Illés T, Fischer J
Orthopaedic Clinic, University Medical School of Pécs, Hungary.
Histochemistry. 1989;91(1):55-9. doi: 10.1007/BF00501912.
Arachis hypogaea (PNA) lectin, specific for Gal-B-1,3-GalNac disaccharide and Wheat germ (WGA) lectin, specific for (GlcNac) and terminal neuraminic acid were used to identify histiocytic giant cells, osteoclast like giant cells and osteoclasts. PNA lectin, without neuraminidase predigestion was not bound by the giant cells, while they showed a strong reaction with WGA lectin. Neuraminidase pretreatment decreased WGA lectin binding, which supports that neuraminic acid plays a role in the binding of WGA. On the other hand, neuraminidase digestion liberated large amounts of PNA binding sites in every type of giant cells examined, showing a strong, intracytoplasmic granular staining. This observation is indicative of presence of PNA binding sites masked by neuraminic acid. Instead of the intracytoplasmic PNA binding in some osteoclasts a well defined part of the cytomembrane was heavily stained. We suppose that this PNA binding part of cytomembrane equals to the zone of resorption, characterized by the ruffled border of osteoclasts. Our findings indicate that a neuraminic acid substituted PNA binding glycoprotein is synthetized both in osteoclasts and histiocytic giant cells which may indicate a common origin of these cell types.
针对Gal-β-1,3-GalNAc二糖具有特异性的花生凝集素（PNA）和针对（GlcNAc）及末端神经氨酸具有特异性的小麦胚芽凝集素（WGA），被用于鉴定组织细胞性巨细胞、破骨细胞样巨细胞和破骨细胞。未经神经氨酸酶预先消化的PNA凝集素不与巨细胞结合，而它们与WGA凝集素呈现强烈反应。神经氨酸酶预处理降低了WGA凝集素的结合，这支持神经氨酸在WGA的结合中起作用。另一方面，神经氨酸酶消化在每种检测的巨细胞类型中释放出大量PNA结合位点，呈现强烈的胞浆颗粒染色。这一观察结果表明存在被神经氨酸掩盖的PNA结合位点。在一些破骨细胞中，胞浆内的PNA结合部位并非如此，而是细胞膜的一个明确部分被重度染色。我们推测细胞膜的这个PNA结合部分等同于吸收区，其特征为破骨细胞的皱褶缘。我们的研究结果表明，破骨细胞和组织细胞性巨细胞中均合成了一种神经氨酸取代的PNA结合糖蛋白，这可能表明这些细胞类型有共同的起源。
