Nerve growth factor effects on human and mouse melanoma cell invasion and heparanase production

Marchetti, Dario; Menter, David G.; Li, Jin; Nakajima, Motowo; Gl, Nicolson

doi:10.1002/ijc.2910550430

Cited by 84 publications

(98 citation statements)

References 24 publications

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“…B16B15b or 70W melanoma cells were used as a source of heparanase activity (7,27). We have previously shown that 1) these brainmetastatic clones possess higher heparanase content than their respective murine (B16F1) or human (MeWo) parental counterparts, and 2) the heparanase activity is indistinguishable in these two cellular sources by the two heparanase assays used in the present studies (7,27,29). Briefly, subconfluent cells were harvested and solubilized in 50 mM Tris-HCl, pH 7.5, 0.05% (w/v) sodium azide, 0.5% (v/v) Triton X-100 for 30 min at 4°C.…”

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confidence: 67%

“…Alternatively, heparanase activity was determined by high speed gel permeation chromatography (38) with some modifications (27). B16B15b or 70W melanoma cells were used as a source of heparanase activity (7,27). We have previously shown that 1) these brainmetastatic clones possess higher heparanase content than their respective murine (B16F1) or human (MeWo) parental counterparts, and 2) the heparanase activity is indistinguishable in these two cellular sources by the two heparanase assays used in the present studies (7,27,29).…”

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confidence: 91%

“…Heparanase activity by gel permeation chromatography decreased in the area of the high M r half of intact radiolabeled HS peak and correlated with incubation time. Only data within a linear range for relative activity measurements were taken into account, with relative degradation activity determined by the amount of radiolabeled HS degraded/ min/ g of protein (7). By performing these heparanase analyses using cellular extracts from subconfluent murine (B16B15b) or human (70W) cells, we have determined heparanase activity, whether from murine or human sources, to behave identically toward the substrate as already reported (7,29).…”

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confidence: 99%

“…Indeed, HSPG catabolism is observed in inflammation, wound repair, diabetes, and cancer metastasis, suggesting that enzymes that degrade the HS chains play important roles in pathologic processes (3, 4). Furthermore, malignant cells are capable of modulating cellular interactions with HSPGs by producing and releasing a HS-degrading enzyme, heparanase (3,7,27,28). Recently, we reported that purified, high M r subpopulations of cell surface HS were more sensitive to heparanase action than secreted HS (29).…”

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confidence: 99%

“…Important ECM targets for degradation by invading melanoma cells are the heparan sulfate (HS) chains found on proteoglycans (3,6,7). HS are highly negatively charged linear polysaccharides consisting of alternating residues of uronic acids and glucosamine.…”

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Heparanase and a Synthetic Peptide of Heparan Sulfate-interacting Protein Recognize Common Sites on Cell Surface and Extracellular Matrix Heparan Sulfate

Marchetti¹,

Liu²,

Spohn³

et al. 1997

Journal of Biological Chemistry

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Metastasis occurs via a sequential and complex series of interactions between tumor cells and normal host cells and tissues (1, 2). During the formation of metastases, migrating cells are confronted by natural tissue barriers, such as connective tissue stroma and basal lamina (2, 3). The ability of malignant cells to penetrate these barriers depends upon the presence of enzymes capable of degrading extracellular matrix (ECM) 1 components (1-5). For these reasons, considerable effort has been focused on the study of tissue-degradative enzymes produced and secreted by metastatic tumor cells as well as normal cells of the tissue being invaded.Important ECM targets for degradation by invading melanoma cells are the heparan sulfate (HS) chains found on proteoglycans (3, 6, 7). HS are highly negatively charged linear polysaccharides consisting of alternating residues of uronic acids and glucosamine. Proteins containing one or more covalently attached HS chains are called HS proteoglycans (HSPGs). The dynamic role of HSPGs in biology has become increasingly apparent (8 -23). As a result of characterizing heparin (HP) and HS binding sites related to the initial attachment of trophoblast cells to uterine epithelial cells of murine and human origin, we recently reported the cell surface expression and molecular cloning of a novel HP/HS-interacting protein (HIP) of human epithelial and endothelial cells (24 -26). HIP not only recognizes HS and HP in a highly specific fashion, but it also binds a subset of HP and forms of HS enriched at cell surfaces and in ECM. In contrast, HIP does not bind intracellular or secreted forms of HS. Furthermore, HIP also appears to bind the anticoagulantly active species of HP efficiently and with high affinity. 2 HP octasaccharides, but not hexasaccharides, are large enough to bind HIP with high affinity. Thus, HIP appears to recognize a motif that at least overlaps the anticoagulant motif in HP and HS chains.In light of the above findings, activities that mediate HSPG degradation are expected to have significant regulatory consequences. Indeed, HSPG catabolism is observed in inflammation, wound repair, diabetes, and cancer metastasis, suggesting that enzymes that degrade the HS chains play important roles in pathologic processes (3, 4). Furthermore, malignant cells are capable of modulating cellular interactions with HSPGs by producing and releasing a HS-degrading enzyme, heparanase (3,7,27,28). Recently, we reported that purified, high M r subpopulations of cell surface HS were more sensitive to heparanase action than secreted HS (29). In the present study, we have investigated the relationship between tumor (melanoma) heparanase activity and HIP binding in HS subpopulations whether on the cell surface, secreted, or deposited in the ECM. By use of sensitive heparanase assays that separate

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Heparanase and a Synthetic Peptide of Heparan Sulfate-interacting Protein Recognize Common Sites on Cell Surface and Extracellular Matrix Heparan Sulfate

Marchetti¹,

Liu²,

Spohn³

et al. 1997

Journal of Biological Chemistry

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Neurotrophins and Trk receptors in human pancreatic ductal adenocarcinoma: Expression patterns and effects onIn vitro invasive behavior

Miknyoczki¹,

Lang²,

Huang³

et al. 1999

Int. J. Cancer

171

125

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Correlation of overexpression of the low-affinity p75 neurotrophin receptor with augmented invasion and heparanase production in human malignant melanoma cells

1999

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The role of growth factor receptors in regulating the progression of human melanocytes toward tumorigenicity and ultimately a malignant phenotype is poorly understood. In particular, the autocrine and paracrine influences that modulate cellular invasion and extracellular matrix (ECM)‐degradative enzymes in melanoma cells remain undefined at the molecular level. The low‐affinity p75 neurotrophin receptor (p75NTR), a cysteine‐rich transmembrane glycoprotein, is frequently expressed in advanced stages of human melanoma, but the biological consequences of this expression are unknown. p75NTR can enhance the invasive potential of brain‐metastatic melanoma cells in vitro. We have extended here these results and related the level of p75NTR in human metastatic melanoma cells to their invasive potential to target organs other than brain. Fluorescence activated cell sorting (FACS) analysis showed that 3 melanoma cell lines (SK‐MEL‐146, SK‐MEL‐119, 70W) had differential p75NTR contents, whereas SK‐MEL‐147 cells had elevated amounts of p75NTR. Two other melanoma cell lines (SK‐MEL‐94, SK‐MEL‐110) with point mutations in the p75NTR transmembrane domain had reduced (SK‐MEL‐94) or absent (SK‐MEL‐110) p75NTR. We also examined these cell lines for presence of TrkA receptor, the high‐affinity receptor for nerve growth factor (NGF), the prototypic neurotrophin. No TrkA receptor expression was detected in any of the cell lines. The extent of p75NTR expression correlated with the capability of NGF to promote cellular invasion and with production of heparanase, an important ECM‐degradative enzyme. Melanoma cells sorted for high p75NTR expression (p75NTR‐H cells) had markedly greater (9‐ to 13‐fold increase) invasive capabilities in response to NGF exposure than those sorted for low p75NTR expression (p75NTR‐L cells). Additionally, NGF induced a 8‐ to 10‐fold increase of heparanase activity in p75NTR‐H cells. Thus, we propose that p75NTR‐mediated trophic support profoundly affects melanoma cell invasion to neurotrophin‐rich organs. Int. J. Cancer 82:112–120, 1999. © 1999 Wiley‐Liss, Inc.

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Nerve growth factor effects on human and mouse melanoma cell invasion and heparanase production

Cited by 84 publications

References 24 publications

Heparanase and a Synthetic Peptide of Heparan Sulfate-interacting Protein Recognize Common Sites on Cell Surface and Extracellular Matrix Heparan Sulfate

Heparanase and a Synthetic Peptide of Heparan Sulfate-interacting Protein Recognize Common Sites on Cell Surface and Extracellular Matrix Heparan Sulfate

Neurotrophins and Trk receptors in human pancreatic ductal adenocarcinoma: Expression patterns and effects onIn vitro invasive behavior

Correlation of overexpression of the low-affinity p75 neurotrophin receptor with augmented invasion and heparanase production in human malignant melanoma cells

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