Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The University of Michigan endometrial carcinoma cell line UM-EC-1 was derived from a poorly differentiated endometrial adenocarcinoma of a 66-yr-old white female. Cell cultures were started using both tumor explants and a cell suspension obtained from collagenase-treated tumor tissue. The collagenase-derived cell suspension gave rise to monolayer cultures which grew rapidly from the outset. This subline of UM-EC-1 has now been subcultured more than 50 times. Cells derived from the tumor explants grew more slowly initially, but after a lag phase of 5 to 6 wk, this subline also exhibited rapid logarithmic growth and reached the same growth rate as that of the collagenase-treated cells. The explant subline has been subcultured more than 37 times. The doubling time of both sublines is 24 h under optimal growth conditions. The karyotype of both cell cultures is 43, XX, inv(1)(p32q42), -4, +der(8) t(8;12)(p23.1;q22), del(9)(q11), -13, -13, +t(13;13) (p13;p13), del(18)(q), -19, -22, -22, +t(22;22)(p11;p11). The net result of the chromosome losses and rearrangements was monosomy 4, duplication 8p23.1----qter, deletion 9q11----9qter, duplication 12q22----qter, deletion 18q, and monosomy 19. The t(13;13) and the t(22;22) were dicentric by C-banding. Virtually all of the chromosome changes were stable in multiple passages except that there was mosaicism for chromosome 13. Some cells contained a single copy of 13 and others had t(13;13). The available evidence indicates the t(13;13) is an isochromosome. UM-EC-1 cells produced tumors histologically similar to the original tumor in male, female, and ovariectomized female athymic mice. UM-EC-1 cells express human class I histocompatibility antigens as assessed by binding of antibodies to nonpolymorphic HLA and beta-2-microglobulin antigens. Blood group antigens A and H were absent although the patient is blood type A and these antigens are normally expressed in endometrial glands. A rearrangement involving the region of chromosome nine that carries the ABH locus may be related to the absence of blood group antigen expression by these cells. The E7 membrane antigen, the locus for which resides on the short arm of chromosome 11, was expressed strongly which is consistent with the presence of two intact copies of chromosome 11 in these cells.
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PMID:UM-EC-1, a new hypodiploid human cell line derived from a poorly differentiated endometrial cancer. 334 65

Peroxidase activity was measured in specimens of human endometrium taken at different days of the menstrual cycle. High specific activities were more frequently found in secretory endometrium than in proliterative tissue, but the variance at each phase of the cycle was large and differences were statistically not significant. The results obtained do not support the hypothesis that peroxidase activity is determined by the levels of circulating estrogens, as is apparently true in rats. Extremely high levels of peroxidase activity were noticed in some, but not all, specimens of endometrial adenocarcinoma. Endometrial glands were separated from the stroma after collagenase digestion of normal and abnormal endometrial glands were separated from the stroma after collagenase digestion of normal and abnormal endometrium, and peroxidase activity was measured in each fraction. The enzyme was found to be preferentially localized in the stroma, in contrast to the reported findings of predominantly epithelial localization in the rat.
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PMID:Peroxidase activity in glands and stroma of human endometrium. 743 24

To elucidate potential mechanisms involved in the increased incidence of endometrial carcinomas in tamoxifen-treated patients, we examined the in-vitro effects of tamoxifen on endometrial cancer cells. The effects of tamoxifen, alone and in combination with oestradiol, on cell proliferation, plasminogen activator (PA) activity, glycogen synthase and phosphorylase activities, p53 protein concentration, and collagenase expression were assessed in two human adenocarcinoma cell lines. These lines were the oestrogen receptor-positive (Ishikawa) cells, representing a well-differentiated endometrial adenocarcinoma, and oestrogen receptor-negative (HEC-1A) cells, derived from a poorly differentiated endometrial adenocarcinoma. Tamoxifen or oestradiol alone and their combination significantly enhanced cellular proliferation of Ishikawa but not of HEC-1A cells. Both lines produced appreciable PA activity, most of which was of the urokinase type. Tamoxifen and oestradiol stimulated this activity in Ishikawa cells but not in HEC-1A cells. The effect of oestradiol was dose-dependent in a linear fashion, while tamoxifen produced a stimulation peaking at 10(-8) M and declining at higher concentrations. Tamoxifen in combination with oestradiol exhibited a synergistic effect on proliferation and on PA activity. The response of PA extended beyond the increase in proliferation, leading to higher specific activity of PA in the tamoxifen-treated cultures. In Ishikawa cells, oestradiol also increased glycogen synthase and glycogen phosphorylase activities, while tamoxifen markedly suppressed these enzymes. Oestradiol, tamoxifen, and their combination had no apparent effect on the expression of protein p53 in Ishikawa cells, or on gelatinase activity in either Ishikawa or HEC-1A cells. The present findings imply that tamoxifen produces oestrogen-agonistic effects on cell proliferation and PA activity, and oestrogen antagonistic effects on glycogen synthase and glycogen phosphorylase activities, but fails to regulate p53 and gelatinase expression. The tamoxifen-responsive systems were only observed in oestrogen-responsive adenocarcinoma cells. Thus, only certain potential oncogenic effects of tamoxifen can be simulated in vitro, and when present, these effects are enhanced in the presence of oestradiol.
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PMID:Tamoxifen exerts oestrogen-agonistic effects on proliferation and plasminogen activation, but not on gelatinase activity, glycogen metabolism and p53 protein expression, in cultures of oestrogen-responsive human endometrial adenocarcinoma cells. 946 46

Lipolysis-stimulated lipoprotein receptor (LSR) is a novel molecule present at tricellular contacts which recruits tricellulin (TRIC), a molecular component of tricellular tight junctions (tTJs). LSR and TRIC are colocalized with the bicellular tight junction (bTJ) protein claudin (CLDN)-1-based tight junction strands at tricellular corners. Knockdown of LSR in normal epithelial cells affects tTJ formation and the epithelial barrier function. In cancer cells knockdown of LSR has been demonstrated to increase cell invasion. However, the detailed mechanisms of how the downregulation of LSR enhances cell invasion in cancer remain unclear. In the present study, knockdown of LSR by small interfering RNA (siRNA) in Sawano human endometrial adenocarcinoma cells induced cell invasion. In LSR-knockdown Sawano cells, upregulation of CLDN-1 protein, which contributes to the cell invasion via matrix metalloproteinases (MMPs), was observed compared with the control group by western blotting and immunostaining. Knockdown of LSR significantly induced Sp1 transcription factor activity in the CLDN-1 promoter region. In LSR-knockdown Sawano cells, DNA microarray analysis demonstrated that MMP-1, MMP-2 and MMP-10 mRNA levels were increased, and the protein levels of membrane-type 1-MMP, MMP-2, MMP-9 and MMP-10 were shown to be increased on western blots. Knockdown of CLDN-1 with siRNA prevented the upregulation of cell invasion induced by the knockdown of LSR in Sawano cells. On the invasive front of human endometrial carcinoma tissue samples, a decrease in LSR and increase in CLDN-1 protein levels were observed using immunohistochemical methods. In conclusion, the results indicate that the downregulation of LSR promotes cell invasion of human endometrial cancer via CLDN-1 mediation of MMPs. This mechanism is important for studying the association of tTJs with the cellular invasion of cancer.
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PMID:Downregulation of lipolysis-stimulated lipoprotein receptor promotes cell invasion via claudin-1-mediated matrix metalloproteinases in human endometrial cancer. 2915 17