Document Detail


Knockdown of heme oxygenase-2 impairs corneal epithelial cell wound healing.
MedLine Citation:
PMID:  21506105     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Heme oxygenase (HO) represents an intrinsic cytoprotective system based on its anti-oxidative and anti-inflammatory properties mediated via its products biliverdin/bilirubin and carbon monoxide (CO). We showed that deletion of HO-2 results in impaired corneal wound healing with associated chronic inflammatory complications. This study was undertaken to examine the role of HO activity and the contribution of HO-1 and HO-2 to corneal wound healing in an in vitro epithelial scratch injury model. A scratch wound model was established using human corneal epithelial (HCE) cells. These cells expressed both HO-1 and HO-2 proteins. Injury elicited a rapid and transient increase in HO-1 and HO activity; HO-2 expression was unchanged. Treatment with biliverdin or CORM-A1, a CO donor, accelerated wound closure by 10% at 24 h. Inhibition of HO activity impaired wound closure by more than 50%. However, addition of biliverdin or CORM-A1 reversed the effect of HO inhibition on wound healing. Moreover, knockdown of HO-2 expression, but not HO-1, significantly impaired wound healing. These results indicate that HO activity is required for corneal epithelial cell migration. Inhibition of HO activity impairs wound healing while amplification of its activity restores and accelerates healing. Importantly, HO-2, which is highly expressed in the corneal epithelium, appears to be critical for the wound healing process in the cornea. The mechanisms by which it contributes to cell migration in response to injury may reside in the cytoprotective properties of CO and biliverdin.
Authors:
Adna Halilovic; Kiran A Patil; Lars Bellner; Giuseppina Marrazzo; Kirkland Castellano; Giuseppe Cullaro; Michael W Dunn; Michal Laniado Schwartzman
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cellular physiology     Volume:  226     ISSN:  1097-4652     ISO Abbreviation:  J. Cell. Physiol.     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-04-20     Completed Date:  2011-06-17     Revised Date:  2014-03-19    
Medline Journal Info:
Nlm Unique ID:  0050222     Medline TA:  J Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1732-40     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Wiley-Liss, Inc.
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MeSH Terms
Descriptor/Qualifier:
Biliverdine / metabolism
Boranes / pharmacology
Carbon Monoxide / metabolism
Carbonates / pharmacology
Cell Movement
Cells, Cultured
Cytoprotection
Dose-Response Relationship, Drug
Epithelium, Corneal / drug effects,  enzymology*,  injuries,  pathology
Heme Oxygenase (Decyclizing) / deficiency*,  genetics
Heme Oxygenase-1 / deficiency,  genetics
Humans
RNA Interference
Time Factors
Transfection
Wound Healing* / drug effects
Grant Support
ID/Acronym/Agency:
EY06513/EY/NEI NIH HHS; R01 EY006513/EY/NEI NIH HHS; R01 EY006513-22/EY/NEI NIH HHS; R01 EY006513-22S1/EY/NEI NIH HHS; R01 EY006513-23/EY/NEI NIH HHS
Chemical
Reg. No./Substance:
0/Boranes; 0/Carbonates; 0/sodium boranocarbonate; 7U1EE4V452/Carbon Monoxide; EC 1.14.99.3/HMOX1 protein, human; EC 1.14.99.3/Heme Oxygenase (Decyclizing); EC 1.14.99.3/Heme Oxygenase-1; EC 1.14.99.3/heme oxygenase-2; O9MIA842K9/Biliverdine
Comments/Corrections

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


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