Campbell B J, Finnie I A, Hounsell E F, Rhodes J M
Department of Medicine, University of Liverpool, United Kingdom.
J Clin Invest. 1995 Feb;95(2):571-6. doi: 10.1172/JCI117700.
Increased binding of the lectin peanut agglutinin is a common feature in epithelial malignancy and hyperplasia. This may have considerable functional importance in the intestine by allowing interaction between the epithelium and mitogenic lectins of dietary or microbial origin. Peanut agglutinin binds the disaccharide Thomsen-Friedenreich (TF, T or core 1) blood group antigen, Gal beta (1-3) GalNAc alpha-, but is not totally specific for this site. Consequently, there has been controversy about the presence of this structure in colon cancer; studies with anti-TF monoclonal antibodies have failed to detect it. We have examined the presence of TF antigen in colonic mucus glycoprotein (mucin) using endo-alpha-N-acetylgalactosaminidase (O-Glycanase), which specifically catalyzes the hydrolysis of TF antigen from glycoconjugates. Samples of adenocarcinoma, inflammatory bowel disease (ulcerative colitis), and normal mucin were treated with O-glycanase, the liberated disaccharide was separated from the glycoprotein and analyzed using dual CarboPac PA-100 column high performance anion-exchange chromatography coupled with pulsed amperometric detection. O-Glycanase treatment released increased amounts of TF antigen from both colonic adenocarcinoma (8.0 +/- 3.9 ng/micrograms protein, n = 11; P < 0.0001 ANOVA) and ulcerative colitis mucin (3.3 +/- 0.3 ng/micrograms protein, n = 5; P = 0.04) compared with mucin samples from histologically normal mucosa distant from carcinoma (1.5 +/- 1.1 ng/micrograms protein, n = 9). However, after mild acid treatment to remove sialic acids and fucose, releasable TF antigen was increased in all nine of these histologically normal mucin samples (5.5 +/- 2.6 ng/micrograms protein, P < 0.0002). We conclude that TF antigen is an oncofetal antigen which is expressed in colon cancer, but is concealed by further glycosylation (sialylation and/or fucosylation) in the normal colonic mucosa.
凝集素花生凝集素结合增加是上皮恶性肿瘤和增生的一个共同特征。这在肠道中可能具有相当重要的功能意义,因为它允许上皮细胞与饮食或微生物来源的促有丝分裂凝集素之间相互作用。花生凝集素结合二糖汤姆森 - 弗里德赖希(TF、T或核心1)血型抗原,即Galβ(1 - 3)GalNAcα - ,但并非完全特异性针对该位点。因此,关于结肠癌中这种结构的存在一直存在争议;使用抗TF单克隆抗体的研究未能检测到它。我们使用内切α - N - 乙酰半乳糖胺酶(O - 聚糖酶)检测了结肠黏液糖蛋白(黏蛋白)中TF抗原的存在,该酶特异性催化从糖缀合物中水解TF抗原。腺癌、炎症性肠病(溃疡性结肠炎)和正常黏蛋白的样本用O - 聚糖酶处理,释放的二糖与糖蛋白分离,并使用双CarboPac PA - 100柱高效阴离子交换色谱结合脉冲安培检测进行分析。与远离癌的组织学正常黏膜的黏蛋白样本(1.5±1.1 ng/μg蛋白质,n = 9)相比,O - 聚糖酶处理从结肠腺癌(8.0±3.9 ng/μg蛋白质,n = 11;P < 0.0001,方差分析)和溃疡性结肠炎黏蛋白(3.3±0.3 ng/μg蛋白质,n = 5;P = 0.04)中释放出更多量的TF抗原。然而,经过温和酸处理以去除唾液酸和岩藻糖后,所有这九个组织学正常的黏蛋白样本中可释放的TF抗原都增加了(5.5±2.6 ng/μg蛋白质,P < 0.0002)。我们得出结论,TF抗原是一种癌胚抗原,在结肠癌中表达,但在正常结肠黏膜中被进一步糖基化(唾液酸化和/或岩藻糖基化)所掩盖。