ReGen, Strattice, SurgiMend and Surgisis retained necessary structural and functional proteins to form the extracellular protein–protein interaction networks for cell adhesion, proliferation and tissue regeneration, whereas CollaMend, Heal‐All, JayyaLife, Renov, UniTrump and Vidasis had only retained certain structural collagens. Principal component analysis showed that proteomic variations among acellular matrices were largely attributed to tissue source and processing method. Differences in proteomic profiles among acellular matrices offers insights into molecular interpretation for different clinical outcomes, and can serve as useful references for rational design of regenerative bio‐scaffolds.