Characterizing the inherent activity of urinary bladder matrix for adhesion, migration, and activation of fibroblasts as compared with collagen-based synthetic scaffold

J Biomater Appl. 2023 Mar;37(8):1446-1457. doi: 10.1177/08853282221130883. Epub 2022 Sep 29.

Abstract

The mechanism of action underlying the intriguing prominent bioactivity of urinary bladder matrix (UBM) for in situ tissue regeneration of soft tissue defects remains to be elucidated. It is speculated that the activity of UBM for cell adhesion, migration, and activation is inherent. The bioactivity of UBM for in situ tissue regeneration and its relation with the structure and intact soluble components of UBM were investigated in comparison to a collagen-based scaffold, PELNAC (PEL). We isolated the soluble component of the two materials with urea buffer, and evaluated the respective effect of these soluble components on the in vitro adhesion and migration of L929 fibroblasts. The spatiotemporal pattern of endogenous-cell ingrowth into the scaffolds and cell activation were investigated using a model of murine subcutaneous implantation. UBM is more capable of promoting the adhesion, migration, and proliferation of fibroblasts than PEL in a serum-independent manner. In vivo, as compared with PEL, UBM exhibits significantly enhanced activity for fast endogenous cell ingrowth and produces a more prominent pro-regenerative and pro-remodeling microenvironment by inducing the expression of TGF-β1, VEGF, MMP-9, and murine type I collagen. Overall, our results suggest the prominent bioactivity of UBM for in situ tissue regeneration is inherent.

Keywords: Urinary bladder matrix; cell activation; cell migration; collagen-based scaffold; in-situ tissue regeneration; remodeling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Collagen Type I / metabolism
  • Extracellular Matrix* / metabolism
  • Fibroblasts
  • Mice
  • Tissue Adhesions / metabolism
  • Tissue Scaffolds / chemistry
  • Urinary Bladder* / chemistry

Substances

  • Collagen Type I