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Placental Alkaline Phosphatase‐like Isoenzymes Produced by Human Gastric Cancer Cells
Author(s) -
Aizawa Kikuo,
Motoyama Teiichi,
Watanabe Hidenobu
Publication year - 1989
Publication title -
acta patholigica japonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
ISSN - 0001-6632
DOI - 10.1111/j.1440-1827.1989.tb02409.x
Subject(s) - alkaline phosphatase , placental alkaline phosphatase , isozyme , pathology , cancer , medicine , chemistry , biology , biochemistry , enzyme
The human gastric cancer cell lines, MKN1 and SCH, were biochemically and biologically characterized according to the monophenotypic expression of placental alkaline phosphatase (PLAP)‐ like enzymes. The MKN1 cell line, derived from adenosquamous carcinoma, showed the same enzyme properties as the Regan isoenzyme, whereas the SCH cell line, derived from primary gastric choriocarcinoma, had properties identical with the Nagao isoenzyme. Regan isoenzyme activity expressed by MKN1 cells was stimulated by glucocorticoid and suppressed by retinoic acid. Both agents had no significant effect on SCH cells. On the other hand, Nagao isoenzyme activity expressed by SCH cells was stimulated by sodium butyrate, which had no stimulatory effect on MKN1 cells. Moreover, the PLAP like activity of MKN1 cells showed no observable relationship to human chorionic gonadotropin (hCG) producibility. Whereas expression of the Nagao isoenzyme by the SCH cell line is presumably a result of functional differentiation in the trophoblastic direction, that of the Regan isoenzyme by the MKN1 cell line is probably not. Perhaps the Regan isoenzyme is related to carcinogenesis. Acta Pathol Jpn 39: 630 637, 1989.

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