Burkholder P M, Oberley T D, Barber T A, Beacom A, Koehler C
Am J Pathol. 1977 Mar;86(3):635-54.
Several very recent reports have indicated the presence of receptor sites for the third component of complement in human but not other vertebrate renal glomeruli. The present study constitutes a demonstration that the glomerular capillary epithelial cell bears this receptor, detectable with either EAC complexes (EAC1423b) or fluores ceinated zymosan-C3 (ZC3b) complexes, Fresh, unfixed frozen sections of normal or diseased human kidneys, mechanically isolated human glomeruli, dissociated glomerular cells, and glomeruli and golmerular cells maintained in tissue culture were examined with various EAC complexes or ZC3b and examined by phase light microscopy, fluorescence microscopy, or transmission and scanning electron microscopy. Clearly, by scanning electron microscopy it was determined that glomerular capillary epithelial cells bind the immune-adherence EAC indicator cells. Because glomeruli or glomerular epithelial cells did not bind E, EA, EACI, EAC14, or EAC142 but did bind EAC1423b or ZC3b, it is concluded that C3b (activated bound fragment of the third component of complement) is responsible for the immune-adherence reaction in glomeruli. Preliminary examination of diseased renal biopsies indicates that sclerotic glomeruli, focal segmental sclerotic or proliferative glomerular capillary lesions, and proliferative epithelial crescents are immune-adherence negative. Furthermore, a clear or consistent inverse relationship between glomerular capillary deposits of C3 which presumably might block epithelial C3 receptor sites, and immune-adherence reactivity with EAC in vitro was not as evident in this study as reported previously by other investigators. Nevertheless, it is still attractive to conceive that glomerular C3 receptor sites might be responsible for binding of antigen-antibody-complement complexes and formation of immune-complex deposits, at least on the epimembranous (subepithelial) surface of glomerular capillary walls. Inability to demonstrate this immune-adherence phenomenon in glomeruli of other vertebrate animals suggests among other things that more investigation is necessary before ascribing a unique or universal significance to the C3 receptors identified in human glomeruli.
最近的几份报告表明,补体第三成分的受体位点存在于人类而非其他脊椎动物的肾小球中。本研究证实肾小球毛细血管上皮细胞带有这种受体,可用EAC复合物(EAC1423b)或荧光标记的酵母聚糖-C3(ZC3b)复合物检测到。对正常或患病人类肾脏的新鲜、未固定冰冻切片、机械分离的人肾小球、解离的肾小球细胞以及组织培养中维持的肾小球和肾小球细胞,用各种EAC复合物或ZC3b进行检查,并通过相差显微镜、荧光显微镜或透射和扫描电子显微镜观察。显然,通过扫描电子显微镜确定肾小球毛细血管上皮细胞结合免疫黏附EAC指示细胞。由于肾小球或肾小球上皮细胞不结合E、EA、EAC1、EAC14或EAC142,但确实结合EAC1423b或ZC3b,因此得出结论,C3b(补体第三成分的活化结合片段)负责肾小球中的免疫黏附反应。对患病肾活检组织的初步检查表明,硬化性肾小球、局灶节段性硬化或增殖性肾小球毛细血管病变以及增殖性上皮新月体免疫黏附呈阴性。此外,本研究中推测可能会阻断上皮C3受体位点的肾小球毛细血管C3沉积物与体外EAC免疫黏附反应之间的明显或一致的负相关关系,并不像其他研究者先前报道的那样明显。然而,仍然有吸引力的推测是,肾小球C3受体位点可能负责抗原-抗体-补体复合物的结合以及免疫复合物沉积物的形成,至少在肾小球毛细血管壁的膜上(上皮下)表面。在其他脊椎动物的肾小球中无法证明这种免疫黏附现象表明,除其他外,在赋予人类肾小球中鉴定出的C3受体独特或普遍意义之前,还需要更多的研究。