A well-oxygenated cells environment may help to fight against protein glycation.
Int J Occup Med Environ Health
; 24(1): 102-7, 2011 Mar.
Article
in En
| MEDLINE
| ID: mdl-21468907
ABSTRACT
OBJECTIVES:
Normoglycemic Wistar rats' Glycated Hemoglobin Levels (GHL) showed a time-dependent difference between control groups and those exposed to regular inhalation of peroxidizing extracts of turpentine. These extracts were able to optimize the oxygen permeation at the cellular level during and subsequently to a breathing session. The more the rats breathed turpentine peroxidized vapor, the lower their GHL was. This study was designed to confirm, in ex-vivo blood samples, the impact of peroxidizing extract on the GHL. MATERIALS ANDMETHODS:
Red blood cells were separated from plasmas by centrifugation. Plasmas were treated by peroxidizing and non-peroxidizing turpentine vapor or untreated (control), then combined with washed red blood cells three hours before evaluation. Glycation of hemoglobin proteins was quantified according to the Habeed's method.RESULTS:
The ex-vivo experiments showed that the peroxidizing terpenes reduced the GHL after a three-hour contact. So did oxidized terpenes. Controls and the volatile component of the expended essential oil showed the opposite results.CONCLUSION:
Optimal oxygenation, especially when facilitated by the peroxidized volatile component of the essential oil of turpentine, can protect organisms (mammals in this study) from protein glycation. Optimizing oxygenation can also reduce the GHL of treated blood samples after three hours of incubation.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Glycated Hemoglobin
/
Erythrocytes
Limits:
Animals
Language:
En
Journal:
Int J Occup Med Environ Health
Journal subject:
MEDICINA OCUPACIONAL
/
SAUDE AMBIENTAL
Year:
2011
Document type:
Article
Affiliation country: