Optimizing the Decellularized Porcine Liver Scaffold Protocol.

There are few existing methods for shortening the decellularization period for a human-sized whole-liver scaffold. Here, we describe a protocol that enables effective decellularization of the liver obtained from pigs weigh 120 ± 4.2 kg within 72 h. Porcine livers (approx. 1.5 kg) were decellularized for 3 days using a combination of chemical and enzymatic decellularization agents. After trypsin, sodium deoxycholate, and Triton X-100 perfusion, the porcine livers were completely translucent. Our protocol was efficient to promote cell removal, the preservation of extracellular matrix (ECM) components, and vascular tree integrity. In conclusion, our protocol is efficient to promote human-sized whole-liver scaffold decellularization and thus useful to generate bioengineered livers to overcome the shortage of organs.

A VANADIUM BROMOPEROXIDASE CATALYZES THE FORMATION OF HIGH-MOLECULAR-WEIGHT COMPLEXES BETWEEN BROWN ALGAL PHENOLIC SUBSTANCES AND ALGINATES(1).

The interaction between phenolic substances (PS) and alginates (ALG) has been suggested to play a role in the structure of the cell walls of brown seaweeds. However, no clear evidence for this interaction was reported. Vanadium bromoperoxidase (VBPO) has been proposed as a possible catalyst for the binding of PS to ALG. In this work, we studied the interaction between PS and ALG from brown algae using size exclusion chromatography (SEC) and optical tweezers microscopy. The analysis by SEC revealed that ALG forms a high-molecular-weight complex with PS. To study the formation of this molecular complex, we investigated the in vitro interaction of purified ALG from Fucus vesiculosus L. with purified PS from Padina gymnospora (Kütz.) Sond., in the presence or absence of VBPO. The interaction between PS and ALG only occurred when VBPO was added, indicating that the enzyme is essential for the binding process. The interaction of these molecules led to a reduction in ALG viscosity. We propose that VBPO promotes the binding of PS molecules to the ALG uronic acids residues, and we also suggest that PS are components of the brown algal cell walls.