Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

TL antigen was solubilized from the tumor ASLI (TL. 1,2,3) by papain digestion. The subfragments of 125I-labeled TL were examined by two methods. The first involved immune precipitation followed by electrophoresis on SDS-acrylamide gels. This treatment yielded three bands of molecular weight 39,000 and 19,000, as well as material which migrated with the tracking dye. In the second procedure the papain digested material was partially purified on Sephadex G-200. The active fraction from G-200 was labeled with 125Iodine, mixed with alloantiserum and rechromatographed on G-200. The isolated immune complexes were boiled in SDS and 2-mercaptoethanol, then separated on a SDS-Sephadex G-150 column. Two radioactive peaks were eluted indicating an absence of the 19,000 m.w. component following the latter method of purification.
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PMID:Subfragments of the papain solubilized TL antigen. 117 64

Evidence is presented that at least one of the antigens of human ovarian cancer tissue which appeared to be tumor-associated in immunodiffusion and immunoelectrophoresis experiments actually represents a quantitative rather than a qualitative difference between normal and malignant tissue. A glucoprotein band (Rf equals 0.01) believed to contain at least one tumor-associated antigen was isolated by disc-gel electrophoresis with 5.6 per cent SDS-acrylamide and was used to immunize rabbits. Immunodiffusion and immunoelectrophoresis experiments with the resulting antiserum indicated that the glycoprotein band contained two antigens, one which was present in normal extracts at a concentration approximately one tenth of that in tumor extracts and another which was detectable only in tumor tissue. The tenfold difference between normal and tumor tissue was confirmed by studies of the appearance and disappearance of the glycoprotein band when acrylamide gel electrophoresis was performed on varying amounts of normal and tumor extracts.
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PMID:Quantitation of antigens in normal and malignant ovarian tissue. 118 Feb 93

Levels of putrescrine, spermidine, and spermine in urine were determined by means of a sensitive ion-exchange chromatographic method in patients with advanced solid tumor malignancies, in patients with diseases other than cancer, and in normal control subjects. Elevation above 2 SDS of the normal mean were found in varying number of patients in each tumor category. For those malignancies studied that involved more than 20 patients, the greatest incidences of increased excretion were 66% for spermine in patients with colon carcinoma and 50% for putrescine and spermidine in patients with bronchogenic carcinoma. The highest levels and greatest frequency of elevated polyamine levels were found in patients with Burkitt's lymphoma, and changes in clinical tumor status associated with treatment appeared to correlate well with polyamine levels in this disease. Abnormal amounts of polyamines were also excreted by some patients with diseases other than cancer, indicating that increased polyamine excretion is not restricted or specific to the neoplastic state. It was also found that the levels of polyamines were apparently not affected by the intake of meat or the diet eaten, and remained in a rather narrow excretion range for any one individual at different time intervals. This study was carried out as part of a program to determine and evaluate biologic materials present in body fluids that may be used to follow and evaluate response or progression of neoplastic disease in patients during treatment regimens. The results suggest that abnormal urinary polyamine levels may be characteristic of neoplastic growth for some patients with malignant disease. Further studies are necessary to determine if these compounds may be helpful in assessing disease status for patients with such solid tumor malignancies as colon and bronchogenic carcinoma although their potential as useful "biologic markers" appears less promising than originally anticipated.
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PMID:Urinary excretion of polyamines by patients with advanced malignancy. 122 94

Discontinuation of recommencement of estrone-progesterone treatment causes regression and regrowth, respectively, of transplantable hormone-dependent GR mouse mammary tumors. This tumor model was found convenient for the demonstration of hormonal responses in hormone-dependent mouse mammary tumor cells. Tumor regression was palpable 2 days after discontinuation of hormonal treatment and tumors reached half their size within 3-6 days. At this point, hormones were readministered and 2-4 days later the tumors had grown to their preregression size. In the growing and regressing tumor we have investigated: (1) the content of RNA, DNA and protein per g wet weight, (2) in vivo incorporation for 45 min of 32P-orthophosphate into RNA and DNA and the 35S-methionine incorporation into protine; (3) SDS polyacrylamide gel electrophoresis of soluble proteins after in vivo incorporation of 14C- and 3H-leucine. The RNA content per g wet weight was found to decrease during regression and to increase during regrowth. DNA and protein content showed no variation. RNA/DNA ratio thus varied in parallel to the RNA content. The precuursor incorporation into all three macromolecular species decreased during regression. The incorporation into DNA showed the most pronounced decrease. After readministration of hormones, regrowth was accompanied by a rapid increase in precursor incorporation into RNA, while the incorporation into DNA showed a lag of 1 to 2 days. SDS polyacrylamide gel electrophoresis was carried out with soluble proteins labelled in vivo with 14C- and 3H-leucine during regression and regrowth, respectively. No differences in 14C/3H ratios could be demonstrated for the major fractions detectable in the electropherogram.
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PMID:Biochemical changes during regression and regrowth of hormone-dependent GR mouse mammary tumors. 124 97

The p53 gene, located on chromosome 17p13.1, may be important in the pathogenesis of human neuroepithelial tumors, because it is a tumor suppressor gene and genetic alteration is essential for certain human cells to acquire the neoplastic phenotype. The structure and expression of the p53 gene were investigated in cultured human glioma cells and biopsied specimens of neuroepithelial tumors. Immunocytochemical examination of p53 gene expression revealed positive nuclear staining in six of seven glioma cell lines tested. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis demonstrated unequivocal heterogeneity of migration rate in p53 bands. Pulse-chase analysis clearly showed an increased half-life of p53 in cultured human glioma cells. These abnormalities are presumably due to genetic alterations in the p53 gene. Nucleotide substitutions in exon 5, 7, or 8 of the p53 gene could be detected by polymerase chain reaction-single strand conformational polymorphic analysis in four of seven (57%) human glioma cell lines, and nine of 29 (31%) biopsied specimens of neuroepithelial tumors examined. The present results indicate that genetic alterations in the p53 gene are responsible for the tumorigenesis of at least some human neuroepithelial tumors.
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PMID:Altered structure and expression of the p53 gene in human neuroepithelial tumors. 128 Jul 73

We have earlier reported production and characterization of monoclonal antibodies (MAbs) to human thyroglobulin (h-tg). In the present study H10 I MAb was evaluated for its immunoreactivity towards different forms of tg and various human thyroid tumours. The specificity of H10 I MAb was validated by the absence of cross reaction with tri-iodothyronine (T3) Thyroxine (T4) and human gamma globulins. Sodium-dodicyl-sulphate polyacrylamide gel electrophoresed (SDS-PAGE) immunoblot of h-tg on the nitrocellulose membrane revealed multiple immunoreactive bands on reaction with polyclonal antibody (PAb) in comparison with total lack of reactivity with H10 I MAb. The absence of immunoreactivity of H10 I MAb was demonstrated with SDS treated, Dithiothreitol (DT) treated and heat denatured tg using dot immunobinding technique. However, the H10 I MAb was able to react with tg treated with unfolding agents such as urea and guanidine hydrochloride. All the treated forms of tg were equally recognized by PAb. The immunoreactivity of the oxidized/reduced tg towards H10 I MAb was markedly reduced (60.0%) as compared to that obtained with native tg. It appears that H10 I MAb is directed towards conformational epitope involving sulphydryl bonds. Immunohistochemically, a comparable immunoreactivity between PAb and MAb was observed with normal thyroid tissues, follicular thyroid tissues, Hurthle cell carcinoma tissues and poorly differentiated thyroid tumor tissues using immunoperoxidase staining. The sections from papillary carcinoma tissue (thyroid as well as metastatic lymph node) exhibited intense immunoreactivity with PAb. Thyroglobulin present on these sections was not recognized by H10 I MAb. Nonetheless, H10 I MAb was able to detect tg in follicular differentiation wherever present. The absence of immunoreactivity of H10 I MAb in papillary carcinoma strongly suggests that this neoplasm produces tg which is antigenically different from the protein present in the normal tissue. The reactivity of H10 I MAb with metastatic lymph node of an unknown primary origin suggests its usefulness in the identification of prevalent metastasis of differentiated thyroid carcinoma other than papillary type.
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PMID:Monoclonal antibodies to human thyroglobulin: evaluation of immunoreactivity. 128 24

FcRs (Fc Receptors) have been detected on the cell surface of two human neuroblastoma cell lines; IMR 32 and SK-N-SH, by immunocytochemistry and flow cytometric analysis, using a previously characterized polyclonal antiserum raised against the Fc gamma R isolated from a human CLL line (Gorini, Medgyesi, Garavini, Dorrington and Down, 1987; Rozsnay, Sarmay, Szabo, Medgyesi, Gorini and Gergely, 1990). FcR is expressed on all the cells of both lines at least at the same level as on the HL60 promyelocyte cell line used as positive control. Two electrophoretic components displaying apparent molecular masses of 70 and 43 kDa respectively have been identified by SDS-PAGE followed by Western blotting analysis of crude cell membranes. In addition, "in situ" hybridization experiments seem to exclude a correlation between FcR expression and N-myc oncogene activity. The presence of FcR in neuroblastoma could be related to a possible functional role even on these cells which do not belong to the immune system; moreover, they could also be exploited for a diagnostic characterization of this tumor.
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PMID:Fc gamma receptors are expressed on human neuroblastoma cell lines: lack of correlation with N-myc oncogene activity. 130 13

A novel non-phorbol-ester-like tumor promoter, okadaic acid (OA) has been shown to be an inhibitor of protein phosphatase I and IIA and, thus, to cause an "apparent activation" of protein kinase C (PKC). We previously showed that cis-diamminedichloroplatinum(II) (CDDP)-resistant cells, PC-9/CDDP, were cross-resistant to OA and that the cross-resistance was not due to the increased efflux of OA. We hypothesized that the phosphorylation status of some cellular proteins might be important in CDDP-resistance. No significant difference in PKC activity or total protein phosphatase activity measured in vitro was seen between PC-9 and PC-9/CDDP cells, nor in their sensitivity to inhibition by OA, nor in the amount of phosphorylation of whole cells or TCA-insoluble material. By SDS-PAGE after incubation of intact cells with 32P, we detected a marked increase, compared to PC-9 cells, in phosphorylation of the nuclear proteins of MW 32 and 20 kDa in CDDP-resistant PC-9/CDDP cells with no apparent difference in protein content. When phosphorylation of nuclear proteins observed in PC-9/CDDP cells was analyzed by 2-dimensional SDS-PAGE, the 32-kDa protein had a PI of about 4.5. The 32-kDa and 20-kDa bands were increased in a dose-dependent manner by CDDP treatment. On the other hand, no increase in phosphorylation of these proteins was observed in parental PC-9 cells. These results demonstrate a marked difference in the phosphorylation status of specific nuclear proteins between parental and CDDP-resistant cell lines, which may be related to CDDP-resistance.
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PMID:Increased phosphorylation of nuclear phosphoproteins in human lung-cancer cells resistant to cis-diamminedichloroplatinum (II). 131 Apr 90

The pathogenesis and etiology of giant cell tumor of bone was studied by analysing the bone resorptive factors in the conditioned culture medium. In the primary culture characteristic multinucleated giant cells and mononuclear cells were coexisted. The values of interleukin 1 (IL-1) and prostaglandin E2 (PGE2) in the conditioned medium obtained from the primary culture were high. In the primary culture, an immunohistochemical technique revealed the presence of IL-1 both in mononuclear cells and in giant cells. When the medium obtained from the primary culture was tested for proteolytic activity by zymography with SDS/polyacrylamide containing gelatin, multiple gelatinolytic activities were observed. In subcultures, multinucleated giant cells were not persisted and only stromal cells were visible. In subcultures, the values of IL-1 and PGE2 were much lower. Proteolytic activities were similarly weak. However, the exposure of the passaged stromal cells to the medium containing IL-1 stimulated the stromal cells to produce PGE2 and proteolytic enzymes. Immunofluorescent localization technique revealed the expression of the proteolytic enzymes in the stromal cells. These findings demonstrated that coexistence of multinucleated giant cells with mononuclear cells should be needed for the tumor to express the original phenotype. In the presence of multi-nucleated cells, mononuclear cells seem to be stimulated to produce PGE2 and proteolytic enzymes, which accelerate the bone resorption. These factors are considered to act synergetically in the resorption of bones.
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PMID:[The pathogenesis and etiology of giant cell tumor of bone from a viewpoint of bone resorptive factors]. 132 84

The cellular urokinase-type plasminogen-activator (uPA) receptor (uPAR) is a glycolipid-anchored membrane protein thought to be involved in pericellular proteolysis during cell migration and tumor invasion. In the present study, we have identified and characterized two soluble forms of uPAR which have retained their ligand-binding capability. One variant was generated in vitro by treatment of intact normal cells with either a phosphatidylinositol-specific phospholipase C (PLC) or endoproteinase Asp-N. The other soluble uPAR variant was secreted in vivo from peripheral blood leukocytes affected by the stem-cell disorder paroxysmal nocturnal hemoglobinuria (PNH), and was found in the plasma from these PNH patients as well as in the conditioned medium from cultured PNH leukocytes. Under normal conditions, we find no evidence for any shedding or secretion of a soluble uPA-binding counterpart to human uPAR in plasma. Unlike normal leukocytes, the PNH-affected cells do not express uPAR on the cell surface, although they do contain apparently normal levels of uPAR-specific mRNA. The secreted uPAR derived from PNH cells has a mobility in SDS/PAGE that is slightly higher than that of uPAR solubilized by PtdIns-specific PLC or detergent, but resembles that of a truncated, recombinant uPAR variant, which has its C-terminus close to the proposed glycolipid-attachment site, suggesting that the secreted protein has been proteolytically processed for glycolipid attachment. The presence in plasma from PNH patients of such a secreted, hydrophilic form of uPAR lends support to the hypothesis that the lesion underlying the PNH disorder resides either in glycolipid biosynthesis or in the function of an as-yet-unidentified transamidating enzyme assumed to cleave and assemble the truncated uPAR with the preformed glycolipid moiety.
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PMID:A soluble form of the glycolipid-anchored receptor for urokinase-type plasminogen activator is secreted from peripheral blood leukocytes from patients with paroxysmal nocturnal hemoglobinuria. 132 6


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