Meyer T, Uher T, Ramadori G, Ringe B, Schwoerer H
Center for Internal Medicine, University of Goettingen, Germany.
Hepatogastroenterology. 1998 Sep-Oct;45(23):1522-6.
The expression of tryptophan hydroxylase, the rate-limiting enzyme in the biosynthesis of serotonin, is described in a case of a 35 year-old patient with metastatic jejunal carcinoid. Immunohistochemically, monoclonal anti-tryptophan hydroxylase antibodies positively identified liver metastases of a neuroendocrine tumor. The cellular distribution of tryptophan hydroxylase was restricted exclusively to the cytoplasm of carcinoid cells, where it was found in large amounts. By means of immunoblotting, anti-tryptophan hydroxylase antibodies detected in samples from carcinoid tissue two closely migrating polypeptide bands with molecular weights of 26 kDa and 29 kDa, respectively. These two protein bands appear to represent proteolytically degraded polypeptides, since tryptophan hydroxylase is known for its extreme unstability in vitro. In our case, the immunohistochemical and biochemical identification of tryptophan hydroxylase in liver lesions of a neuroendocrine tumor permitted the correct diagnosis of a metastatic carcinoid.
在一例35岁转移性空肠类癌患者中,对血清素生物合成限速酶色氨酸羟化酶的表达进行了描述。免疫组织化学分析显示,单克隆抗色氨酸羟化酶抗体可明确识别神经内分泌肿瘤的肝转移灶。色氨酸羟化酶的细胞分布仅局限于类癌细胞的细胞质中,且含量丰富。通过免疫印迹法,抗色氨酸羟化酶抗体在类癌组织样本中检测到两条紧密迁移的多肽带,分子量分别为26 kDa和29 kDa。这两条蛋白带似乎代表蛋白水解降解的多肽,因为色氨酸羟化酶在体外以极端不稳定著称。在我们的病例中,通过对神经内分泌肿瘤肝病灶进行色氨酸羟化酶的免疫组织化学和生化鉴定,得以正确诊断转移性类癌。