Association between cigarette smoking and serum alpha klotho levels among US adults over 40-years-old: a cross-sectional study.

Alpha klotho (α-Klotho) is an anti-aging molecule associated with aging and several diseases. Previous studies have reported inconsistent levels of α-Klotho in smokers. This study aimed to demonstrate serum α-Klotho levels in smokers among the US population. This cross-sectional study recruited 11,559 participants (aged 40-79 years; 48.2% males). All data were collected from the 2007-2016 National Health and Nutrition Examination Survey. The study comprised adults with reliable Klotho and smoking questionnaire results. The relationship between smoking and serum α-klotho levels was assessed using multivariate linear regression models after adjusting for potential confounders. We also performed a stratified analysis of clinically important variables. The mean serum α-klotho level among the 11,559 participants was 843.85 pg/mL. After full adjustment, habitual smoking was significantly associated with decreased serum levels of α-klotho level (ß = - 34.89; 95% CI - 54.97, - 14.81; P = 0.0013) in the total study population. Furthermore, the stratified analysis indicated that the association was insignificant in the 60-79 age group. Quitting smoking was not significantly associated with serum levels of α-klotho as expected (P = 0.1148) in the total study population. However, stratified analyses showed a significant inversed association in the male, those with chronic kidney disease, or those with cancer who quit smoking (all P < 0.05). Cigarette smoking was inversely associated with serum α-Klotho levels among US adults.

[Study on the effect of aluminum (III) on NADH in the presence of NH4Ac in aqueous solution].

This paper studied the interactions of Al (III ) and dihydronicotinamide adenine dinucleotide (NADH) in nearly neutral aqueous solutions (pH 6.5) by means of UV-Vis and 1H, 13C-NMR techniques. The results suggested that Al (III) interacts with NADH to form Al-NADH complexes by occupying the binding sites of phosphate oxygen atoms O(N)1 and O(A)1 and ribose ring hydroxyl groups, which are the potential recognition sites for substrates, coenzyme and enzyme. In the presence of NH4Ac salt buffer and with Al (III) salt solution, NADH will be marked with structural changes at the nicotinamide moiety in contrast with almost no structural changes in Tris-HCl buffer solution with Al (III) salt.