Transforming growth factor‐β1 in a sterilized tissue derived from the pig small intestine submucosa

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Abstract
The extracellular matrices of connective tissues contain growth factors such as transforming growth factor (TGF)-β1. The possibility arises, therefore, that animal connective tissues that have been excised and rendered acellular in the sterilization, lyophilization, and other preparative processes for human use may still retain active growth factors that could contribute to the clinical efficacy of the product. We therefore analyzed 4M guanidine HCl extracts of a sterilized, acellular matrix, Oasis® Wound Matrix, for the presence of TGF-β1 by a sandwich enzyme-linked immunosorbent assay using the soluble type II receptor for TGF-β to capture the growth factor, and for biological activity by testing the capacity of the extracts to inhibit 3[H]thymidine incorporation into Mv1Lu cells (mink lung epithelial cells). The enzyme-linked immunosorbent assay determined that TGF-β1 was present at a concentration of 710.9 ± 157.7 pg/g dry weight of tissue in Oasis® and 768.1 ± 182.1 pg/g dry weight of tissue in SIS (porcine small intestinal submucosa), the disinfected precursor of Oasis®. The growth inhibition assays demonstrated that the Oasis® extracts inhibited the proliferation of Mv1Lu cells in culture, consistent with the TGF-β1 in the material having biological activity. Most of the TGF-β1 survives the sterilization and lyophilization processes in the preparation of the Oasis® Wound Matrix, and is functional in its ability to bind to its receptor and, apparently, in its capacity to inhibit growth. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 637–640, 2003