TY - JOUR
T1 - Normal wound healing in mice deficient for fibulin-5, an elastin binding protein essential for dermal elastic fiber assembly
AU - Zheng, Qian
AU - Choi, Jiwon
AU - Rouleau, Leonie
AU - Leask, Richard L.
AU - Richardson, James A.
AU - Davis, Elaine C.
AU - Yanagisawa, Hiromi
N1 - Funding Information:
We thank members of the Histology Core Lab for excellent histology. We also thank Shelby Chapman for technical assistance and Dr Eric Olson for encouragement. This work was supported in part by the grant from the Skin Research Center at the University of Texas Southwestern Medical Center and SHISEIDO Grants for Science Research. E.C.D. is a Canada Research Chair.
PY - 2006/12
Y1 - 2006/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33751092791&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33751092791&partnerID=8YFLogxK
U2 - 10.1038/sj.jid.5700501
DO - 10.1038/sj.jid.5700501
M3 - Article
C2 - 16902421
AN - SCOPUS:33751092791
SN - 0022-202X
VL - 126
SP - 2707
EP - 2714
JO - Journal of Investigative Dermatology
JF - Journal of Investigative Dermatology
IS - 12
ER -