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Protein Carbamylation: A Marker Reflecting Increased Age-Related Cell Oxidation
- Source :
- E-Prints Complutense: Archivo Institucional de la UCM, Universidad Complutense de Madrid, International Journal of Molecular Sciences, Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid, Consejería de Sanidad de la Comunidad de Madrid, International Journal of Molecular Sciences, Vol 19, Iss 5, p 1495 (2018), E-Prints Complutense. Archivo Institucional de la UCM, instname, International Journal of Molecular Sciences; Volume 19; Issue 5; Pages: 1495, DDFV: Repositorio Institucional de la Universidad Francisco de Vitoria, Universidad Francisco de Vitoria, DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
- Publication Year :
- 2018
- Publisher :
- International Journal of Molecular Sciences, 2018.
-
Abstract
- Carbamylation is a post-translational modification of proteins that may partake in the oxidative stress-associated cell damage, and its increment has been recently proposed as a “hallmark of aging”. The molecular mechanisms associated with aging are related to an increased release of free radicals. We have studied whether carbamylated proteins from the peripheral blood of healthy subjects are related to oxidative damage and aging, taking into account the gender and the immune profile of the subjects. The study was performed in healthy human volunteers. The detection of protein carbamylation and malondialdehyde (MDA) levels was evaluated using commercial kits. The immune profile was calculated using parameters of immune cell function. The results show that the individuals from the elderly group (60–79 years old) have increased carbamylated protein and MDA levels. When considered by gender, only men between 60 and 79 years old showed significantly increased carbamylated proteins and MDA levels. When those subjects were classified by their immune profile, the carbamylated protein levels were higher in those with an older immune profile. In conclusion, the carbamylation of proteins in peripheral blood is related to age-associated oxidative damage and to an aging functional immunological signature. Our results suggest that carbamylated proteins may play an important role at the cellular level in the aging process. post-print 1319 KB
- Subjects :
- 0301 basic medicine
Male
Aging biomarker
Aging
functional immune signature
Functional immune signature
Cell
oxidative damage
Lipid peroxidation
Oxidative damage
lcsh:Chemistry
chemistry.chemical_compound
Malondialdehyde
lcsh:QH301-705.5
protein carbamylation
Spectroscopy
Aged, 80 and over
Protein carbamylation
aging biomarker
immune profile
lipid peroxidation
malondialdehyde
Age Factors
General Medicine
Middle Aged
Computer Science Applications
Immune profile
medicine.anatomical_structure
Female
Oxidation-Reduction
Adult
medicine.medical_specialty
Inmunología
Oxidative phosphorylation
Catalysis
Article
Inorganic Chemistry
03 medical and health sciences
Young Adult
Immune system
Sex Factors
Internal medicine
Age related
medicine
Humans
Physical and Theoretical Chemistry
Molecular Biology
Cell damage
Aged
Biología celular
business.industry
Organic Chemistry
Proteins
medicine.disease
030104 developmental biology
Endocrinology
chemistry
lcsh:Biology (General)
lcsh:QD1-999
business
Reactive Oxygen Species
Protein Processing, Post-Translational
Biomarkers
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- E-Prints Complutense: Archivo Institucional de la UCM, Universidad Complutense de Madrid, International Journal of Molecular Sciences, Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid, Consejería de Sanidad de la Comunidad de Madrid, International Journal of Molecular Sciences, Vol 19, Iss 5, p 1495 (2018), E-Prints Complutense. Archivo Institucional de la UCM, instname, International Journal of Molecular Sciences; Volume 19; Issue 5; Pages: 1495, DDFV: Repositorio Institucional de la Universidad Francisco de Vitoria, Universidad Francisco de Vitoria, DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
- Accession number :
- edsair.doi.dedup.....76449c354776244312e20bfe69935253