Cho S S, Lucas J J, Roh E J, Yoo Y B, Lee K H, Park K H, Hwang D H, Baik S H
Department of Anatomy, Seoul National University, College of Medicine, Korea.
J Comp Neurol. 1997 Jun 2;382(2):260-71.
Transferrin binding protein (TfBP) is a glycoprotein originally purified from chicken oviduct that exhibits transferrin binding activity. Recent work has shown that TfBP is a post-translationally modified form of the heat shock protein (HSP108), the avian homologue of a glucose regulated protein, GRP94. The function of this protein, however, has not yet been clearly defined. Antiserum to TfBP was found to selectively stain oligodendrocytes of the avian brain. In this study, we further describe these oligodendrocytes and other cell types positive to anti-TfBP in the chick nervous system. In accordance with previous studies, the most prominent cell type that labels with antiserum to TfBP is the oligodendrocyte. At the electron microscopic level, the immunoreactive product is confined to the perinuclear cytoplasm and fine processes of the oligodendrocytes, whereas myelin and axoplasm are devoid of staining. The immunoreactive product is found both in the cytoplasmic matrix and bound to the endoplasmic reticulum and plasma membrane, suggesting that TfBP may have properties of both a soluble and an integral membrane protein. There is great variability in the number of TfBP-oligodendrocytes in different areas of the central nervous system (CNS); large numbers of cells are associated with the white matter regions and are found in the myelinated tracts, whereas few cells are present in the gray matter regions. In the retina, TfBP is localized specifically in the cells, that are morphologically oligodendrocytic and is present in the optic nerve fiber layer and the ganglion cell layer. Obvious staining is also seen in the Bergmann glial cells of the cerebellum and in the Schwann cells of the sciatic nerve. Furthermore, the choroid plexus cells similarly exhibit a strong reaction. The association of TfBP in these specific cell types responsible for myelination and sequestering iron and transferrin implies that TfBP may be involved in myelination and iron metabolism of the chick nervous system, perhaps through a role in transferrin concentration in these cells. A putative role of TfBP, as HSP108, is considered.
转铁蛋白结合蛋白(TfBP)是一种最初从鸡输卵管中纯化出来的糖蛋白,具有转铁蛋白结合活性。最近的研究表明,TfBP是热休克蛋白(HSP108)的翻译后修饰形式,HSP108是葡萄糖调节蛋白GRP94的禽类同源物。然而,这种蛋白质的功能尚未明确界定。发现抗TfBP血清可选择性地对禽脑的少突胶质细胞进行染色。在本研究中,我们进一步描述了这些少突胶质细胞以及鸡神经系统中其他抗TfBP阳性的细胞类型。与先前的研究一致,用抗TfBP血清标记的最突出细胞类型是少突胶质细胞。在电子显微镜水平上,免疫反应产物局限于少突胶质细胞的核周细胞质和细突起中,而髓鞘和轴质则无染色。免疫反应产物存在于细胞质基质中,并与内质网和质膜结合,这表明TfBP可能同时具有可溶性蛋白和整合膜蛋白的特性。中枢神经系统(CNS)不同区域的TfBP阳性少突胶质细胞数量差异很大;大量细胞与白质区域相关,存在于有髓神经纤维束中,而灰质区域中细胞很少。在视网膜中,TfBP特异性定位于形态上为少突胶质细胞的细胞中,存在于视神经纤维层和神经节细胞层。在小脑的伯格曼胶质细胞和坐骨神经的施万细胞中也可见明显染色。此外,脉络丛细胞同样表现出强烈反应。TfBP在这些负责髓鞘形成以及铁和转铁蛋白隔离的特定细胞类型中的存在,意味着TfBP可能参与鸡神经系统的髓鞘形成和铁代谢,可能是通过在这些细胞中转铁蛋白浓度方面发挥作用。还考虑了TfBP作为HSP108的假定作用。