title: Fibronectin at select sites binds multiple growth factors and enhances their activity: expansion of the collaborative ECM-GF paradigm.
abstract: Intensive research has demonstrated that extracellular matrix (ECM) molecules and growth factors (GF) collaborate at many different levels. The ability of ECM to modulate GF signals has important implications in tissue formation and homeostasis as well as novel therapies for acute and chronic wounds. Recently, a number of GF-binding sites was identified in fibronectin (FN) and was shown to provide another layer of regulation on GF signaling. Here, we review these new findings on FN interaction with GF in the context of general ways ECM molecules regulate GF signaling.
authors: Department of Biochemistry, Stony Brook University, Stony Brook, New York, USA.
authors: Jia
authors: J
authors: Zhu
authors: Department of Biomedical Engineering, Stony Brook University, Stony Brook, New York, USA; Department of Dermatology, Stony Brook University, Stony Brook, New York, USA; Department of Medicine, Stony Brook University, Stony Brook, New York, USA. Electronic address: richard.clark@stonybrook.edu.
authors: Richard A F
authors: RAF
authors: Clark
mesh_terms: D000818:Animals; D001665:Binding Sites; D005109:Extracellular Matrix / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D005786:Gene Expression Regulation; D006706:Homeostasis; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry; D054730:Protein Interaction Domains and Motifs; D017978:Receptors, Growth Factor / Q000378:metabolism*; D015398:Signal Transduction; D013314:Stress, Mechanical; D023822:Tissue Engineering / Q000379:methods; D014945:Wound Healing
chemical_list: D005353:Fibronectins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D017978:Receptors, Growth Factor