Protective properties of sardine and chickpea protein hydrolysates against lipoprotein oxidative damages and some inflammation markers in hypercholesterolemic rats

OBJECTIVE: This study evaluated the effect of sardine (SPH) and chickpea protein hydrolysates (CPH) on oxidant stress and inflammatory profile in cholesterol-fed rats. METHODS: The experiment was undertaken for thirty days on 18 cholesterol-fed Wistar rats (220±10 g) divided into three groups and receiving 1 g/kg of body weight either chickpea protein hydrolysate (CPH), sardine protein hydrolysate (SPH) or casein in water (CG). RESULTS: Compared to CG, SPH and CPH treatment reduced cholesterol, hydroperoxide and malondialdehyde contents in serum, lipoproteins, erythrocytes and aorta. These same treated groups showed also lower serum isoprostane levels. However, serum paraoxonase activity and HDL-antioxidant property were improved only by CPH compared to CG. SOD activity of aorta and erythrocytes was higher in CPH but in SPH group, SOD activity was lower in these tissues and remained unchanged in serum. Furthermore, CPH and SPH stimulated glutathione peroxidase and catalase activities of aorta and erythrocytes. In CPH group, nitric oxide levels of serum, erythrocytes and aorta were increased by respectively 1.4- to 1.8-fold compared to CG and SPH. In addition, among the three groups, CPH exhibited the best anti-inflammatory effect by lowering serum C reactive protein, uric acid and albumin concentrations. CONCLUSIONS: SPH and particularly CPH possess antioxidant and anti-inflammatory properties and could be useful as nutraceuticals for health improving and preventing numerous disorders such as cardiovascular diseases.

Lysine Reacts with Cholesterol Hydroperoxide to Form Secosterol Aldehydes and Lysine-Secosterol Aldehyde Adducts

Two cholesterol secosterol aldehydes, namely, 3β-hydroxy-5-oxo-5,6-secocholestan-6-al (secosterol A) and its aldolization product 3β-hydroxy-5β-hydroxy-B-norcholestane-6β-carboxyaldehyde (secosterol B), are highly bioactive compounds which have been detected in human tissues and potentially contribute to the development of physiological dysfunctions such as atherosclerosis, Alzheimer’s disease, diabetes, and cancer. They were originally considered to be exclusive products of cholesterol ozonolysis and thus to be evidence for endogenous ozone formation. However, it was recently postulated that primary amines such as lysine may catalyse their formation from cholesterol-5α-hydroperoxide (Ch-5α-OOH), the main product of the oxidation of cholesterol with singlet oxygen. This involves cyclization of Ch-5α-OOH to an unstable dioxetane intermediate, which decomposes to form secosterol aldehydes with triplet carbonyl groups, whose return to the singlet state is at least partly coupled to the conversion of triplet molecular oxygen to singlet oxygen. Here, we subjected cholesterol to photosensitized oxidation, which predominantly produces Ch-5α-OOH and minor amounts of the 6α- and 6β-hydroperoxides, exposed the hydroperoxide mixture to lysine in the presence of the antioxidant 2,6-ditertiary-butyl-4-hydroxytoluene (BHT), and analysed the reaction mixture by liquid chromatography-electrospray ionization-mass spectrometry. Consistent with the postulated lysine-catalysed formation of secosterol aldehydes, we detected formation of the latter and several types of their lysine adducts, including carbinolamines, Schiff’s bases, and amide-type adducts. We propose that the amide type adducts, which are major biomarkers of lipid oxidation, are mainly formed by singlet oxygen-mediated oxidation of the carbinolamine adducts.