Apostolski S, Sadiq S A, Hays A, Corbo M, Suturkova-Milosevic L, Chaliff P, Stefansson K, LeBaron R G, Ruoslahti E, Hays A P
Department of Neurology, Columbia Presbyterian Medical Center, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
J Neurosci Res. 1994 Jun 1;38(2):134-41. doi: 10.1002/jnr.490380203.
A subset of human anti-GM1 ganglioside antibodies cross-reacts with Gal(beta 1-3)GalNAc bearing glycoproteins in peripheral nerve and spinal cord. The same oligosaccharide determinant is recognized by the lectin peanut agglutinin (PNA) which binds at the nodes of Ranvier in intact peripheral nerve. The Gal(beta 1-3)GalNAc bearing glycoproteins were isolated using PNA lectin affinity chromatography followed by separation on Western blot, and the proteins were subjected to partial amino acid sequence analysis. Two major PNA binding glycoproteins were identified in peripheral nerve and spinal cord; one had an approximate molecular weight of 120 kD and had sequence homology to the oligodendrocyte-myelin glycoprotein (OMgp). The other migrated between 70 and 80 kD and had sequence homology to the hyaluronate binding domain of versican, which has been reported to share sequence homology with the 70 kD proteins hyaluronectin and the glial hyaluronic acid binding protein (GHAP). By immunocytochemistry, OMgp was localized to the paranodal region of myelin, and the protein homologous to the hyaluronate binding domain of versican was localized to the nodal gap in peripheral nerve. These PNA binding glycoproteins might be target antigens for autoantibodies in peripheral nerve.
一部分人抗GM1神经节苷脂抗体与外周神经和脊髓中携带Gal(β1-3)GalNAc的糖蛋白发生交叉反应。凝集素花生凝集素（PNA）可识别相同的寡糖决定簇，它能结合完整外周神经的郎飞结。使用PNA凝集素亲和层析法分离出携带Gal(β1-3)GalNAc的糖蛋白，随后通过蛋白质印迹法进行分离，并对这些蛋白质进行部分氨基酸序列分析。在外周神经和脊髓中鉴定出两种主要的PNA结合糖蛋白；一种的分子量约为120kD，与少突胶质细胞髓磷脂糖蛋白（OMgp）具有序列同源性。另一种在70至80kD之间迁移，与多功能蛋白的透明质酸结合结构域具有序列同源性，据报道该结构域与70kD蛋白透明质连接蛋白和神经胶质透明质酸结合蛋白（GHAP）具有序列同源性。通过免疫细胞化学方法，OMgp定位于髓磷脂的结旁区域，与多功能蛋白透明质酸结合结构域同源的蛋白定位于外周神经的结间隙。这些PNA结合糖蛋白可能是外周神经自身抗体的靶抗原。
