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

A human melanoma cell line established in our laboratory was characterized in terms of tyrosinase activity and anionic polysaccharide production. Tyrosinase levels were diluted during the growth phase and increased after the cell culture became confluent. The anionic polysaccharides produced included hyaluronic acid, heparitin sulfate, and a high-molecular-weight condroitin 4-sulfate. In contrast, a primary culture of human melanocytes derived from embryonic iris produced much greater amounts of hyaluronic acid, about 30-fold less heparitin sulfate, and a mixture of chondroitin 4-sulfate and dermatan sulfate. Saccharides secreted into the culture medium were generally identical to those remaining cell associated except for the melanoma heparitin sulfate, wherein the latter fraction appeared to be of lower molecular weight.
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PMID:Anionic polysaccharide production and tyrosinase activation in cultured human melanoma cells. 13 Sep 71

The treatment of chondroitin sulfate isolated from cultured B16 mouse melanoma cells with 0.04 M HCl at 100 degrees C for 90 min released up to 45% of O-sulfate residues as free inorganic sulfate. In addition to the release of inorganic sulfate, extensive degradation of this polysaccharide as well as of cartilage chondroitin sulfate, pig rib cartilage proteoglycan, heparin and hyaluronic acid was also evident under these conditions. The above hydrolysis conditions are used for characterizing 35S-labeled heparan sulfates synthesized by cultured cells and to calculate ratio of N- and O-sulfates in these molecules. Our results suggest that caution is necessary in interpreting the results of mild acid hydrolysis of glycosaminoglycans.
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PMID:Release of O-sulfate groups under mild acid hydrolysis conditions used for estimation of N-sulfate content. 88 53

B16 melanoma cells were treated in culture with 5-bromo-2-deoxyuridine. The cell-associated and released proteoglycans and sialoglycopeptides were compared to those of control cultures treated with thymidine. The 5-bromo-2-deoxyuridine-treated cultures showed a marked reduction in the proportion of cell-associated proteoglycans and sialoglycopeptides, an increase in the synthesis of hyaluronic acid, the absence of high-molecular-weight chondroitin sulfate, and the presence of increased amounts of heparan sulfate in the media. In addition, the 5-bromo-2-deoxyuridine-treated cells had a higher DNA content and were larger than controls.
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PMID:The production of acidic polysaccharides by 5-bromodeoxyuridine-treated B16 mouse melanoma cells. 117 Sep 45

In order to investigate the metastatic potential of tumors in vivo by measuring hyaluronic acid metabolism, C57BL/6 mice with B16 melanoma variants and C3H/He mice with FM3A tumor variants were evaluated using N-[18F]fluoroacetyl-D-glucosamine (18F-GlcNFAc). The uptake of 18F-GlcNFAc was slightly higher (P less than 0.05) in B16-F10 tumors (high metastatic potential) than in B16-F1 (low metastatic potential). Analysis of metabolites showed that acid-insoluble fraction was the largest one in the liver by 60 min, whereas in the tumors, phosphates fraction was the major metabolite. Slower metabolism in tumors was suggested, and it may be one of the reasons for the difficulty of detecting the characteristics of their hyaluronic acid synthesis. 18F-GlcNFAc uptake by FM3A variants showed no significant correlation with their metastatic potential. In addition, N-acetyl-D-[1-14C]glucosamine, 2-deoxy-D-[1-14C]glucose and [6-3H]thymidine failed to demonstrate any difference between tumors' metastatic variants in vivo.
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PMID:Investigation of tumor metastatic potential with N-[18F]fluoroacetyl-D-glucosamine. 139 95

A murine monoclonal antibody, VM-1, which binds to basal cells of normal human epidermis, reduces the ability of human squamous cell carcinoma cells (SCL-1) derived from the skin to attach and spread on collagen by about 50% and causes cell rounding. Similar effects have been previously shown using normal human keratinocytes. The attachment of cell lines derived from human lung squamous cell carcinomas (SW1271 and SW900), melanoma A375, glioblastoma 126, and fibrosarcoma HT1080 is also inhibited by this antibody. VM-1 antibody does not bind to normal human fibroblasts, benign nevus cells, or the human B-cell-derived line 8866. VM-1 antibody inhibits the growth of SCL-1 cells in vitro as measured by cell numbers and [3H]thymidine ([3H]TdR) incorporation. It is not cytolytic in the presence of complement as measured by 51Cr release. Repeated treatment of SCL-1 cells with VM-1 antibody significantly reduces the proportion of SCL-1 cells that attach to collagen. In addition, after treatment of SCL-1 cells with VM-1 antibody, several proteins can no longer be demonstrated by gel electrophoresis of the cell-free supernatant. The VM-1 antibody effect on attachment and spreading is partially reversed by pretreatment of the collagen surface with laminin and fibronectin, but not with the carbohydrates chondroitin-6-sulfate or hyaluronic acid or with the protein lysozyme. By fluorescence staining, the antigen recognized by VM-1 antibody is membrane-bound and Triton X-100 extractable. The VM-1 antigen is excluded from Bio-Sil TSK-400 and sediments at about 10.5 S. It has a covalent molecular weight on the order of 10(6). Proteinase K digestion produces VM-1 antibody reactive fragments, assumed to be polysaccharides, with a polydisperse molecular weight distribution in the range 5000 to 30,000. The VM-1 antigen is partially lost from solution on boiling and is no longer detectable in the aqueous or organic phase after chloroform-methanol extraction. The properties of the VM-1 antigen are consistent with those of a proteoglycan involved in attachment and spreading of keratinocytes and certain tumor cells on collagen.
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PMID:Inhibition of attachment and growth of tumor cells on collagen by a monoclonal antibody. 369 49

Skin fibroblasts incorporated into a lattice of hydrated collagen contract it to form a tissue-like structure. Fibroblasts from patients with skin diseases, including psoriasis, epidermolysis bullosa, and scleroderma, and from control subjects, all showed a similar ability to contract the lattice. The established skin epithelial cell line NCTC 2544, melanoma cells, and 3T6 mouse fibroblasts produced little contraction. Contraction required the presence of serum and was unaffected by the addition of fibronectin (10-20 micrograms/ml). Hyaluronic acid at 50-500 micrograms/ml had no effect, but contraction was inhibited at 1 mg/ml.
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PMID:Contraction of collagen lattices by skin fibroblasts from dystrophic recessive epidermolysis bullosa and other dermatoses. 376 Jun 13

Circulating macrophages and metastatic tumor cells can penetrate the vascular endothelium and migrate from the circulatory system to extravascular compartments. Both activated murine macrophages and different metastatic tumor cells (B16-BL6 melanoma; ESb T-lymphoma) attach, invade, and penetrate confluent vascular endothelial cell monlayer in vitro, by degrading heparan sulfate proteoglycans in the subendothelial extracellular matrix. The sensitivity of the enzymes from the various sources degrading the heparan sulfate proteoglycan was challenged and compared by a series of inhibitors. Activated macrophages demonstrate a heparanase with an endoglycosidase activity that cleaves from the [35S]O4 = -labeled heparan sulfate proteoglycans of the extracellular matrix 10 kDa glycosaminoglycan fragments. The macrophages do not store the heparanase intracellularly but it is instead found pericellularly and requires a continuous cell-matrix contact at the optimal pH for maintaining cell growth. The degradation of [35S]O4 = -labeled extracellular matrix proteoglycans by the macrophages' heparanase is significantly inhibited in the presence of heparan sulfate (10 micrograms/ml), arteparon (10 micrograms/ml), and heparin at a concentration of 3 micrograms/ml. In contrast, other glycosaminoglycans such as hyaluronic acid, dermatan sulfate, and chondroitin sulfate as well as the specific inhibitor of exo-beta-glucuronidase D-saccharic acid 1,4-lactone failed to inhibit the degradation of sulfated proteoglycans in the subendothelial extracellular matrix. Degradation of this heparan sulfate proteoglycan is a two-step sequential process involving protease activity followed by heparanase activity. However, the following antiproteases--alpha 2-macroglobulin, antithrombin III, leupeptin, and phenylmethylsulfony fluoride (PMSF)--failed to inhibit this degradation process, and only alpha 1-antitrypsin inhibited the heparanase activity. B16-BL6 metastatic melanoma cell heparanase, which is also a cell-associated enzyme, was inhibited by heparin to the same extent as the macrophage heparanase. On the other hand, heparanase of the highly metastatic variant (ESb) of a methylcholanthrene-induced T lymphoma, which is an extracellular enzyme released by the cells to the incubation medium, was more sensitive to heparin and arteparon than the macrophages' heparanase, inhibited at concentrations of 1 and 3 micrograms/ml, respectively. These results may indicate the potential use of heparin or other glycosaminoglycans as specific and differential inhibitors for the formation in certain cases of blood-borne tumor metastasis.
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PMID:Murine macrophage heparanase: inhibition and comparison with metastatic tumor cells. 380 31

The human tumor cell lines, MM-96, FME, HCT-8, HT-29, MCF-7 and T-47D, in culture produced a factor or factors able to stimulate glycosaminoglycan (GAG) synthesis in human skin fibroblasts (HF). Conditioned growth media from the melanoma MM-96 and the colon carcinoma HT-29 produced a 10- and 8-fold stimulation of HF GAG synthesis, respectively, with an even larger stimulation of hyaluronic acid. Conditioned media from the melanoma FME and the breast carcinomas MCF-7 and T-47D stimulated GAG synthesis 2-fold, whereas media from the colon carcinoma HCT-8 gave a variable response often with no effect on GAG levels. Conditioned media from HF cultures had no effect on tumor cell GAG synthesis. Coculture of tumor cells and HF also resulted in increased GAG synthesis, and the degree of stimulation was similar to that with the conditioned media. Tumor cell-conditioned media were also effective in stimulating GAG synthesis by porcine smooth muscle cells and by chick embryo fibroblasts in culture, although the increase in GAG synthesis was much less than with HF cultures. These findings support the concept that the stromal desmoplasia characteristic of many growing and invasive tumors in vivo arises by tumor cell modulation of GAG synthesis by surrounding normal connective tissue cells.
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PMID:Human tumor cells in culture stimulate glycosaminoglycan synthesis by human skin fibroblasts. 401 Feb 30

Glycosaminoglycan (GAG) synthesis of B-16 melanoma metastatic variants was examined in vivo and in vitro to begin to assess the relationship between the presence of these polymers and the process of primary invasion and metastasis. The variants that were examined for GAG production included the F-1 line that exhibits low metastatic potential, the F-10 line selected for high metastatic potential, and the BL6 line selected for high invasiveness. The F-1 cell line was routinely less invasive than the F-10 and BL6 lines when injected s.c. into the legs of irradiated Swiss Webster mice. All cell lines formed palpable tumors after s.c. injection, but histological sections revealed early and extensive invasion in only F-10 and BL6 tumors. The F-1 tumors were surrounded by a connective tissue capsule and did not begin to invade into host tissue until this structure disappeared approximately 16 days after injection of tumor cells. Some consistent alterations in GAG synthesis, particularly the release of hyaluronic acid and heparan sulfate, were observed among the cell lines in vivo and in vitro, although differences observed in vitro were small and variable. In vivo all tumors were surrounded by a hyaluronic acid-rich zone that was concentrated at the tumor-stromal interface and was transitory. Hyaluronate occurred as a diffuse band around BL6 and F-10 tumors but was confined to a capsule surrounding the less aggressive F-1 tumor. In vitro the BL6 and F-10 cell lines released larger amounts of heparan sulfate and hyaluronic acid than did the F-1 cell line. Differences in release of chondroitin sulfate by the cell lines were not observed. Differences in trypsin-releasable GAG, presumably associated with the glycocalyx, were also not apparent. These results link the release in vitro and organization in vivo of hyaluronic acid and heparan sulfate to invasion and metastasis.
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PMID:Glycosaminoglycan production by murine melanoma variants in vivo and in vitro. 402 88

Monoclonal antibody (Mab) 9.2.27 was utilized in a combination of biosynthetic and biochemical investigations as an immunological probe for the study of chondroitin sulfate proteoglycans (CSP) in human melanoma cells. Pulse-chase and long-term intrinsic labeling immunoprecipitation experiments combined with the biosynthetic inhibitors monensin, cycloheximide, and paranitrophenol-beta-D-xyloside all suggest that Mab 9.2.27 recognizes a set of glycoprotein molecules ranging to a 250-kDa glycoprotein which serves as the core glycoprotein for CSP in human melanoma cells. Peptide maps comparing the 250-kDa and CSP molecule verify that the 250-kDa glycoprotein is the CSP core protein in human melanoma cells. Further studies document that the CSP released by melanoma cells and recognized by Mab 9.2.27 contains (2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-beta-4-O-sulfo-D-galactose and 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-beta-6-O-sulfo-D-galactose saccharides and this CSP can interact with hyaluronic acid-Sepharose. Topographical studies indicate that this CSP has pericellular punctuated distribution on the melanoma cell surface and may play a role in cell-substrate interactions in the biology of metastatic human melanoma.
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PMID:Biosynthetic studies of proteoglycans in human melanoma cells with a monoclonal antibody to a core glycoprotein of chondroitin sulfate proteoglycans. 638 1


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