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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
Mol Cell Biochem 1986 Aug
PMID:H1(0) histones of normal and cancer human cells. Amino acid composition of H1 purified by polyacrylamide gel electrophoresis. 302 19

Two-dimensional electrophoretograms of newly synthesized polypeptides from low-metastatic (P29) and high-metastatic (D6) Lewis lung carcinoma cells were compared. The results showed that the synthesis of tropomyosin 2 (TM2) was significantly less in D6 cells than in P29 cells. Furthermore, suppression of TM2 synthesis was induced in P29 cells during incubation in medium containing dimethyl sulfoxide or butyric acid, which induced the metastatic phenotype of P29 cells. These results suggest that the suppression of TM2 synthesis is linked to the metastatic potential of Lewis lung carcinoma cells.
Mol Cell Biol 1988 Sep
PMID:Differential expression of a tropomyosin isoform in low- and high-metastatic Lewis lung carcinoma cells. 322 70

We isolated and characterized a cDNA clone encoding tropomyosin isoform 2 (TM2) from a mouse fibroblast cDNA library. TM2 was found to contain 284 amino acids and was closely related to the rat smooth and skeletal muscle alpha-TMs and the human fibroblast TM3. The amino acid sequence of TM2 showed a nearly complete match with that of human fibroblast TM3 except for the region from amino acids 189 to 213, the sequence of which was identical to those of rat smooth and skeletal muscle alpha-TMs. These results suggest that TM2 is expressed from the same gene that encodes the smooth muscle alpha-TM, the skeletal muscle alpha-TM, and TM3 via an alternative RNA-splicing mechanism. Comparison of the expression of TM2 mRNA in low-metastatic Lewis lung carcinoma P29 cells and high-metastatic D6 cells revealed that it was significantly less in D6 cells than in P29 cells, supporting our previous observations (K. Takenaga, Y. Nakamura, and S. Sakiyama, Mol. Cell. Biol. 8:3934-3937, 1988) at the protein level.
Mol Cell Biol 1988 Dec
PMID:Isolation and characterization of a cDNA that encodes mouse fibroblast tropomyosin isoform 2. 324 65

We studied the expression of the genes encoding the A and B chains of platelet-derived growth factor (PDGF) in a number of human leukemia cell lines. Steady-state expression of the A-chain RNA was seen only in the promonocytic leukemia cell line U937 and in the T-cell leukemia cell line MOLT-4. It has previously been reported that both PDGF A and PDGF B genes are induced during megakaryoblastic differentiation of the K562 erythroleukemia cells and transiently during monocytic differentiation of the promyelocytic leukemia cell line HL-60 and U937 cells. In this study we show that PDGF A RNA expression was induced in HL-60 and Jurkat T-cell leukemia cells and increased in U937 and MOLT-4 cells after a 1- to 2-h stimulation with an 8 pM concentration of transforming growth factor beta (TGF-beta). PDGF A RNA remained at a constant, elevated level for at least 24 h in U937 cells, but returned to undetectable levels within 12 h in HL-60 cells. No PDGF A expression was induced by TGF-beta in K562 cells or in lung carcinoma cells (A549). Interestingly, essentially no PDGF B-chain (c-sis proto-oncogene) RNA was expressed simultaneously with PDGF A. In the presence of TGF-beta and protein synthesis inhibitors, PDGF A RNA was superinduced at least 20-fold in the U937 and HL-60 cells. PDGF A expression was accompanied by secretion of immunoprecipitable PDGF to the culture medium of HL-60 and U937 cells. The phorbol ester tumor promoter tetradecanoyl phorbol acetate also increased PDGF A expression with similar kinetics, but with a mechanism distinct from that of TGF-beta. These results suggest a role for TGF-beta in the differential regulation of expression of the PDGF genes.
Mol Cell Biol 1987 Oct
PMID:Regulation of platelet-derived growth factor gene expression by transforming growth factor beta and phorbol ester in human leukemia cell lines. 347 82

Expression of the calcitonin (CT)/calcitonin gene related peptide (CGRP) gene and the proopiomelanocortin (POMC) gene has been demonstrated by Northern blot hybridization analysis of RNA extracted from human medullary thyroid carcinoma (MTC), pheochromocytoma and lung carcinoma. CT mRNA in these tumors could not be distinguished in size from CT mRNA isolated from normal human thyroid tissue. CGRP mRNA (previously demonstrated in 12 out of 12 lung tumor cell lines investigated) could not be detected in 13 primary lung tumors or 10 metastases thereof. The length of POMC mRNA in MTCs (present in all 4 metastases investigated but not in 7 primary tumors) and pheochromocytomas is about 100 nucleotides more than pituitary POMC RNA. In lung tumors 2 POMC RNA species can be detected, one of the same size as in pituitary tissue and one about 100 nucleotides larger.
Mol Cell Endocrinol 1986 Sep
PMID:Detection of mRNA encoding calcitonin, calcitonin gene related peptide and proopiomelanocortin in human tumors. 348 30

Morphologic transformation of NIH 3T3 mouse cells occurs upon transfection of these cells with large amounts (greater than or equal to 10 micrograms) of recombinant DNA molecules carrying the normal human H-ras-1 proto-oncogene. We provide experimental evidence indicating that transformation of these NIH 3T3 cells results from the combined effect of multiple copies of the H-ras-1 proto-oncogene rather than from spontaneous mutation of one of the transfected H-ras-1 clones (E. Santos, E.P. Reddy, S. Pulciani, R.J. Feldman, and M. Barbacid, Proc. Natl. Acad. Sci. USA 80:4679-4683, 1983). Levels of H-ras-1 RNA and p21 expression are highly elevated in the NIH 3T3 transformants, and in those cases examined, these levels correlate with the malignant properties of these cells. We have also investigated the presence of amplified ras genes in a variety of human carcinomas. In 75 tumor biopsies, we found amplification of the human K-ras-2 locus in one carcinoma of the lung. These results indicate that ras gene amplification is an alternative pathway by which ras genes may participate in the development of human neoplasia.
Mol Cell Biol 1985 Oct
PMID:ras gene Amplification and malignant transformation. 391 35

The various epithelial cells of the lower respiratory tract and the carcinomas derived from them differ markedly in their differentiation characteristics. Using immunofluorescence microscopy and two-dimensional gel electrophoresis of cytoskeletal proteins from microdissected tissues we have considered whether cytokeratin polypeptides can serve as markers of cell differentiation in epithelia from various parts of the human and bovine lower respiratory tract. In addition , we have compared these protein patterns with those found in the two commonest types of human lung carcinoma and in several cultured lung carcinoma cell lines. By immunofluorescence microscopy, broad spectrum antibodies to cytokeratins stain all epithelial cells of the respiratory tract, including basal, ciliated, goblet, and alveolar cells as well as all tumor cells of adenocarcinomas and squamous cell carcinomas. However, in contrast, selective cytokeratin antibodies reveal cell type-related differences. Basal cells of the bronchial epithelium react with antibodies raised against a specific epidermal keratin polypeptide but not with antibodies derived from cytokeratins characteristic of simple epithelia. When examined by two-dimensional gel electrophoresis, the alveolar cells of human lung show cytokeratin polypeptides typical of simple epithelia (nos. 7, 8, 18 and 19) whereas the bronchial epithelium expresses, in addition, basic cytokeratins (no. 5, small amounts of no. 6) as well as the acidic polypeptides nos. 15 and 17. Bovine alveolar cells also differ from cells of the tracheal epithelium by the absence of a basic cytokeratin polypeptide. All adenocarcinomas of the lung reveal a "simple-epithelium-type" cytokeratin pattern (nos. 7, 8, 18 and 19). In contrast, squamous cell carcinomas of the lung contain an unusual complexity of cytokeratins. We have consistently found polypeptides nos. 5, 6, 8, 13, 17, 18 and 19 and, in some cases, variable amounts of cytokeratins nos. 4, 14 and 15. Several established cell lines derived from human lung carcinomas (SK-LU-1, Calu -1, SK-MES-1 and A-549) show a uniform pattern of cytokeratin polypeptides (nos. 7, 8, 18 and 19), similar to that found in adenocarcinomas. In addition, vimentin filaments are produced in all the cell lines examined, except for SK-LU-1.(ABSTRACT TRUNCATED AT 400 WORDS)
Virchows Arch B Cell Pathol Incl Mol Pathol 1984
PMID:Cytokeratins in normal lung and lung carcinomas. I. Adenocarcinomas, squamous cell carcinomas and cultured cell lines. 620 12

A contiguous region of cellular DNA sequence, 64 kb in length and representing overlapping cellular inserts from three independent cosmid clones, has been isolated from a representative library of human lung carcinoma DNA partially digested with MboI. Within this region of the cellular genome, v-abl homologous sequences are dispersed over a total region of around 32 kb. These sequences represent the entire v-abl human cellular homologue, are colinear with the viral v-abl transforming gene, and contain a minimum of seven intervening sequences. At least eight regions of highly repetitive DNA sequences have been shown to map in close proximity to c-abl coding sequences. In addition to the major c-abl human locus, three regions of human DNA sequence, corresponding to only portions of the v-abl gene, have been identified. Two of these have been molecularly cloned and shown to be distinct from the primary human c-abl locus. Upon transfection to rat embryo fibroblasts in culture, none of the cosmid DNAs containing v-abl homologous sequences exhibited transforming activity. These findings identify and map a single genetic locus of human DNA, c-abl, representing the complete v-abl homologue, and demonstrate the existence of additional human DNA sequences corresponding to more limited, subgenomic regions of v-abl.
J Mol Appl Genet 1983
PMID:The human v-abl cellular homologue. 630 94

The pattern of subtypes of the nucleosomal histones and of histone H1 was investigated in human cells from adult and fetal lung and liver, from carcinoma tissues and from carcinoma-derived cell lines, with the object of comparing these patterns, and their relationship to cell growth rate, with those in cells of other species. The subtype pattern of the nucleosomal histones H2A and H3 shows a correlation with replication rate. In adult tissues, subtype H3-3 predominates over H3-2 and H3-1, and the subtype H2A-1 and H2A-2 are approximately equally abundant. In fetal tissues, lung carcinoma and cultured carcinoma-derived cell lines, the subtype H3-1 is predominant and H2A-1 is more abundant than H2A-2. The subtype pattern of H1 also differs between normal and carcinoma cells, among different tissues, and in different cell lines derived from the same type of carcinoma. In particular, the relative level of H1 degrees differs in several cell lines showing relatively high rates of replication, and in some cases represents more than 25% of the total H1, similar to the level in slowly replicating normal adult liver and lung tissues. The relative level of H1 degrees does not therefore appear to be correlated in a simple manner with cell growth rate in these human cells.
Mol Cell Biochem 1984 Nov
PMID:Histone complements of human tissues, carcinomas, and carcinoma-derived cell lines. 654 67

A monoclonal antibody, 16B-13, derived from the immunization of BALB/c mice with a lung tumor line, immunoprecipitates a common tumor-associated molecule with an apparent mol. wt of 37,000 from lactoperoxidase-iodinated lung carcinoma, colon carcinoma, gastric carcinoma, brest carcinoma, melanoma and lymphoma cells, but not from normal fibroblasts. Analysis by two-dimensional gel electrophoresis of the cell surface-labeled 16B-13 antigen from a colorectal and a melanoma cell line reveals four components with similar mol. wts but with different isoelectric points. The antigen purified from a colorectal carcinoma cell line by immunoaffinity chromatography was shown to be a 37,000 mol. wt polypeptide similar to that obtained by the lactoperoxidase-labeling procedure. However, the purified antigen from the melanoma cell line shows the presence of a 65,000 mol. wt polypeptide and the loss of the 37,000 mol. wt component as detected by Coomassie blue staining and immunoprecipitation.
Mol Immunol 1983 Dec
PMID:Identification and isolation of a common tumor-associated molecule using monoclonal antibody. 665 79


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