Bronfman F C, Garrido J, Alvarez A, Morgan C, Inestrosa N C
Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile.
Neurosci Lett. 1996 Nov 8;218(3):201-3. doi: 10.1016/s0304-3940(96)13147-5.
Laminin, an important extracellular matrix component is induced by brain injury and colocalizes with amyloid-beta-peptide (A beta) deposits in Alzheimer brains. We report here that laminin inhibits amyloid fibril formation as determined by thioflavin T fluorescence spectroscopy and electron microscopic examination. The inhibition of amyloid formation by laminin was concentration dependent and was observed at a laminin concentration of 300 nM, corresponding to a laminin/A beta protein molar ratio of 1:800. The potential effect of laminin, may prove important to inhibit A beta fibrillogenesis in vivo, specifically at the level of cerebral blood vessels.
层粘连蛋白是一种重要的细胞外基质成分，由脑损伤诱导产生，并与阿尔茨海默病患者大脑中的β-淀粉样肽（Aβ）沉积物共定位。我们在此报告，通过硫黄素T荧光光谱法和电子显微镜检查确定，层粘连蛋白可抑制淀粉样纤维的形成。层粘连蛋白对淀粉样蛋白形成的抑制作用呈浓度依赖性，在层粘连蛋白浓度为300 nM时即可观察到，该浓度对应的层粘连蛋白/Aβ蛋白摩尔比为1:800。层粘连蛋白的潜在作用可能对体内抑制Aβ纤维形成很重要，特别是在脑血管水平。
