Piela-Smith T H, Korn J H
Division of Rheumatic Diseases, Veterans Administration Medical Center, Newington, Connecticut, USA.
Cell Immunol. 1995 Apr 15;162(1):42-8. doi: 10.1006/cimm.1995.1049.
Monoclonal antibodies were developed against human dermal fibroblast cell-surface membranes. Our goal was to find evidence of differential expression of antigens on fibroblast clones derived by limiting dilution. Antibodies were then used to isolate and identify membrane proteins. By sequence analysis of membrane immunoprecipitates, one monoclonal antibody, BR2, was subsequently shown to recognize the enzyme aminopeptidase N (hAPN; EC 3.4.11.2), originally described as a marker for certain hematopoetic cells. We have used biochemical techniques, electron microscopy, flow cytometry, and ELISA to characterize aminopeptidase N expression by human dermal fibroblasts. The presence of abundant aminopeptidase N confers enzymatic properties to human dermal fibroblasts which heretofore have been largely unexplored and suggest that the cellular distribution of aminopeptidase N is wider than originally appreciated.
针对人真皮成纤维细胞表面膜开发了单克隆抗体。我们的目标是寻找通过有限稀释获得的成纤维细胞克隆上抗原差异表达的证据。然后使用抗体分离和鉴定膜蛋白。通过对膜免疫沉淀物的序列分析，随后发现一种单克隆抗体BR2可识别氨肽酶N（hAPN；EC 3.4.11.2），该酶最初被描述为某些造血细胞的标志物。我们已使用生化技术、电子显微镜、流式细胞术和酶联免疫吸附测定（ELISA）来表征人真皮成纤维细胞中氨肽酶N的表达。丰富的氨肽酶N的存在赋予人真皮成纤维细胞酶学特性，而这些特性迄今为止在很大程度上尚未被探索，这表明氨肽酶N的细胞分布比最初认为的更广泛。
