Ultrastructural localization of Helix pomatia lectin-binding sites in mouse lung elastic fibers.
Ultrastructural localization of Helix pomatia lectin-binding sites in mouse lung elastic fibers.
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小鼠肺弹性纤维中蜗牛凝集素结合位点的超微结构定位。
DOI：
10.1007/bf00490173
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Bale,LA
中科院分区：
文献类型：
--
作者：
Palmer,KC;Bale,LA
乳突螺旋体(蜗牛)凝集素与胶体金(HPL-Gold)络合后，可识别不同年龄小鼠肺组织塑料包埋切片中弹性纤维上的结合部位。用电子显微镜观察凝集素-金粒子的沉积情况。肺血管弹力板和整个肺的弹性纤维等结构被HPL-Gold复合体特异性地和强烈地装饰，并容易被观察到。HPL-金颗粒主要结合在弹性蛋白无定形成分上的位置，几乎排除了微纤维弹性蛋白成分、胶原纤维和细胞外基质的其他成分。此外，HPL-Gold与弹性蛋白结合的中等年龄差异也很明显。这些观察结果似乎首次证明，在弹性蛋白的无定形成分中，存在由HPL特异性识别的糖结合物，并提出了一种方法，通过该方法可以探索糖结合物在肺弹性形成中的参与。
Helix pomatia(Snail) lectin complexed with colloidal gold (HPL-gold) recognized binding sites on elastic fibers in plastic embedded sections of lung tissue from mice of several ages. Deposition of the lectin-gold particles was examined by electron microscopy. Structures such as the elastic laminae of pulmonary vessels and elastic fibers throughout the lung was specifically and intensely decorated by the HPL-gold complex and easily visualized. The binding of the HPL-gold particles was primarily to sites on the amorphous component of elastin, to the virtual exclusion of the microfibrillar elastin elements, collagen fibers and other components of the extracellular matrix. In addition, moderate age differences in the binding of HPL-gold to elastin were apparent. These observations appear to be the first demonstration of the presence, in the amorphous component of elastin, of glycoconjugates that are specifically recognized by HPL and suggest a method by which the involvement of glycoconjugates in lung elastogenesis could be explored.