Human epidermal keratinocyte expression of sialyl-Lewis X.
Human epidermal keratinocyte expression of sialyl-Lewis X.
复制标题
人表皮角质形成细胞表达唾液酸-Lewis X。
DOI：
10.1111/1523-1747.ep12668005
复制
发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Symington,BE
中科院分区：
文献类型：
--
作者：
Symington,FW;Holmes,EH;Symington,BE
细胞表面寡糖可以作为细胞间粘附受体、基质蛋白和生长因子的配体。据报道，人类新生儿和成人表皮角质形成细胞（KC）表达sialyl Lewis X [s-Lex；SAα2-3Galβ-4(Fucα1-3)GlcNAcβ-3R]，内皮和血小板选择素的配体。新鲜分离或培养的KC结合FH6单克隆抗体（MoAb），这是特异性的含s- lex寡糖。相关的表位是真正的s-Lex，因为唾液酸酶处理的KC悬浮液消除了FH6的结合，同时产生了新的KC反应性，在冷冻悬浮液中染色的抗lexkc显示出免疫荧光显微镜可检测到的s-Lex的结状膜分布。正如其他人所报道的那样，在垂直的皮肤切片中，FH6似乎没有与KC结合。然而，在完整表皮片中，当染色和正面观察时，基底KC与FH6表现出明显的“蜂房”反应性，这表明s-Lexin完整表皮可能出现在平行于主要组织轴的带状中。FH6特异性免疫沉淀来自[35S]标记的KC的Mr为34 kd、44 kd和56 kd的蛋白，以及来自唾液酸酶处理的KC的抗lex沉淀物类似蛋白。通过分析KC聚焦转移酶的受体特异性和其他特性，研究了KC s- lex表达的酶基础。结果表明，KC表达lewis和骨髓型α1-3聚焦转移酶。KC s-Lexand可能是上皮环境的重要组成部分，因为上皮细胞和上皮细胞所在地的免疫细胞都表达s-Lexand相关结构，并且因为KC s-Lexand在经皮损伤后很好地定位于选择素介导的血小板结合。s-Lexin在表皮和分离的KC上的明显分布与s-Lexin在细胞间相互作用中的功能作用是相容的。
Cell-surface oligosaccharides can function as ligands for intercellular adhesion receptors, matrix proteins, and growth factors. 9ge report that human neonatal and adult epidermal keratinocytes (KC) express sialyl Lewis X [s-Lex; SAα2-3Galβ-4(Fucα1-3)GlcNAcβ-3R], a ligand for endothelial and platelet selectins. Freshly isolated or cultured KC bind FH6 monoclonal antibody (MoAb), which is specific for s-Lex-containing oligosaccharides. The relevant epitope is bona fide s-Lex, because sialidase treatment of KC suspensions abrogates FH6 binding while generating de novo KC reactivity with anti-LexKC stained in ice-cold suspension display a knobby membrane distribution of s-Lexdetectable by immunofluorescence microscopy. As others have reported, FH6 appeared not to bind KC in perpendicular skin sections However, basal KC in intact epidermal sheets exhibited obvious “honeycomb” reactivity with FH6 when stained and viewed en face, suggesting that s-Lexin intact epidermis may occur in bands that parallel the major tissue axis. FH6 specifically immunoprecipitated proteins of Mr 34 kd, 44 kd, and 56 kd from [35S]-labeled KC, and anti-Lexprecipitated similar proteins from sialidase-treated KC The enzymatic basis for KC s-Lexexpression was studied by analyzing acceptor specificities and other properties of KC fucosyltransferases. Results indicate that KC express both Lewisand myeloid-type α1-3fucosyltransferases. KC s-Lexcould be an important element of the epithelial milieu, because both epithelial cells and immune cells that home to epithelia express s-Lexand related structures, and because KC s-Lexis well positioned for selectin-mediated platelet binding after transcutaneous wounding. The apparent distributions of s-Lexin epidermis and on isolated KC are compatible with a functional role for s-Lexin these intercellular interactions.