Burke R E, Harris S C, McGuire W L
Cancer Res. 1978 Sep;38(9):2773-6.
Lactate dehydrogenase activity (LDH) was measured in the MCF-7 human breast cancer cell line derived at the Michigan Cancer Foundation from a patient with metastatic breast adenocarcinoma. LDH was found in the 46,000 X g supernatant of cell lysates, but not in the culture medium. Only the fifth isozyme (LDH-5) could be demonstrated by cellulose acetate electrophoresis and relative heat inactivation studies. When endogenous steroids were removed from the medium, addition of estrogen to the growth medium for several days elevated LDH 2-fold above controls; LDH was not altered when MCF-7 cells were treated with progesterone, hydrocortisone, prolactin, insulin, or triiodothyronine. A physiological concentration (0.1 nM) of 17beta-estradiol was sufficient to produce a maximal LDH increase. There were no qualitative isozyme changes in response to estrogen. LDH activity may therefore be a useful marker protein for studying hormone action in the MCF-7 human breast cancer cell line.
乳酸脱氢酶活性（LDH）在密歇根癌症基金会从一名转移性乳腺腺癌患者身上获取的MCF - 7人乳腺癌细胞系中进行了测定。在细胞裂解物的46,000 X g上清液中发现了LDH，但在培养基中未发现。通过醋酸纤维素电泳和相对热失活研究仅能证实第五种同工酶（LDH - 5）的存在。当从培养基中去除内源性类固醇时，在生长培养基中添加雌激素数天，可使LDH比对照升高2倍；用孕酮、氢化可的松、催乳素、胰岛素或三碘甲状腺原氨酸处理MCF - 7细胞时，LDH没有改变。生理浓度（0.1 nM）的17β - 雌二醇足以使LDH产生最大增加。雌激素处理后同工酶没有定性变化。因此，LDH活性可能是研究MCF - 7人乳腺癌细胞系中激素作用的一种有用的标记蛋白。
