Winrow V R, Mojdehi G M, Ryder S D, Rhodes J M, Blake D R, Rampton D S
Bone and Joint Research Unit, London Hospital Medical College, UK.
Dig Dis Sci. 1993 Nov;38(11):1994-2000. doi: 10.1007/BF01297075.
Stress (heat shock) proteins are ubiquitous intracellular proteins that can be induced in vitro by physiological stress events that occur during inflammation. We have used an indirect immunoperoxidase method to locate 60-kDa stress proteins in biopsies taken from normal and inflamed colorectal mucosa. An anti-60-kDa monoclonal antibody (ML30) produced specific staining of surface epithelial cells localized to the site of the Golgi apparatus. In ulcerative colitis, there was an increased concentration of this stress protein compared with controls (P < or = 0.002) and also with a small group of active Crohn's colitis (P < or = 0.01), but no relationship between its concentration and disease activity. All biopsies also showed staining of goblet cells by ML30, suggesting a possible cross-reaction with mucin; electroblotting of crude but not purified mucin showed a faint 60-kDa band with ML30. We conclude that the 60-kDa stress protein is present in normal colorectal epithelial cells and is markedly induced in vivo in ulcerative colitis. Further, we suggest that since the 60-kDa protein functions as a molecular chaperone, it may associate with colonic mucin aiding in its synthesis and/or secretion.
应激（热休克）蛋白是普遍存在的细胞内蛋白质，可在体外由炎症期间发生的生理应激事件诱导产生。我们采用间接免疫过氧化物酶法，在取自正常和发炎的结直肠黏膜的活检组织中定位60 kDa应激蛋白。一种抗60 kDa单克隆抗体（ML30）对定位于高尔基体部位的表面上皮细胞产生特异性染色。在溃疡性结肠炎中，与对照组相比（P≤0.002）以及与一小群活动性克罗恩结肠炎患者相比（P≤0.01），这种应激蛋白的浓度有所增加，但其浓度与疾病活动度之间无关联。所有活检组织的杯状细胞也显示出ML30染色，提示可能与粘蛋白发生交叉反应；粗制而非纯化的粘蛋白的电印迹显示与ML30有一条 faint 60 kDa条带。我们得出结论，60 kDa应激蛋白存在于正常结直肠上皮细胞中，并在溃疡性结肠炎中在体内显著诱导产生。此外，我们认为，由于60 kDa蛋白作为分子伴侣发挥作用，它可能与结肠粘蛋白结合，有助于其合成和/或分泌。
