Heme oxygenase-1 and heme oxygenase-2 expression in bruises.

Abstract

The first step in catabolism of hemoglobin in a bruise is performed by the enzyme heme oxygenase, which produces biliverdin that is then reduced to bilirubin. The development of yellow coloration in bruises can be attributed to local accumulation of degradation products of hemoglobin, including bilirubin, but it is not clear why there is a delay before this color change is apparent. One explanation may be that time is required for the establishment of heme oxygenase activity at the bruise site. This study used immunohistochemistry to examine the time course of expression of heme oxygenase-1 and heme oxygenase-2 in a rat bruise model. Heme oxygenase-1 levels rose above background from 6 h to peak from days 1 to 3. There was strong expression by macrophages, but only occasional neutrophils expression of heme oxygenase-1. Heme oxygenase-2 did not change significantly from background levels. The results suggest that the delay in the development of yellow coloration of bruises may in part be attributed to the requirement for macrophages to be recruited to the site of injury.

• Authors: Neil E I Langlois, Kelly Olds, Claire Ross, Roger W Byard
• Journal: Forensic science, medicine, and pathology (Forensic Sci Med Pathol) Vol. 11 Issue 4 Pg. 482-7 (Dec 2015) ISSN: 1556-2891 [Electronic] United States
• PMID: 25772118 (Publication Type: Journal Article)

Chemical References

• Biomarkers
• Heme Oxygenase (Decyclizing)
• Heme Oxygenase-1
• heme oxygenase-2

Topics

• Animals
• Biomarkers (metabolism)
• Contusions (enzymology, pathology)
• Forensic Pathology
• Heme Oxygenase (Decyclizing) (metabolism)
• Heme Oxygenase-1 (metabolism)
• Immunohistochemistry
• Macrophages (enzymology)
• Models, Animal
• Neutrophils (enzymology)
• Rats, Sprague-Dawley
• Staining and Labeling
• Time Factors