title: Normal wound healing in mice deficient for fibulin-5, an elastin binding protein essential for dermal elastic fiber assembly.
abstract: Extracellular matrix proteins play a critical role in dermal wound healing by mediating matrix-cell interactions and re-establishing the dermal architecture and environment. Fibulin-5 is an elastin-binding protein essential for elastic fiber development in vivo, and it has recently been shown to inhibit angiogenesis in vitro. Here, we use mice deficient for the fibulin-5 gene (fbln5) to examine the role of fibulin-5 and the effect of the loss of elastic fibers in dermal wound healing. Fbln5 is upregulated in the granulation tissue 14 days after full-thickness wounding in wild-type mice, before the formation of elastic fibers. Although wounded fbln5(-/-) skin showed enhanced neovascularization compared to the wild-type skin, no difference in the rate of wound closure was observed between mutant and wild-type mice. In addition, a breaking strength test revealed that there was no difference in breaking stress or strain between wild-type and fbln5(-/-) wounded skin. These results suggest that fibulin-5 and elastic fibers are not directly involved in short-term wound healing. Clearly, the long-term effect of the absence of fibulin-5 on the function and integrity of regenerated skin needs to be further addressed.
authors.affiliation: Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148, USA.
authors.forename: Qian
authors.initials: Q
authors.lastname: Zheng
authors.forename: Jiwon
authors.initials: J
authors.lastname: Choi
authors.forename: Leonie
authors.initials: L
authors.lastname: Rouleau
authors.forename: Richard L
authors.initials: RL
authors.lastname: Leask
authors.forename: James A
authors.initials: JA
authors.lastname: Richardson
authors.forename: Elaine C
authors.initials: EC
authors.lastname: Davis
authors.forename: Hiromi
authors.initials: H
authors.lastname: Yanagisawa
mesh_terms: D000818:Animals; D002465:Cell Movement; D049109:Cell Proliferation; D002478:Cells, Cultured; D020405:Dermis / Q000473:pathology / Q000503:physiopathology; D004547:Elastic Tissue / Q000503:physiopathology*; D016326:Extracellular Matrix Proteins / Q000172:deficiency* / Q000378:metabolism; D051379:Mice; D018345:Mice, Knockout; D018919:Neovascularization, Physiologic; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012867:Skin / Q000098:blood supply / Q000293:injuries* / Q000503:physiopathology*; D013718:Tensile Strength; D013997:Time Factors; D015854:Up-Regulation; D014945:Wound Healing; D014950:Wounds, Penetrating / Q000503:physiopathology
chemical_list: D016326:Extracellular Matrix Proteins; C120769:Fbln5 protein, mouse; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; C054901:elastin-binding proteins