Prevalence of lipid risk factors for atherosclerosis in the Curacao Health Study: interactions with demographic and socio-economic variables - asbtract

The Curacao Health Study is a cross-sectional population-based study designed to give insight into the determinants of health on Curacao. This study presents prevalence data for lipid risk factors and interactions with demographic and socio-economic variables. Serum was collected from 1001 (44.5 percent) respondents included in the CHS study. These respondents were representative for all respondents. Cholesterol, HDL-cholesterol and triglycerides were measured and LDL-cholesterol was calculated. Cholesterol levels increased significantly in women > 50 years of age, as did LDL-cholesterol levels. HDL-cholesterol was higher in women than in men (52 ñ 13 mg/dl vs 48 ñ 15 mg/dl). Mean total and LDL-cholesterol levels were comparable to Western European and Northern American populations. Multiple regression indicated that race (Black vs non-Black) did not contribute to cholesterol levels, whereas education, living in the East District, age, and gender did. These associations need further study before definitive conclusions can be drawn. We conclude that lipid risk factors are as prevalent on Curacao as in most Western societies (AU)

Lysine-binding heterogeneity of Lp(a): consequences for fibrin binding and inhibition of plasminogen activation.

Lipoprotein(a) [Lp(a)] is recognized as an independent risk factor for atherosclerosis. Lp(a) consists of a LDL-like moiety with an additional glycoprotein, apo(a), linked to apolipoprotein B-100. Apo(a) has a high homology with plasminogen (Pg). In vivo, Pg is activated on a fibrin surface by tissue Pg activator (tPA). We prepared Lp(a) from plasma by sequential ultracentrifugation followed by lysine-sepharose affinity chromatography. We found that a changing (donor dependent) fraction of the Lp(a) did not bind to lysine-sepharose. This fraction, designated Lp(a)lys-, was further purified using gel filtration. Bound Lp(a) [Lp(a)lys+] was eluted with 0.2 M EACA. Apo(a) isoforms in both fractions were identical. In contrast Lp(a)lys+ inhibited Pg activation by tPA in vitro (IC50% 20 mg/l), whereas Lp(a)lys- did not. In addition Lp(a)lys- did not bind to CNBr-digested fibrinogen whereas Lp(a)lys+ did (Kd, app = 0.2 nM). Therefore we conclude that a changing donor dependent fraction of human plasma Lp(a) does not inhibit Pg activation in vitro and does not bind to CNBr-digested fibrinogen.