Taniguchi N, Yokosawa N, Narita M, Mitsuyama T, Makita A
J Natl Cancer Inst. 1981 Sep;67(3):577-83.
The activities of the two enzymes (UDP-acetylgalactosamine-globoside alpha-N-acetylgalactosaminyltransferase and alpha-N-acetyl-D-galactosaminidase) involved in the synthesis and degradation of Forssman antigen were studied in uninvolved and neoplastic human lungs. The Forssman synthetic enzyme activities of 17 of 18 squamous cell carcinomas were higher than those of the uninvolved lung tissues of the subjects studied, and the degradation enzyme activities of 16 of 18 squamous cell carcinomas were higher than those of the uninvolved portions. No consistent abnormalities in both enzyme activities were seen in 28 adenocarcinomas, whereas the mean activities of the two enzymes were elevated in these neoplasms. These differences in enzyme activities between those samples may indicate that the synthesis and degradation of Forssman antigen in adenocarcinoma of the lung are expressed or repressed according to the individual, whereas in squamous cell carcinoma, these activities are expressed unrelated to the individual.
对参与福斯曼抗原合成与降解的两种酶(UDP - 乙酰半乳糖胺 - 球蛋白α - N - 乙酰半乳糖胺基转移酶和α - N - 乙酰 - D - 半乳糖苷酶)在未受累及肿瘤性人肺组织中的活性进行了研究。18例鳞状细胞癌中有17例的福斯曼合成酶活性高于所研究对象的未受累肺组织,18例鳞状细胞癌中有16例的降解酶活性高于未受累部分。28例腺癌中未观察到两种酶活性的一致异常,而在这些肿瘤中两种酶的平均活性升高。这些样本之间酶活性的差异可能表明,肺腺癌中福斯曼抗原的合成与降解是根据个体情况表达或受抑制的,而在鳞状细胞癌中,这些活性的表达与个体无关。