Document Detail


Topical prolyl hydroxylase domain-2 silencing improves diabetic murine wound closure.
MedLine Citation:
PMID:  21627711     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Prolyl hydroxylase domain 2 (PHD2) has been implicated in several pathways of cell signaling, most notably in its regulation of hypoxia-inducible factor (HIF)-1α stability. In normoxia, PHD2 hydroxylates proline residues on HIF-1α, rendering it inactive. However, in hypoxia, PHD2 is inactive, HIF-1α is stabilized and downstream effectors such as vascular endothelial growth factor and fibroblast growth factor-2 are produced to promote angiogenesis. In the present study we utilize RNA interference to PHD2 to promote therapeutic angiogenesis in a diabetic wound model, presumably by the stabilization of HIF-1α. Stented wounds were created on the dorsum of diabetic Lepr db/db mice. Mice were treated with PHD2 small interfering RNA (siRNA) or nonsense siRNA. Wounds were measured photometrically on days 0-28. Wounds were harvested for histology, protein, and RNA analysis. Diabetic wounds treated with siRNA closed within 21±1.2 days; sham-treated closed in 28±1.5 days. By day 7, Western blot revealed near complete suppression of PHD protein and corresponding increased HIF-1α. Angiogenic mediators vascular endothelial growth factor and fibroblast growth factor-2 were elevated, corresponding to increased CD31 staining in the treated groups. siRNA-mediated silencing of PHD2 increases HIF-1α and several mediators of angiogenesis. This corresponded to improved time to closure in diabetic wounds compared with sham-treated wounds. These findings suggest that impaired wound healing in diabetes can be ameliorated with therapeutic angiogenesis.
Authors:
Meredith Wetterau; Finny George; Andrew Weinstein; Phuong D Nguyen; John Paul Tutela; Denis Knobel; Oriana Cohen Ba; Stephen M Warren; Pierre B Saadeh
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-05-31
Journal Detail:
Title:  Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society     Volume:  19     ISSN:  1524-475X     ISO Abbreviation:  Wound Repair Regen     Publication Date:    2011 Jul-Aug
Date Detail:
Created Date:  2011-07-06     Completed Date:  2011-12-06     Revised Date:  2012-03-02    
Medline Journal Info:
Nlm Unique ID:  9310939     Medline TA:  Wound Repair Regen     Country:  United States    
Other Details:
Languages:  eng     Pagination:  481-6     Citation Subset:  IM    
Copyright Information:
© 2011 by the Wound Healing Society.
Affiliation:
Institute of Reconstructive Plastic Surgery, New York University Langone Medical Center, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Diabetes Mellitus / metabolism
Disease Models, Animal
Fibroblast Growth Factor 2 / genetics,  metabolism
Gene Silencing*
Hypoxia-Inducible Factor 1, alpha Subunit / genetics,  metabolism*
Mice
Neovascularization, Physiologic
Procollagen-Proline Dioxygenase / antagonists & inhibitors*,  genetics
RNA, Messenger / metabolism
RNA, Small Interfering*
Skin / injuries,  metabolism
Vascular Endothelial Growth Factor A / genetics,  metabolism
Wound Healing*
Grant Support
ID/Acronym/Agency:
1UL1RR029893-01/RR/NCRR NIH HHS; UL1 RR029893-01/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Hif1a protein, mouse; 0/Hypoxia-Inducible Factor 1, alpha Subunit; 0/RNA, Messenger; 0/RNA, Small Interfering; 0/Vascular Endothelial Growth Factor A; 103107-01-3/Fibroblast Growth Factor 2; EC 1.14.11.2/Egln1 protein, mouse; EC 1.14.11.2/Procollagen-Proline Dioxygenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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