Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0025202 (melanoma)
 69,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A pigmented subclone of Cloudman S91 melanoma cells, PS1-wild type, can grow in medium lacking tyrosine. This ability is conferred by phenylalanine hydroxylase activity, and not by tryptophan hydroxylase, tyrosine hydroxylase or tyrosinase activities, although the latter activity is also present in these cells. Conversion of phenylalanine to tyrosine was measured in living cells by chromatographic identification of the metabolites of [14C]phenylalanine and in cell extracts using a sensitive assay for phenylalanine hydroxylase. Phenylalanine hydroxylase activity in melanoma cell extracts was identified by its inhibition with p-chlorophenylalanine and not with 6-fluorotryptophan, 3-iodotyrosine, phenylthiourea, tyrosine or tryptophan; and by adsorption with antiserum prepared against purified rat liver phenylalanine hydroxylase, and migration of immunoprecipitable activity with authentic phenylalanine hydroxylase subunits in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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PMID:Phenylalanine hydroxylase in melanoma cells. 2 86

Specimens from various types of Paget disease, other tumors, and certain normal tissues were examined with a battery of histochemical techniques, including the sodium borohydride-potassium hydroxide-PAS method that specifically stains certain sialomucins that are found in terminal parts of the ileum and of the colon. These sialomucins were present in normal anal ducts but were not present in transitional or anal-covering epithelium. A case of perianal Paget disease showed strongly positive staining, both in the underlying mucinous adenocarcinoma and in Paget cells of the affected anal and perianal skin. In contrast, stains of other forms of Paget disease were totally negative with this technique, as well as malignant melanoma and Bowen disease. These results support the theory that Paget disease represents epidermal invasion by malignant cells from underlying tumor.
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PMID:Perianal Paget disease. Histochemical differentiation utilizing the borohydride-KOH-PAS reaction. 5 63

Biochemical characterization of serologically detected human melanoma antigens was undertaken for the development of immunodiagnostic assays in melanoma. An antiserum from a human melanoma patient, which detected melanoma antigens expressed on a large proportion of different melanoma cells, was used in leucocyte-dependent cytotoxic antibody (LDA) 51Cr-release assays to monitor the purification of melanoma antigens in urea/acetate extracts of lactoperoxidase 125I-labelled melanoma cell membranes. The separation procedures included affinity chromatography on Concanavalin A, gel filtration on porous polyacrylamide beads and preparative isoelectric focusing. The fractions were also monitored by polyacrylamide electrophoresis in sodium dodecyl sulphate and by measurement of beta 2 microglobulin and carcinoembryonic antigen content. The antigens detected by this antiserum appeared to be acidic (pI 3.5) low-mol.-wt glycoproteins of approximately 15,000 daltons which were resistant to heating at 56 degrees C and digestion with neuraminidase, but susceptible to repeated freeze-thawing and trypsin digestion. They did not appear to be related to HLA antigens, beta 2 microglobulin or known foetal antigens. The nature of the antigens detected in these studies is as yet unknown, but they appear similar to those described in the sera and urine of melanoma patients in previous reports. Thes combined results and the frequent expression of these antigens on melanoma cells from different patients suggest that assays to detect this antigen may provide a valuable immunodiagnostic aid in the management of melanoma.
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PMID:Detection of a low-molecular-weight antigen on melanoma cells by a human antiserum in leukocyte-dependent antibody assays. 9 79

The addition of 1 percent (w/v) bovine serum albumin (BSA) to the F12 medium utilized for the growth of the B16 melanoma cells significantly stimulated the growth of this cell line. The synthesis of mucopolysaccharides and sialoglycopeptides in this medium is identical with that in Eagle's minimal essential medium with Earle's balanced salt solution supplemented with 2 mM L-glutamine, twice the recommended concentration of vitamins, nonessential amino acids, sodium pyruvate, and 10 percent (v/v) fetal calf serum. Cell volume and morphology did not change significantly, under the different growth conditions and tumorigenicity, as assayed by injection of cultured cells into syngeneic animals, was not decreased. Analysis of the BSA used indicated the presence of a sialoglycoprotein contaminant. This sialoglycoprotein contaminant was present in all lots examined and contains N-acetyl-and N-glycolylneuraminic acid, mannose, galactose, and glucosamine. The sialoglycoprotein can be removed by chromatography on acetate form anion-exchange resin at pH 4.3. F12 media containing the purified BSA plus selenite and the sodium salts of palmitic, oleic, and linoleic acids supported growth of the melanoma cells to the same extent as did the media containing unpurified BSA, indicating that the sialoglycoprotein has no role in sustaining the growth of the cells.
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PMID:Chemical and biological properties of B16 murine melanoma cells grown in defined medium containing bovine serum albumin. 14 59

The proliferation of human melanocytes in vitro was stimulated by MSH. This stimulation was further intensified by the simultaneous addition of theophylline with MSH. Theophylline alone stimulated proliferation moderately. Dibutyryl cyclic AMP strongly stimulated the proliferation, but sodium butyrate, 5'-AMP and cGMP did not. The stimulation by dibutyryl cyclic AMP was continued up to 4 days so far tested. These findings are directly opposed to those on mouse melanoma cells in culture which responded with retarded growth to MSH and cyclic AMP. It is suggested that the difference of proliferation control may explain the different reaction of the melanocyte and the melanoma cells. The epidermal melanocytes seem to belong to the exceptional group of the cells which responded to cyclic AMP with accelerated proliferation.
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PMID:Stimulation by melanocyte stimulating hormone and dibutyryl adenosine 3'5'-cyclic monophosphate of DNA synthesis in human melanocytes in vitro. 18 88

Sodium butyrate and cyclic AMP-stimulating agents (prostaglandin E1, papaverine, theophylline, and RO20-1724) caused reductions in the cell number (primarily due to reduction in cell division) when added individually to human melanoma cells in culture. However, the combination of sodium butyrate with one of the cyclic AMP-stimulating agents produced a marked reduction in cell number (primarily due to cell death).
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PMID:Effect of sodium butyrate in combination with prostaglandin E1 and inhibitors of cyclic nucleotide phosphodiesterase on human amelanotic melanoma cells in culture. 21 47

Human melanoma cell membrane tumor-associated antigens (TAA's) were solubilized in an active form by pronase digestion of either a fresh melanoma or cells from a melanoma cell line maintained in tissue culture. Upon elution from Sephadex G-200 column, TAA's solubilized from the melanoma cell line were found in four distinct peaks that had apparent molecular weights of approximately 48,000 (partition coefficient Kd, 0.426), 25,000 (Kd, 0.567)8 17,000 (Kd, 0.699), and 13,000 (Kd, 0.831) daltons, respectively. Fetal antigen activity was found in all but the 13,000-dalton peak. HLA antigen activity was detected in the 17,000-dalton material. TAA's prepared from the fresh tumor source eluted from Sephadex G-200 column with an apparent molecular weight of 14,000-25,000 (Kd, 0.786-0.572) daltons, as did HLA antigens. A partial resolution of the TAA's from the HLA antigens was achieved with the use of DEAE-cellulose chromatography. Results of antigenic stability assays suggested that the TAA structure is stable to prolonged exposure to low pH. Recovery of TAA activity from the strong denaturing agents 5 m urea, 0.5% (wt/vol) sodium dodecyl sulfate, and 4 m guanidine hydrochloride was partially successful. These properties of the TAA's may be useful for further isolation of the TAA's.
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PMID:Solubilization and partial isolation of human melanoma tumor-associated antigens. 27 39

Using normal human lymphocytes isolated by sedimentation and cotton column adherence, we have developed a reliable assay of immunosuppression of PHA-induced blastogenesis by serum from selected melanoma patients. These lymphocyte cultures contained both responder cells (subpopulation x) and regulator cells (subpopulation y). Lymphocytes isolated by gradient centrifugation on sodium metrizoate-Ficoll contained responder cells (x) but no regulator cells (y). Cultures of lymphocytes isolated by this method were stimulated by PHA but were not suppressed by the addition of melanoma serum. When lymphocytes were isolated by a cotton column adherence/Lymphoprep centrifugation-double separation, subpopulations (x) and (y) were isolated. We have established that both subpopulations are necessary for suppression to occur, and that (y) operates as the regulator of (x). Finally, by manipulating B cell and T cell populations isolated by nylon column adherence or AET rosette separation, we have determined that the regulator ability of subpopulation (y) is the result of B cell activation of suppressor T cells.
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PMID:Melanoma-associated immunosuppression through B cell activation of suppressor T cells. 808 5

Disc gel electrophoresis of tyrosinase solubilized by sodium deoxycholate (DOC) from the particle fraction of B16 mouse melanoma was carried out in the presence of DOC. A single tyrosinase band, considered to be T3, was detected at the Rx value of 0.60 against Coomassie brilliant blue. The T3 band which is located between T1 and T2 seems to be distinct from the soluble forms of tyrosinase. Its molecular weight was estimated to be 102,000. When treated with proteolytic enzymes or refrigerated, the T3 molecule converted into a molecule whose mobility was equivalent tothat of T1.
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PMID:Granule-bound tyrosinase: solubilization and its relation to the soluble form of tyrosinase. 40 50

A highly purified toxin (vibriolysin) from Vibrio parahaemolyticus caused degeneration of cell shape, such as bleb and balloon formation, of mouse myocardial cells and mouse melanoma cells in culture. An extracellular Ca2+ concentration of more than 10(-6) M was necessary for the degeneration of cell shape, but extracellular Mg2+, Na+, and K+ were not necessary. In the presence of extracellular Ca2+, vibriolysin also caused full contraction of myofibrils of mouse myocardial cells and reduction of both actin cables and tubulin networks of mouse melanoma cells. Vibriolysin also caused excess uptake of Ca2+ from the incubation medium by mouse myocardial cells and mouse melanoma cells. Chick myocardial cells, which show neither degeneration of cell shape nor full contraction of myofibrils, did not take up excess 45Ca2+ in the presence of vibriolysin. These findings suggest that the vibriolysin-induced degeneration of cell shape of mouse myocardial cells and mouse melanoma cells is due to excess uptake of Ca2+ from the incubation medium by the cells.
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PMID:Requirement of calcium ions for cell degeneration with a toxin (vibriolysin) from Vibrio parahaemolyticus. 56 46


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