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Acellular 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. [ABSTRACT FROM AUTHOR]

Regenerative bio‐scaffolds, widely used for clinical tissue reconstruction and tissue repairs, are functionally diversified and structurally complex decellularized tissue materials (e.g., extracellular matrix, ECM). ECM is naturally cross‐linked and can be further selectively cross‐linked upon processing. Identification, quantification and bioinformatics functional comparison of all ECM proteins are challenging for regenerative bio‐scaffolds. In this study, we have applied proteomic profiling with a two‐step sequential trypsinization method, and identified and quantified 300–400 constituent proteins in three commercially available regenerative bio‐scaffolds (BioDesign Surgisis, ReGen tissue matrix, and ThormalGEN mesh). These proteins were classified into four categories and 14 subcategories based on their mainly biological function. The main components of regenerative bio‐scaffolds were highly abundant ECM structural proteins, and the minor parts of bio‐scaffolds were lowly abundant, less cross‐linked, functionally more diversified proteins, especially extracellular fluid proteins that were easily solubilized by trypsin. The comparative analysis has revealed large differences in the number, type, abundance and function of identified proteins, as well as the extent of decellularization and cross‐linking among regenerative bio‐scaffolds. So, the proteomic profiling with a two‐step sequential trypsinization method could not only provide the molecular basis to better understand the degradation process of regenerative bio‐scaffolds in vivo and different clinical outcomes among various regenerative bio‐scaffolds, facilitate the exploration of the response mechanisms in the host's early clinical stages of ECM‐induced tissue regeneration that is still poorly understood, but also can be used for optimization of the decellularization and cross‐linking process, product characterization and rational design of new ECM products. [ABSTRACT FROM AUTHOR]