Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments.
Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments.
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DOI：
10.1083/jcb.114.3.567
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发表时间：
1991-08
期刊：
影响因子：
--
通讯作者：
Burgeson RE
中科院分区：
文献类型：
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作者：
Rousselle P;Lunstrum GP;Keene DR;Burgeson RE
基底角质形成细胞通过超微结构独特且复杂的基底膜区域附着在下面的真皮基质上。沿着基底表面质膜的电子致密斑块（称为半桥粒）似乎通过细丝（称为锚定丝）直接附着在基底膜的致密层上。致密层通过含有锚定原纤维和锚定斑块的 VII 型胶原复合物固定到基质上。我们已经鉴定出我们认为是该组织区域特有的新抗原。针对该抗原的单克隆抗体定位于锚定丝，位于半桥粒基底致密板的正下方。在细胞培养中，抗原通过生长和迁移人角质形成细胞沉积在培养基质上。在培养物中添加单克隆抗体会导致细胞变圆和分离，但不会损害它们的代谢。与抗体一起温育的皮肤碎片广泛去上皮化。这些发现强烈表明该抗原与角质形成细胞与基底膜的附着密切相关。通过免疫亲和层析从角质形成细胞培养物中分离出该抗原。观察到两个分子。最完整的物种包含三个不同的链，分别为 165、155 和 140 kD，通过链间二硫键连接。第二种也是更丰富的物种包含 165-和 140-kD 链，但 155-kD 链已被蛋白水解裂解为 105 kD。同样，观察到两个旋转阴影图像。两者中较大的一个，大概对应于最完整的形式，看起来像一根不对称的 107 纳米长的棒，一端有一个小球，另一端有两个较小的球。更丰富的物种，大概是蛋白水解裂解的形式，缺乏远端小球。我们建议将这种新分子命名为“kalinin”。
Basal keratinocytes attach to the underlying dermal stroma through an ultrastructurally unique and complex basement membrane zone. Electron- dense plaques along the basal surface plasma membrane, termed hemidesmosomes, appear to attach directly to the lamina densa of the basement membrane through fine strands, called anchoring filaments. The lamina densa is secured to the stroma through a complex of type VII collagen containing anchoring fibrils and anchoring plaques. We have identified what we believe is a novel antigen unique to this tissue region. The mAbs to this antigen localize to the anchoring filaments, just below the basal-dense plate of the hemidesmosomes. In cell culture, the antigen is deposited upon the culture substate by growing and migrating human keratinocytes. Addition of mAb to the cultures causes the cells to round and detach, but does not impair them metabolically. Skin fragments incubated with antibody extensively de- epithelialize. These findings strongly suggest that this antigen is intimately involved in attachment of keratinocytes to the basement membrane. This antigen was isolated from keratinocyte cultures by immunoaffinity chromatography. Two molecules are observed. The most intact species contains three nonidentical chains, 165, 155, and 140 kD linked by interchain disulfide bonds. The second and more abundant species contains the 165- and 140-kD chains, but the 155-kD chain has been proteolytically cleaved to 105 kD. Likewise, two rotary-shadowed images are observed. The larger of the two, presumably corresponding to the most intact form, appears as an asymmetric 107-nm-long rod, with a single globule at one end and two smaller globules at the other. The more abundant species, presumably the proteolytically cleaved form, lacks the distal small globule. We propose the name "kalinin" for this new molecule.