Plasma lipid oxidation and susceptibility of low-density lipoproteins to oxidation in male patients with stable coronary artery disease.

Objectives: Oxidative modifications of low-density lipoproteins (LDL) are considered to be important in the pathogenesis of atherosclerosis. However, the data on the association between LDL oxidation and severity of clinical manifestations of coronary artery disease (CAD) are contradictory. Previous reports were concerned mostly with unstable angina patients.

Structure and possible biological roles of Lp(a).

Lipoprotein(a) [Lp(a)] is a plasma macromolecular complex that is assembled from low-density lipoproteins (LDL) and a large hydrophilic glycoprotein, named apolipoprotein(a) [apo(a)], linked by a disulfide bond to apolipoprotein B-100. Apo(a) is formed by different structural domains one of which is present in multiple copies, the number of which is determined by variation in the hypervariable apo(a) gene. Sequence homology of apo(a) with plasminogen may explain the competition of Lp(a) for some physiological functions of plasminogen in the coagulation and fibrinolytic cascade in vitro.

Lysine-binding species of lipoprotein(a) in coronary artery disease.

Elevated levels of plasma lipoprotein(a) [Lp(a)] have frequently been associated with coronary artery disease (CAD). Recently Lp(a) was fractionated into two species with different affinities for Lysine-Sepharose. The influence of lysine-binding heterogeneity of Lp(a) on its cardiovascular pathogenicity has not previously been studied.

Adhesion of mouse hepatocytes to type I collagen: role of supramolecular forms and effect of proteolytic degradation.

Mouse hepatocytes were found to adhere much stronger to intact native type I collagen than to native, telopeptide-devoid collagen. Removal of telopeptides (by pepsin treatment) caused disintegration of supramolecular collagen aggregates. Similar differences in hepatocyte adhesion were observed between oligomeric and monomeric collagens separated from intact native preparations.