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Sex influences systemic and peripheral blood mononuclear cell production of superoxide in older adults (1153.11)
Author(s) -
Schanzle Jennifer,
Deo Shekhar,
Fadel Paul
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.1153.11
Subject(s) - nadph oxidase , peripheral blood mononuclear cell , oxidative stress , superoxide , western blot , medicine , intracellular , endocrinology , reactive oxygen species , andrology , immunology , enzyme , chemistry , gene , biochemistry , in vitro
Previous work suggests that elevations in oxidative stress are associated with cardiovascular disease. Although it is well known that oxidative stress increases with age, whether this occurs differently in men and women remains unclear. Likewise, recent work indicating that mRNA expression for NADPH oxidase is greater in peripheral blood mononuclear cells (PBMCs) of older subjects did not differentiate sex effects. Therefore, we measured plasma and intracellular levels of superoxide (O 2 ●‐ ), along with PBMC expression of NADPH oxidase subunits in 12 healthy older post‐menopausal women and 10 age‐matched older men. Older men demonstrated greater plasma O 2 ●‐ levels (lucigenin chemiluminescence; men 202.73 ± 9.28 vs. women 171.67 ± 7.72, Relative Light Units; P <0.05) as well as intracellular O 2 ●‐ in PBMCs (dihydroethidium fluorescence; men 1.94 ± 0.20 vs. women 0.96 ± 0.14, Relative Fluorescence Units; P <0.05) compared to older women. Similarly, western blot analysis demonstrated that older men exhibit greater NADPH oxidase subunit protein expression for gp91 phox , p22 phox , and p47 phox in PBMCs (e.g., gp91 phox ; men 1.48 ± 0.38 vs. women 0.31 ± 0.07; P <0.05) and p67 phox tended to be higher ( P =0.14). These preliminary findings suggest that systemic O 2 ●‐ levels are greater in older men compared to older women and PBMC‐derived O 2 ●‐ production via NADPH oxidase is a likely contributing source. Grant Funding Source : Supported by NIH R01 HL093167