@article{oai:niigata-u.repo.nii.ac.jp:00023628,
 author = {藍沢, 喜久雄},
 issue = {1},
 journal = {新潟医学会雑誌, 新潟医学会雑誌},
 month = {Jan},
 note = {Characteristics of heat-stable alkaline phosphatase (HSAP) in human gastric cancers were studied on various aspects by using their cultured cells. HSAP was identified in 3 (MKN 1, MKN7 and SCH) out of 9 gastric cancer cell lines. Cytochemical, biochemical and eiectrophoretic examinations on enzyme revealed that MKN 1 and MKN7 cell lines had Regan isoenzyme, while SCH cell line had Nagao isoenzyme. Although the strongest activity of HSAP was observed on the plasma membrane ultrastructurally., considerable activities were detected in the intracellular organelles such as endoplasmic reticulum and Golgi apparatus. These findings indicate a biosynthetic route of HSAP. The HSAP activities of 3 cell lines increased progressively during the logarithmic to the early plateau phase. This datum suggests that the production of HSAP is related to cellular differentiation and maturation. The HSAP activities of MKN 1 and MKN 7 cell lines were accelerated by hydrocortisone, while they were markedly suppressed by retinoic acid. The HSAP activity of SCH cell line was accelerated by sodium butyrate and N^6, O^2’-dibutyryl adenosme 3', 5' -cyclic monophosphate, but it was not influenced by either hydrocortisone or retinoic acid. These data suggest that the regulatory mechanism of enzyme biosynthesis is different between Regan and Nagao isoenzymes. These 3 cell lines, which continuously produce high levels of HSAP, will be helpful for the development of radioimmunoassay and the evaluation of immunotherapy. Furthermore, they are expected to give us valuable informations regarding the mechanism of carcinogenesis.},
 pages = {8--24},
 title = {ヒト胃癌培養細胞の耐熱性アルカリホスファターゼ活性},
 volume = {102},
 year = {1988}
}