Eskenasy M, Mora R, Simionescu N
Morphol Embryol (Bucur). 1984 Apr-Jun;30(2):147-52.
Possibility of LDL--collagen complex formation was investigated in vitro by biochemical assay and electron microscopy. Types I and III collagen isolated from bovine thoracic aorta were incubated with human low density lipoproteins (LDL) at physiological ionic strength, pH and temperature. Biochemical quantification showed that 10-20 micrograms LDL (cholesterol) were bound per 100 micrograms collagen, binding of type III being slightly more pronounced (17%) than that of type I (11%). Binding was in inversely proportional to the extent of fibrillation. The increase of ionic strength and pH reduced the binding, indicating the electrostatic nature of the interaction. These observations suggest a possible trapping mechanism of LDL in the extracellular matrix by means of collagen, which may be relevant for the development of the atherosclerotic lesions.
通过生化分析和电子显微镜在体外研究了低密度脂蛋白（LDL）与胶原蛋白复合物形成的可能性。从牛胸主动脉分离出的I型和III型胶原蛋白在生理离子强度、pH值和温度下与人低密度脂蛋白（LDL）一起孵育。生化定量分析表明，每100微克胶原蛋白结合10 - 20微克LDL（胆固醇），III型胶原蛋白的结合比I型（11%）略明显（17%）。结合与原纤维形成程度成反比。离子强度和pH值的增加会降低结合，表明这种相互作用具有静电性质。这些观察结果提示LDL可能通过胶原蛋白在细胞外基质中被捕获，这可能与动脉粥样硬化病变的发展有关。
