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Characterization of estrogen receptor in human gastric cancer
Author(s) -
Matsui Michinori,
Kojima Osamu,
Uehara Yasuo,
Takahashi Toshio
Publication year - 1991
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(19910715)68:2<305::aid-cncr2820680216>3.0.co;2-a
Subject(s) - cytosol , estrogen receptor , estrogen , centrifugation , receptor , endocrinology , medicine , cancer , chemistry , biochemistry , biology , breast cancer , enzyme
Estrogen receptors (ER) were examined in cytosol, nuclear potassium chloride (KCl) extractable fraction, and nuclear KCl unextractable fraction by the dextran‐coated charcoal adsorption method in various gastric cancer tissue. The overall ER‐positive rate in the cytosol and nuclear fraction was 19.2%. The maximum binding site (Bmax) was 36.0 to 175.0 fmol/mg of protein, and the dissociation constant (Kd) was 0.6 to 1.6 × 10 ‐9 in cytosol fraction. In the nuclear fraction, Bmax was 7.5 fmol/mg of DNA and Kd was 2.3 × 10 ‐9 . Estrogen receptors were characterized in cytosol protein. In cytosol, the estrogen (E 2 )‐ER complex was sedimented at approximately the 5S and 8S regions by 5% to 20% linear sucrose gradient centrifugation. A steroid specificity study of ER showed the presence of an E 2 ‐specific binder in gastric cancer tissue. In conclusion, these results that gastric cancer tissue has E 2 binding sites with the same biochemical characteristics as in breast cancer and endometrial cancer strongly suggest the hormonal dependency of gastric cancer.