Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0684249 (lung carcinoma)
 23,830 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In vitro and in vivo metastatic variants derived from Lewis lung carcinoma (3LL) were examined for the level of the expression of several growth-regulated genes, oncogenes, and transforming growth factor (TGF) genes. To determine whether the proliferative advantage of metastatic cells is due to an increased growth fraction of the cell population or to a deregulated expression of some growth-regulated genes, the mRNA levels of the S-phase-specific H3 histone gene were compared with that of some cell cycle-related genes (vimentin, calcyclin, c-myc, and p53) and oncogenes (Ki-ras, Ha-ras, c-sis, c-src, c-fes, and c-erb). In addition, to evaluate whether an autocrine pattern of cell proliferation is responsible for the proliferative advantage of metastatic cells, the level of the expression of TGF genes (alpha and beta 1) was studied. Northern blot analysis demonstrated that in 3LL metastatic variants the expression of TGF-alpha as well as the expression of all growth-regulated genes and oncogenes studied are similar. Only the TGF-beta 1 gene is expressed at higher levels in highly metastatic 3LL variants maintained either in vitro or in vivo. Data suggest that the proliferative advantage of 3LL metastatic cells is not due to a deregulated expression of some growth-regulated genes and oncogenes, but more likely is acquired through the expression of genes which might interfere with the ability of the tumor cells to escape hostile microenvironmental conditions.
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PMID:Differential expression of transforming growth factor-beta 1 gene in 3LL metastatic variants. 191 69

The heparan sulfate proteoglycan/heparin-binding proteins of the human lung carcinoma cell line LX-1 have been identified, partially purified, and characterized. Analysis of the binding of [3H]heparin to membranes isolated from LX-1 cells indicated the presence of two classes of binding sites, with Kd values of approximately 2 x 10(-10) and 4 x 10(-8) M and corresponding Bmax values of 1 x 10(5) and 2 x 10(7) binding sites/cell. Binding was also observed with isolated heparan sulfate chains and with intact heparan sulfate proteoglycan isolated from two different cell types. With each ligand, binding was inhibited by addition of unlabeled heparin. The binding proteins were extracted from LX-1 cell membranes in detergent solution, and two size classes of binding proteins were identified by overlaying transblots of electrophoretically separated proteins with radioactive ligands. These two classes of binding proteins were shown to contain doublets with estimated molecular masses of approximately 16 kDa (HSBP1A and HSBP1B) and approximately 32 kDa (HSBP2A and HSBP2B). The proteins were partially purified by heparin-Sepharose chromatography and shown to bind heparin and heparan sulfate proteoglycan. By amino acid composition, N-terminal amino acid sequence, and reactivity with antibody, HSBP1A was shown to be very similar to histone 2B; HSBP1B may also be related to histone 2A. HSBP2A and HSBP2B, however, did not react with antibodies to the major histones and had compositions different from one another and from HSBP1.
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PMID:Identification and characterization of heparan sulfate-binding proteins from human lung carcinoma cells. 224 53

Immunochemical methods were used to examine the effect of viral infection on the dynamics of intracellular ubiquitin pools. Infection of either the human lung carcinoma line A-549 or the mouse fibroblast line L929 with encephalomyocarditis virus had little effect on either the distribution or fractional level of intracellular ubiquitin conjugates. In contrast, viral infection resulted in a significant decline in the steady state content of the mono-ubiquitin conjugate to histone 2A (uH2A). Prior treatment with interferons protected against this decrease of uH2A. Furthermore, interferons induced the de novo synthesis of a 15-kDa protein immunologically related to ubiquitin. The ubiquitin cross-reactive protein (UCRP) was not constitutively present in control cells but was significantly induced in various cells sensitive to the biological effects of interferons. Induction of UCRP with respect to both time and interferon concentration dependence closely paralleled the appearance of resistance to viral infection and could be blocked by low levels of actinomycin D. Subsequent studies demonstrated that UCRP was identical to an interferon-induced 15-kDa protein whose sequence has recently been reported (Blomstrom, D. C., Fahey, D., Kutny, R., Korant, B. D., and Knight, E. (1986) J. Biol. Chem. 261, 8811-8816). An authentic sample of the 15-kDa protein was found to co-migrate with UCRP and to cross-react with two different anti-ubiquitin antibodies. Using the authentic 15-kDa protein as a standard, UCRP accumulated to 6.2 +/- 0.5 pmol/10(6) cells and 34 +/- 2 pmol/10(6) cells in interferon-treated A-549 and L929 cultures, respectively. Comparison of the primary sequence of the 15-kDa protein to that of ubiquitin indicated that the former is composed of two domains, each of which bears striking homology to ubiquitin. These observations suggest that the 15-kDa protein may represent one example of a functionally distinct family of ubiquitin-like proteins.
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PMID:Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin. 244 Aug 90

H1 histones were purified by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis from human lung carcinoma (line DMS79), human hepatoblastoma (HepG2), human adult lung and human adult and fetal liver. The purified human H1 histones were analyzed for their amino acid composition and terminal residues. The comparative analysis of the amino acid compositions of the different human H1 histones showed that: all the H1 preparations have the characteristically high lysine content associated with a low arginine content, which distinguishes outer histones from core histones; H1 is distinguishable from other H1 histones by the presence of methionine and histidine; H1 histones from human adult, fetal and cancer cells are very similar in amino acid composition, and in cancer cells the level of the H1 histone is not inversely related with cell growth rate nor with the expression of the alpha-fetoprotein gene.
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PMID:H1(0) histones of normal and cancer human cells. Amino acid composition of H1 purified by polyacrylamide gel electrophoresis. 302 19

The organization and expression of human histone genes were examined in W138 normal human diploid fibroblasts, SV40 transformed W138 cells, A549 epithelial lung carcinoma cells, two adeno-carcinoma cell lines (LOVO and HT29) and three leukemia cell lines (HL60, KG1 and K562). Analysis of the restriction enzyme digests of total genomic DNAs by hybridization with a series of cloned human histone sequences indicated polymorphic organization of at least a subset of the moderately reiterated human histone genes in these cells. Quantitative and qualitative differences were also observed in the representation of histone mRNAs by Northern blot analysis using cloned human histone genes as hybridization probes. However, there was no apparent correlation between variations in the representation of transcripts from various copies of the histone genes, variations in histone gene organization, and the extent of tumor progression.
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PMID:Variations in the organization and expression of human histone genes in normal diploid and tumor cell lines. 620 Nov 32

The influence of delta 9-tetrahydrocannabinol (delta 9-THC) on the cellular levels of histone mRNAs and ribosomal RNAs was examined in several normal and transformed human cell lines--HeLa S3 cells, WI-38 human diploid fibroblasts, SV40-transformed WI-38 cells, and A549 lung carcinoma cells. RNA sequences were quantitatively assayed by electrophoretic fractionation, transfer to nitrocellulose, and hybridization with cloned genomic human histone or ribosomal DNA sequences. Treatment with delta 9-THC (10-40 microM) for 10 hr resulted in a concentration-dependent decrease in the representation of H2A, H2B, H3 and H4 histone mRNAs without a significant inhibitory effect on the levels of ribosomal RNAs. The cannabinoid-mediated inhibitory effect on histone gene expression was less evident in cells with active drug-metabolizing systems.
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PMID:Influence of delta 9-tetrahydrocannabinol on expression of histone and ribosomal genes in normal and transformed human cells. 632 10

Histones prepared from human lung and human lung carcinoma were analyzed by a 2-dimensional electrophoresis method able to separate histone subfractions. The comparative analysis of electrophoretograms showed differences in the relative amounts of H1, H2A, and H3 histone subfractions extracted from human lung and human lung carcinoma chromatin.
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PMID:Histones of human lung carcinoma and human lung tissue. Analysis by two-dimensional electrophoresis. 725 76

In this report the effects of single doses of ionizing radiation on the mRNA expression of several proteins involved in multiple drug resistance were analyzed. Murine NIH 3T3 cells treated with single doses of 5, 10 and 20 Gy during the time interval from 1.5 to 72 h after irradiation were compared with their corresponding controls at the same points of time. The glutathione S-transferase-pi (GST pi) level was elevated in cells treated with 10 or 20 Gy from 24 to 72 h after irradiation compared with the control. Topoisomerase II alpha and thymidylate synthase were decreased in irradiated cells 24-72 h after exposure. These down-regulations were associated with cellular proliferation, determined by mRNA expression of the proliferation marker histone 3. Irradiated cells exhibited no alteration in the P-glycoprotein or glutathione peroxidase mRNA content. The finding that GST pi mRNA was overexpressed after irradiation was validated by investigations on a human lung carcinoma cell line (LXF 289) on the mRNA and protein level. Thus, our results indicate that irradiation alters the expression of proteins involved in multidrug resistance and may, therefore, play a role in clinical drug response.
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PMID:Effects of single doses of irradiation on the expression of resistance-related proteins in murine NIH 3T3 and human lung carcinoma cells. 755 53

Cationic lipids can deliver genes efficiently in vitro, but are generally inhibited by the presence of serum, and their efficiency in vivo is much lower than in vitro. An attractive strategy is to induce strong DNA compaction by its association with proteins, before addition of lipids. However the use of whole proteins might present both production and immunological limitations. We have devised a system in which DNA is associated with short peptides derived from human histone or protamine, before the addition of a cationic lipid or polymer. Peptides strongly associating with DNA confer to such peptide-DNA-lipid particles an enhanced in vitro transfection efficiency over that observed with classical DNA/lipid lipoplexes, and particularly confer the capacity to transfect in the presence of serum. This acquisition of serum resistance is cell type-independent, and observed with all four lipopolyamines tested and polyethylenimine. Precompacting DNA with a histone H1-derived peptide enhances cationic lipid RPR 115335-mediated gene transfer in an in vivo model of Lewis lung carcinoma. Apart from their use in peptide-DNA-lipid association, such peptides could be useful as part of chimeric gene delivery vectors presenting a DNA-binding moiety that can be easily associated with other functional domains.
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PMID:Synthetic DNA-compacting peptides derived from human sequence enhance cationic lipid-mediated gene transfer in vitro and in vivo. 1043 13

Low oxygen tension influences tumor progression by enhancing angiogenesis; and histone deacetylases (HDAC) are implicated in alteration of chromatin assembly and tumorigenesis. Here we show induction of HDAC under hypoxia and elucidate a role for HDAC in the regulation of hypoxia-induced angiogenesis. Overexpressed wild-type HDAC1 downregulated expression of p53 and von Hippel-Lindau tumor suppressor genes and stimulated angiogenesis of human endothelial cells. A specific HDAC inhibitor, trichostatin A (TSA), upregulated p53 and von Hippel-Lindau expression and downregulated hypoxia-inducible factor-1alpha and vascular endothelial growth factor. TSA also blocked angiogenesis in vitro and in vivo. TSA specifically inhibited hypoxia-induced angiogenesis in the Lewis lung carcinoma model. These results indicate that hypoxia enhances HDAC function and that HDAC is closely involved in angiogenesis through suppression of hypoxia-responsive tumor suppressor genes.
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PMID:Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. 1128 70


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