Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0007097 (carcinoma)
 152,788 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The antigen common for continuous epithelial cell lines and gastric mucosa of humans described earlier was studied. This antigen was revealed in one more cell line, namely in that prepared from human mammary carcinoma MDA-MB-231, noncontaminated with HeLa cells. The antigen described can be detected in the exophytely growing adenocarcinomas of the stomach and in the mucosa of the carcinoma affected stomach at a distance of 10--12 cm from the site of affection; no such antigen was revealed in the endophytely growing carcinoma of the stomach and in mucosa areas surrounding gastric ulcer. The antigen is not a glycoprotein since glycoprotein fractions obtained by means of 1.2 M perchloric acid from the normal stomach mucosa homogenate and the E 16b extract were inactive in immunodiffusion with a sensitive serum. The electrophoretic mobility of the antigen was similar to that of globulin alpha1-beta2. This antigen is of interest since its detection or absence would possibly aid in determination of the initial type of cells from which development of carcinoma occurred, and in more precise recognition of the histological form of carcinoma of the stomach.
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PMID:[Study of the "continuous cell antigen" and the human gastric mucosa]. 10 92

Human serum from a pool of normal donors, in the presence of fetal bovine serum, inhibited the growth of the major epithelial cell type observed in primary cultures established from biopsy samples of breast carcinoma. In contrast, the growth of cells from nonmalignant mammary tissues removed during reduction mammoplasty and from fibroadenoma was not inhibited. The replication of MCF-7 cells, an established line from a metastatic breast lesion, was also inhibited, whereas the growth of HBL-100 cells, originally derived from a presumably normal source of mammary tissue, was not inhibited by human serum in combination with fetal bovine serum. The growth of two additional cell lines, MDA 157 and MDA 231, was also not affected by human serum. Studies of growth in primary cultures were restricted primarily to direct microscopic observations of the number of cells per colony and the proportion labeled with [3H]thymidine. The results indicate the use of cell lines as adjuncts to primary cultures in future studies of this inhibitory activity.
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PMID:Human serum and the growth of human mammary cells. 22 2

Glycosaminoglycans have been characterized from a normal human breast cell line (HBL-100) and two different cell lines from human breast carcinoma (MDA-MB-231 and MCF-7). The glycosaminoglycans were labeled by exposure of cell cultures to [3H]glucosamine and [35S]sulfate and then isolated from both spent media and cells by pronase digestion and cetylpyridinium chloride fractionation. They were further characterized by (a) hexosamine composition, (b) controlled-pore glass exclusion chromatography, (c) reactivity with specific enzymes (hyaluronidase chondroitinase, heparitinase, and heparinase), (d) nitrous acid degradation, and (e) DEAD-Sephadex chromatography. The results indicate that the HBL-100 line synthesizes mainly hyaluronic acid, most of which is secreted into the medium. Chondroitin sulfate and heparan sulfate are the predominant glycosaminoglycans synthesized by the cancer lines; both are found mainly in the spent medium, but the hyaluronic acid synthesized by the MDA-MB-231 line remains cell associated. The cell-associated heparan sulfate had a molecular weight in excess of 13,000 and may contain linkages susceptible to testicular hyaluronidase. The MCF-7 cells produce significantly lower amounts of glycosaminoglycans than do the other two lines.
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PMID:Glycosaminoglycans of normal and malignant cultured human mammary cells. 42 76

Seventeen recently established human breast carcinoma cell lines of metastatic origin (MDA series), HeLa cells, and MCF-7 (a well-established breast carcinoma cell line) were studied by starch gel electrophoresis for allozymic differences at 17 enzyme loci. Ten loci proved to be informative in establishing unique genetic signatures for all of the lines with the exception of MDA-134 and -309, which had the same genetic signatures. The probability of these latter two lines being of independent origin and finding their similar genetic signatures by chance is 0.07. These studies enable us to conclude that the chromosomal marker shown to be common to these breast carcinoma cell lines of metastatic origin is not present because of cross-contamination of the lines with other long-term lines or each other.
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PMID:Mutually exclusive genetic signatures of human breast tumor cell lines with a common chromosomal marker. 42 79

Nineteen human breast carcinoma cell lines have been established as continuous cultures during the past 6 years in our laboratory. This preliminary report is designed to list the lines by their designated code numbers (MDA-MB) and present a brief summary of their morphological, cytogenetic and biochemical characteristics. Sixteen of our lines were obtained from pleural effusions, two from brain metastases, and one from pericardial fluid. All lines have been shown to be distinct entities and are uncontaminated by HeLa cells or each other. A lq marker chromosome is present in all but one of the lines examined.
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PMID:Long-term human breast carcinoma cell lines of metastatic origin: preliminary characterization. 73 Feb 2

The effect of the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) and the cytokines interleukin-1 (IL-1) and tumor necrosis factor-alpha (TNF-alpha) on matrix metalloproteinases (MMP) and metalloproteinase inhibitors was studied in a variety of human cell lines. Expression of the mammalian collagenase (MMP-1), 72-kD gelatinase/type IV collagenase (MMP-2), stromelysin (MMP-3), 92-kD gelatinase/type IV collagenase (MMP-9), and tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) was assessed by zymography and Northern blot analysis. MMP-2 and TIMP-2 activities were refractory to TPA, IL-1 and TNF-alpha treatment in most of the cell lines. In contrast, MMP-3, MMP-9 and TIMP-1 activities were markedly stimulated by TPA in most of the tumor cell lines and human umbilical vein endothelial cells (HUVEC), whereas the fibroblast lines were minimally stimulated or unresponsive to TPA. The MMP-3, MMP-9 and TIMP-1 stimulation in response to IL-1 and TNF-alpha treatment was detected in some of the tumor cell lines and HUVEC. The increase in activity was less marked than in TPA. A breast carcinoma cell line, MDA-MB-231, which did not express MMP-2, had high expression of MMP-3 and MMP-9 which were unaffected by TPA and cytokine treatment. Northern blot analysis of MMP and TIMP mRNA expression reflected the zymogram findings for most of the cell lines. TPA-mediated stimulation of MMP-1 was similar to that of MMP-3 and MMP-9. Exceptions were the fibroblast cell lines which showed either a much more marked mRNA response of MMP-9 to TPA than observed at protein level, or a high constitutive MMP-9 mRNA when MMP-9 activity was not detectable by zymography. TPA-mediated stimulation of MMP-9 and TIMP-1 activity was blocked by staurosporine, an inhibitor of protein kinase C (PKC). A non-PKC-activating phorbol ester, 4 alpha-phorbol-12,13-didecanoate, did not stimulate MMP-9 and TIMP-1 activity. TPA treatment caused the increased expression of c-fos containing AP-1-specific binding activity in selected tumor cell lines. This activity was maximal at 6 h. An association was observed between AP-1 binding activity and increased expression of MMP-1, MMP-3 and MMP-9, which possess TPA-responsive elements (TRE). TPA-sensitive MMPs and TIMP-1 were variably stimulated by biologically relevant cytokines, such as IL-1 and TNF-alpha.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Effect of phorbol ester and cytokines on matrix metalloproteinase and tissue inhibitor of metalloproteinase expression in tumor and normal cell lines. 128 26

The aim of this study was to investigate the presence of lactotransferrin receptor on breast non-malignant SV-40 immortalized cells (HBL100 and NB54T), benign mastopathy immortalized cells (NPM14T and NPM21T1), hst oncogene transformed HBL100 cell line (tumorigenic HH9 cells) and breast carcinoma cells (T47D, MCF7, VHB1, BT20 and MDA-MB 231). Flow cytometry analyses of the reversible binding of lactotransferrin labeled on its glycan moiety with fluorescein indicate, for the first time, that all these epithelial breast cell lines, express a specific lactotransferrin receptor. The binding parameters of [125I]-lactotransferrin to non-malignant cells, hst oncogene transformed cells and benign mastopathy cells are of the same order of magnitude as those determined for activated lymphocytes and for cancerous breast cell lines, except for MDA-MB 231 cells. MDA-MB 231 cells bind lactotransferrin with the lowest affinity and, in contrast to other analyzed breast cells, are not recognized by antibodies directed against lymphocyte lactotransferrin receptor. These results suggest that MDA-MB 231 lactotransferrin receptor is different from that characterized at the cell surface of other breast cells. In conclusion, since the lactotransferrin receptor expression was not enhanced at the surface of cancerous cell lines and was not altered by the oncogene transformation of a normal cell (HBL100) to a tumorigenic cell (HH9), the lactotransferrin receptor cannot be considered as a marker of tumor progression.
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PMID:Characterization of lactotransferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas. 133 74

We analyzed the expression of plasma glutathione peroxidase (GSHPx-P) messenger RNA (mRNA) in mouse, rat, and human tissues, using a human GSHPx-P cDNA clone as the probe. Unlike the classical cellular glutathione peroxidase (GSHPx-1), GSHPx-P expression appears to be tissue-specific. In the mouse and rat, kidney expresses an mRNA at a high level detected with the human probe. A signal is also detected in mRNA isolated from mouse and rat heart, rat cardiac myocytes, mouse lung, epididymis, and the mammary gland of midpregnant mice. No signal is detected in mRNA isolated from mouse and rat liver, mouse brain, uterus, and testis. In human tissues, an mRNA hybridizing to GSHPx-P cDNA is present in liver, as well as kidney, heart, lung, breast, and placenta. We have shown that human kidney expresses a GSHPx-P mRNA, and not a GSHPx-P-like message, by isolating a cDNA clone from a human kidney library in lambda gt11. From the 412-nucleotide partial sequence of the kidney cDNA, which codes for the 40-170 amino acids of GSHPx-P including the TGA codon for selenocysteine, we found complete sequence identity of the kidney cDNA with GSHPx-P isolated from placenta. The expression of GSHPx-P mRNA in cell lines was also studied. There is some correlation of the expression of GSHPx-P in these cell lines with that in normal tissues. Cell lines that expressed GSHPx-P mRNA or protein included the human hepatocarcinoma HepG2, Hep3B cells, human kidney carcinoma A498 cells, and the human breast cancer SK-BR-3, T47D, MDA-MB-231, and AdrrMCF-7 cells. Cell lines that did not express GSHPx-P included human choriocarcinoma BeWo cells, human breast cancer MCF-7, ZR-75-1, and Hs578T cells, and mouse hepatoma Hepa-1 cells.
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PMID:Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. 133

The FLG/FGFRI gene, encoding a receptor for members of the FGF family, is located at 8p11.2-p12. It is amplified, overexpressed, and not grossly rearranged in the MDA-MB-134 breast carcinoma cell line, whereas other genes from the pericentromeric 8p region are not amplified. The FGF4/HSTFI gene, located at 11q13, is also amplified with a substantial portion of the 11q13 region, but is not overexpressed in MDA-MB-134 cells. In this cell line, amplified sequences constitute a large homogeneously staining region (HSR) which is part of a marker chromosome containing chromosome 8 and chromosome 11 sequences. Using probes for the FGF4/HSTFI and the FLG/FGFRI genes in fluorescence chromosomal in situ hybridization, we show that the HSR contains de novo fused and amplified 11q13 and 8p11-p12 sequences associated in a complex structure containing approximately the same number of FGF4 and FGFRI genes. The significance of this genetic abnormality for MDA-MB-134 cells, and for breast carcinogenesis in general, is unknown, but may underlie a particular type of oncogene activation.
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PMID:Fusion and amplification of two originally non-syntenic chromosomal regions in a mammary carcinoma cell line. 138 61

The goal of this study was to investigate the heat sensitivity of the microcirculation in normal C3H murine leg muscle and a variety of transplanted tumour lines (KHT, SCC-VII, RIF-1, C3H mouse mammary carcinoma, two human mammary carcinomas MDA-468 and S5). Clearance rate of a radioactive tracer monitored following an intra-tissue injection was used as a measurement of microvascular integrity during heat treatment. Clearance rate in all tumours studied was significantly lower after 1 h of heating at 44 degrees C than the initial pretreatment clearance rate. Response of normal muscle differed from that of tumours in that the clearance rate after 1 h of heating at 44 degrees C was similar to the initial clearance rate. Vasculature in the KHT fibrosarcoma was more sensitive to heat treatment than that in other tumours. In response to a heat treatment at 43, 44, 45 and 46 degrees C the same level of microvascular damage occurred in half the time in KHT fibrosarcoma than in normal muscle. Furthermore, vascular damage in both muscle and KHT tumour followed the same relative isoeffect relationship, a 1 degree C change in temperature was equivalent to a change in heating time by a factor of two.
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PMID:Differential thermal sensitivity of tumour and normal tissue microvascular response during hyperthermia. 140 30


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