Preservation of progesterone receptors of human endometrium.
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Biomedical subjects
Publications and source records attributed to K D Hammond.
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The activities of pyruvate carboxylase (PC), phosphoenolpyruvate carboxykinase (PEPCK), glucose-6-phosphatase (G6Pase), and glycogen synthetase (GS) were determined in the cancerous and in the apparently uninvolved (host) regions of livers from primary hepatoma patients as well as in normal adult human livers and human fetal livers. The activities of these enzymes were also assayed in a fairly fast-growing, 3'-methyl-4-dimethylaminoazobenzene-induced transplantable rat hepatoma and in hepatoma cell lines derived from both rat and human tumors. In the human hepatoma, as in the rat hepatoma, the activities of PC, PEPCK, and G6Pase were considerably reduced, compared to those in the host liver. The activities of both the a (glucose 6-phosphate-independent) and b (glucose 6-phosphate-dependent) forms of GS were also lower in human and rat hepatomas than in the respective host livers. Activities of PC, PEPCK, and G6Pase in the human hepatomas were often comparable with those of fetal livers. In rat and human hepatoma cells, the activities of PC, PEPCK, and G6Pase were similar to or lower than the activities in the respective hepatomas; the activities of GS a were also similar to those in the hepatoma, whereas the activities of GS b were somewhat higher.
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The binding of oestradiol in human placental tissue obtained from spontaneous and caesarean deliveries was investigated. Villous tissue was homogenized and the 800 g 'cytosol' supernatant treated with ammonium sulphate. The precipitate was redissolved and the preparation then equilibrated with [3H]oestradiol. After separation of bound and free steroid with dextran coated charcoal, receptor binding site concentrations and dissociation constants were determined. The presence of high-affinity, saturable binding was clearly demonstrated. Mean values (+/- s.d.) for receptor binding site concentrations were 64.6 +/- 22.9 (n = 6) and 33.8 +/- 32.9 (n = 8) fmol/mg protein for spontaneous and caesarean deliveries, respectively; respective dissociation constants were 16.0 +/- 7.6 and 7.0 +/- 6.0 pM. Heat denaturation studies, equilibration time studies and certain of the Scatchard plots suggested that forms of the oestradiol receptor of differing stability may be present in human placental tissue.
The activities of phosphoamino acid phosphatases were measured in human myometrium and fibroma and normal and cancerous tissues of the cervix and ovary. Phosphoserine and phosphothreonine phosphatases were detected only in myometrium and fibroma and the values were relatively low. Phosphotyrosine phosphatase activities in myometrium and fibroma fell within a similar range; this was also the case for ovary and ovarian carcinoma, whereas values for cervical tumours were significantly higher than for normal cervix. Activities of phosphotyrosine phosphatase in serum from patients with cervical or other tumours were, in most cases, within the range of values obtained for normal serum.
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The different forms of cAMP-dependent, cGMP-dependent and cyclic nucleotide-independent protein kinases were studied in relation to hexamethylene bisacetamide (HMBA)-induced differentiation of murine erythroleukaemic cells, using a nondenaturing polyacrylamide gel electrophoresis system. Several forms of histone-dependent kinases were detected and there was a definite change in the relative proportions of the two major components and of minor components in cells treated with HMBA, as compared with untreated controls. The faster-moving of the two major forms, which increased on HMBA stimulation, appeared to be both cAMP and cGMP dependent; the slower moving form, which decreased with HMBA treatment, showed little dependence on either cAMP or cGMP.