Growth factor binding to the pericellular matrix and its importance in tissue engineering

• Published in: Advanced drug delivery reviews Vol. 59; no. 13; pp. 1366 - 1381
• Main Authors: Macri, Lauren, Silverstein, David, Clark, Richard A.F.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 10.11.2007
• Subjects: Animals; Cell-Matrix Junctions - metabolism; Cytokine; Extracellular matrix; Extracellular Matrix Proteins - metabolism; Glycosaminoglycans - pharmacology; Growth factor; Growth factor binding; Humans; Intercellular Signaling Peptides and Proteins - metabolism; Pericellular matrix; Proteoglycans - pharmacology; Tissue Engineering; Pericellular matrix; Extracellular matrix; Growth factor binding; Tissue engineering; Cytokine; Growth factor
• ISSN: 0169-409X; 1872-8294
• DOI: 10.1016/j.addr.2007.08.015

In addition to its typical role as a scaffold, molecular filter, and cell modulator, the pericellular matrix can bind bioactive molecules and serve as a repository, while regulating their activation, synthesis, and degradation. This review focuses on interactions between bioactives, specifically growth factors and cytokines, with various components of the pericellular matrix. For example, biglycan and betaglycan, proteoglycans of the pericellular matrix, and decorin, a proteoglycan of the interstitial extracellular matrix, bind and regulate the activity and availability of transforming growth factor-beta. From evidence presented in this paper, it is obvious that the presence of growth factors in the pericellular matrix is integral to the spatiotemporal coordination of cellular activities to ensure proper tissue/organ formation during wound healing. It is believed by many researchers that the delivery of the right growth factors at the right time is instrumental to the orchestration of tissue regeneration. Thus, the interplay between the pericellular environment and bioactive molecules provides an underutilized knowledge base in the design and creation of tissue engineered constructs.