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Query: UMLS:C0025202 (melanoma)
 69,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tumor cells release intact portions of their plasma membranes in the process of membrane fragment shedding. This released material has been shown to inhibit various synthetic functions of normal cells, which may play an important role in certain patho-physiological events occurring in advanced-stage cancer patients. Our studies on metastatic variants of the murine B16 melanoma, B16-F1 (low incidence of lung colonization) and B16-F10 (high incidence of lung colonization) indicate that the shed membrane fragment material is composed predominantly of vesicles, ranging in size from 20 to 100 nm in diameter. The release of membrane fragments represents a small percentage (approximately 16%) of the total shedding of plasma membrane components. Membrane fragments were shed at a higher rate from the highly "metastatic" (colonizing) B16-F10 cells than from poorly metastatic B16-F1 cells, resulting in a 2-fold greater accumulation of membrane fragment material by cultures of B16-F10 cells than by B16-F1 cultures during the 48-hr assay period. The study of various intracellu ar metabolic processes (protein and RNA synthesis, glycosylation, and generation of ATP) required for the shedding of membrane fragments indicated that the shedding event is only dependent on energy when inhibitors of the above processes are present for 2 hr. Treatment of cells with these inhibitors for 8 hr results in cessation of the shedding process, indicating both a limited pool of components to be shed and the requirement for further synthesis of the shed material. Glycoprotein components of the shed membrane fragments were analyzed by SDS-polyacrylamide gel electrophoresis. In addition to quantitative differences, 2 additional bands were present in fluorographs from SDS-PAGE gels from the B16-F10 membrane fragment material which were not present in fluorographs from B16-F1 fragments. The glycoprotein components of shed membrane fragments were shown to represent selected domains of the cell's plasma membranes, in that only certain plasma membrane glycoproteins are shed as part of membrane fragments. The glycoproteins released as non-particulate molecules into the extracellular environment failed to exhibit these quantitative and qualitative differences.
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PMID:Characterization of plasma membrane shedding from murine melanoma cells. 335 93

The behaviour in vivo of tight and loose variants of murine melanoma cells is further characterized. In vitro clonal morphology is reproduced on a variety of substrates. Results suggest that repeated selection of loose cells can co-select for cells with high metastatic and colonization potentials. Measurement of cell motility shows that 1G3 (loose) cells are more motile than 1G8 (tight) which are restricted to movements within clonal boundaries. Studies of adhesive properties show that loose cells are more easily detached from the substrate with trypsin or EDTA and that both cell lines attach more quickly to monolayers of loose cells than to tight ones. No gross differences are found either in attachment rates to plastic and ECM or in aggregation and disaggregation rates. Analysis of the cell surface has not revealed any differences between 1G8 and 1G3 in the sialylation of terminal galactose and N-acetylgalactosamine residues or in neuraminidase releasable sialic acid. The binding patterns of iodinated lectins to SDS-PAGE separated proteins are similar for both lines except for one 85/90 KD protein which is more abundant in 1G3 than 1G8 cells after neuraminidase treatment. The results show enhanced differences in metastatic potential of tight and loose clones after selective cloning and that there may be important differences in motility and cell-substrate interactions.
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PMID:Morphological and metastatic murine melanoma variants: motility, adhesiveness, cell surface and in vivo properties. 342 20

Some coat-color loci in mice are considered to control melanosome formation. In order to investigate genetic control of melanosome-associated proteins, we prepared monoclonal antibodies against mouse melanosomes. Melanosomes were isolated from B16 mouse melanoma through differential fractionation. BALB/c mice were immunized with an SDS-solubilized melanosome fraction. The spleen cells were subsequently fused with mouse myeloma cells, the resulting hybridomas cloned. Their secreted IgG was screened for reactivity to the SDS-solubilized melanosome fraction. One monoclonal antibody, M10, was shown to react to melanosomes by immunoelectronmicroscopy. It recognized a single protein band of 61,000 dalton on immunoblots of gel-fractionated melanosomes. The reactivities of M10 to skin homogenates from various coat-color mutants were examined by the ELISA method. Five congenic genotypes, non-agouti (a/a), brown (b/b), albino (c/c), dilute (d/d), and pink-eyed dilution (p/p) were examined. Among these, b/b and p/p showed significantly lower reactivities than a/a. Our results seem to suggest that the pigment abnormalities in these mutants result from abnormalities of the melanosomal proteins. In the case of albino mice, the reactivity of M10 to skin homogenate was almost the same as the wild-type mouse. It seems that the albino mice are capable of producing the melanosomal protein.
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PMID:Deficient melanosome formation in some coat-color mutant mice revealed by a monoclonal antibody against melanosome. 350 65

Cultured human melanoma M21 cells were treated with diethylcarbamazine (DEC), an inhibitor of proteoglycan biosynthesis in rat chondrosarcoma cells, to examine the assembly and transport of a chondroitin sulfate proteoglycan to the plasma membrane. Pretreatment of melanoma cells at 37 degrees C for 15 min with increasing doses of DEC followed by a 60-min pulse with [35S]sulfate in the presence of DEC resulted in a dose-related inhibition of incorporation of [35S]sulfate into macromolecules. In cells incubated for 75 min with both 1 mM beta-D-xyloside and 15 mM DEC, synthesis and secretion of beta-D-xyloside-bound 35S-glycosaminoglycans were inhibited by more than 80% as compared to cells treated with beta-D-xyloside alone; this inhibition was reversible. As assessed by [3H]serine incorporation into protein, overall protein synthesis was not substantially inhibited by DEC treatment. Detergent lysates from [35S]methionine-labeled melanoma cells were incubated with a monoclonal antibody (9.2.27) that specifically recognizes the peptide core of the melanoma proteoglycan. As assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the immunoprecipitate, a 240,000 Mr endoglycosidase H (Endo-H)-sensitive intermediate was the only form of the proteoglycan present inside the cells when the cultures were treated for 60-120 min with 10-15 mM DEC. When the melanoma cells were incubated for 10 min with 15 mM DEC and 100 mu Ci/ml of [35S]methionine, washed, and then chased for 15 min to 4 h in radioactive-free medium, the 240,000 Mr Endo-H-sensitive intermediate was slowly converted to a 250,000 Endo-H-resistant intermediate but not to a mature proteoglycan molecule that possessed chondroitin sulfate glycosaminoglycans. SDS-PAGE analysis of cell surface immunoprecipitates revealed that only a small amount of the 250,000 Mr intermediate was transported to the plasma membrane within 5 h of incubation in the presence of DEC. Proteoglycan synthesis was also inhibited when the melanoma cells were incubated for 60-120 min with ammonium chloride, but unlike DEC-treated cells the majority of the synthesized peptide core was converted to a 245,000 Mr Endo-H-resistant intermediate that was detected on the cell surface. Light and electron microscopic analysis of DEC-treated melanoma cells revealed large vacuoles and a distended Golgi and endoplasmic reticulum. Ammonium chloride-treated cells contained fewer vacuoles than DEC-treated cells but more vacuoles than normal cells.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Inhibition of post-translational modification and surface expression of a melanoma-associated chondroitin sulfate proteoglycan by diethylcarbamazine or ammonium chloride. 351 9

Antimelanosome-associated monoclonal antibody has recognized the common antigenic determinant of melanosomes and cell surface of pigment cells, and it is suggested that melanosomes play a significant role as an antigen in progressive depigmentary disorders, in which melanocytes are selectively altered and disappear presumably by auto-antibodies in vivo. Mouse myeloma cells were fused with spleen cells from BALB/c mice immunized with a melanosomal fraction separated from human melanotic melanoma cells (Mm-1-JCK). The monoclonal antibody (MoAb) A4F11 has been found to react with premelanosomes, melanosomes, and probably with Golgi-associated endoplasmic reticulum lysosomes, but not with mitochondria, nuclei, and cytosol from human melanoma cells, by immunoelectron microscopy using the saponin permeation method, which was carried out together with indirect radioimmunoassay and quantitative absorption assay. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting using melanosome preparations have revealed the antigen(s) reactive with the MoAb A4F11 in 3 bands corresponding to Mr 50,000, 18,000, and 17,000. Cell binding assay has shown the reactivity of the MoAb A4F11 with the cell surface of human normal melanocytes and melanoma cells, but not with other mammalian melanoma cells or with human nonpigment cells examined. Indirect immunofluorescence on cultured cells and frozen sections has revealed distinct granular reactivity not only with human melanotic melanoma, but also with junctional and intradermal nevi, cultured malignant blue nevus cells, as well as normal melanocytes. The above evidence has indicated the presence of an antigenic determinant common to the intracellular melanogenic compartments and to the cell surface of human pigment cells, regardless of their oncogenic differentiation status.
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PMID:Melanosomal antigenic expression on the cell surface and intracellular subunits within melanogenic compartments of pigment cells: analysis by antimelanosome-associated monoclonal antibody. 352 55

B16-F1 melanoma cells cultivated in vitro as spheroids on a non-adhesive substrate acquire in a reversible fashion an increase in lung colonization in vivo as compared to cells cultured as a monolayer. After neuraminidase treatment of protein blots, the spheroidal cells expressed an increased binding of 125I-labelled peanut lectin (PNA) to a unique glycoprotein of Mr 78,000 (gp78) which after desialylation migrated in SDS-polyacrylamide gels as an Mr 86,000 protein. Antibodies were generated against this glycoprotein purified on PNA-Sepharose and its expression on the surface of viable B16-F1 cells was demonstrated. Growth of B16-F1 melanoma cells in suspension is associated with the altered glycosylation of gp78 which may be related to the increased metastatic ability of these cells. In vitro treatment of B16-F1 cells with anti-gp78 Fab fragments prior to their injection into the tail veins of syngeneic mice resulted in a 2-fold increase in the appearance of tumor lung colonies.
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PMID:Cell shape modulation alters glycosylation of a metastatic melanoma cell-surface antigen. 362 18

UV-irradiation at 365 nm of cultured Cloudman S91 mouse melanoma cells in the presence of photoreactive alpha-MSH analogues induced longlasting receptor stimulation as revealed by the ensuring activation of tyrosinase. Receptor labelling was more efficient with 4-diazirinophenyl and 2-nitro-4-azidophenyl photolabels than with 4-azidophenyl, and was further increased when superpotent [Nle4,D-Phe7]-alpha-MSH was used as ligand. Incubation of B16 melanoma cell membranes with mono-iodinated [Nle4,D-Phe7,Trp-(Naps)9]-alpha-MSH followed by UV-irradiation at 310-550 nm labelled a single band on SDS-PAGE with a molecular mass approximately or equal to 45 kDa. The displacement curve obtained in a competitive photolabelling experiment paralleled that of the binding assay, demonstrating that the labelling was specific.
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PMID:Photoaffinity labelling of melanoma cell MSH receptors. 369 12

The ability of lonidamine [1-(2,4)-dichlorobenzyl-1H-indazol-3-carboxylic acid], to induce a stress response in human and murine cultured melanoma cells has been demonstrated. In the M14 and M10 human melanoma cell lines, lonidamine enhances the synthesis of a unique set of proteins, characterized by SDS-PAGE by an Mr of about 72 kDa. In the B16 murine melanoma cell line, exposure to lonidamine increases the synthetic rate of two polypeptides of mol mass 86 and 72 kDa, respectively. Lonidamine is a drug which specifically acts on mitochondria. Therefore the observation that it can also promote a stress response indicates that the mitochondria might be one of the primary cellular targets and postulates a causal relationship between an impairment of the energy supply and induction of stress protein synthesis.
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PMID:Induction of stress proteins by lonidamine in human and murine melanoma cells. 369 38

In order to screen human tumor cells for putative cell surface marker molecules, the glycoprotein composition of in vitro cultivated human tumor cell lines of different origin (12 carcinomas, one neuroblastoma, one melanoma and one sarcoma) was analyzed by metabolically labelling the cells with [3H]galactose, [3H]mannose and [3H]fucose and subsequently separating the labelled material by SDS-PAGE. The cell lines expressed their specific glycoprotein patterns. Strongly glycosylated proteins of apparent mol. wt 40-45 kD, 60-62 kD, 80-82 kD and 90-92 kD were shared by nearly all carcinoma cell lines studied. Apart from these glycoprotein clusters, a great diversity was observed between tumor cell lines derived from the same organ. Three bladder carcinoma cell lines had a 112-114 kD glycoprotein in common. Glycoprotein expression of these cell lines remained constant during 1 yr of in vitro culture. Hence, these glycoprotein patterns seem to be useful for monitoring the phenotypic stability of cell lines. A sarcoma cell line was deficient in incorporating fucose and showed strikingly different glycoprotein patterns compared to the other cell lines studied. The metabolic labelling procedure revealed a wide phenotypic heterogeneity of the human carcinoma cell lines concerning glycoprotein synthesis. This method contributes another parameter to map the major glycoprotein species of various types of carcinomas.
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PMID:Heterogeneity of glycoprotein synthesis in human tumor cell lines. 370 97

Lectin binding glycoproteins of 5 human malignant melanoma cell lines (HMMCL), differing in their ability to grow subcutaneously in athymic nude mice, were compared by electrophoresis of total cellular proteins and subsequent incubation of SDS-poly-acrylamide gel with 125I-labelled lectins. Despite the similarity between the protein profiles of the different HMMCL, Concanavalia ensiformis agglutinin (ConA), wheat-germ agglutinin (WGA) and peanut agglutinin (PNA) revealed differences in their glycoprotein expression, in contrast with Ulex europaeus agglutinin I (UEA I). A great diversity was observed in the electrophoretic mobilities and/or staining intensities of ConA and WGA binding glycoproteins of HMMCL. However, neither ConA-reactive glycoproteins nor WGA-reactive glycoproteins could be detected that were characteristic of HMMCL with high tumorigenicity (HT) or low tumorigenicity (LT). In contrast, the expression of two cell-surface PNA binding glycoproteins appeared to be related to the tumorigenic phenotype of HMMCL. One of them, with an apparent molecular weight of 190 kDa, was only detected in the LT cell lines. The other, with an apparent molecular weight of 60 kDa, was detected in all HMMCL but became strongly labelled after neuraminidase treatment only in the HT cell lines. Thus, the expression of glycoproteins rich in terminal galactose residues may characterize human melanoma cells with different tumorigenic behavior.
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PMID:Lectin binding glycoproteins in human melanoma cell lines with high or low tumorigenicity. 375 39


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