Neural cell surface differentiation antigen gp130<sup>RB13‐6</sup>induces fibroblasts and glioma cells to express astroglial proteins and invasive properties

Deissler, Helmut; Blass-Kampmann, Sabine; Bruyneel, Erik; Mareel, Marc; Rajewsky, Manfred F.

doi:10.1096/fasebj.13.6.657

Cited by 43 publications

(33 citation statements)

References 43 publications

(40 reference statements)

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“…[307] NPP1 has been linked to insulin resistance and type 2 diabetes (for review, see [334][335][336]). NPP3 has been shown to promote differentiation and invasion of glial cells but the underlying mechanisms have not been identified [337]. Moreover, the basophil and mast cell-expressed cell surface antigen CD203c was identified as NPP3 [338].…”

Section: General Properties and Functional Rolementioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: General Properties and Functional Rolementioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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“…However, to date, there have been few in vivo studies to elucidate whether the motility and differentiation e ects associated with these proteins could be physiologically relevant to tumor cells. Recently Deissler et al (1999) reported experiments in which B-10 cDNA was transfected into NIH3T3 and two rat glioma cell lines. Transfectants from the NIH3T3 cell line and one of the glioma lines displayed an altered cellular morphology and increased in vitro invasion into type I collagen gels.…”

Section: Lung Metastasis Incidencementioning

confidence: 99%

Autotaxin (ATX), a potent tumor motogen, augments invasive and metastatic potential of ras-transformed cells

et al. 2000

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Autotaxin (ATX), an exo-nucleotide pyrophosphatase and phosphodiesterase, was originally isolated as a potent stimulator of tumor cell motility. In order to study whether ATX expression a ects motility-dependent processes such as invasion and metastasis, we stably transfected full-length ATX cDNA into two nonexpressing cell lines, parental and ras-transformed NIH3T3 (clone7) cells. The e ect of ATX secretion on in vitro cell motility was variable. The ras-transformed, ATX-secreting subclones had enhanced motility to ATX as chemoattractant, but there was little di erence in the motility responses of NIH3T3 cells transfected with atx, an inactive mutant gene, or empty vector. In Matrigel TM invasion assays, all subclones, which secreted enzymatically active ATX, demonstrated greater spontaneous and ATX-stimulated invasion than appropriate controls. This di erence in invasiveness was not caused by di erences in gelatinase production, which was constant within each group of transfectants. In vivo studies with athymic nude mice demonstrated that injection of atx-transfected NIH3T3 cells resulted in a weak tumorigenic capacity with few experimental metastases. Combination of ATX expression with ras transformation produced cells with greatly ampli®ed tumorigenesis and metastatic potential compared to ras-transformed controls. Thus, ATX appears to augment cellular characteristics necessary for tumor aggressiveness.

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“…[8][9][10][11][12][13][14] These type II transmembrane proteins (N-terminus inside) are highly homologous within their extracellular domains but differ in their transmembrane and cytosolic domains. E-NPP1 was identified as a plasma cell differentiation antigen.…”

mentioning

confidence: 99%

“…11 E-NPP3 was cloned from rat embryonic neural cells 12 and its overexpression in 3T3 fibroblasts results in the up-regulation of glial fibrillary acidic protein. 13 In hematopoietic tissues, surface E-NPP3 is exclusively expressed on basophils, mast cells, and their progenitors. 1 Interestingly, E-NPP3 expression on basophils is up-regulated after stimulation with allergen or cross-linking with IgE.…”

mentioning

confidence: 99%

The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3

Bühring

Seiffert

Giesert

et al. 2001

Blood

131

112

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IntroductionIn an attempt to generate antibodies against surface antigens expressed on rare hematopoietic cell populations, monoclonal antibody (MoAb) 97A6 was raised, which selectively recognizes basophils, mast cells, and their CD34 ϩ precursor cells. 1 Stimulation of the basophils from donors allergic for acarids allergen with either anti-IgE antiserum or allergen results in a dose-dependent increase of 97A6 antigen expression, suggesting that the detected antigen plays an important role in cell activation. 1 Immunoprecipitation of the proteins recognized by MoAb 97A6 revealed 2 bands of 150 kd and 270 kd, respectively. 1 However, the identity of the molecule remained unknown. In this report, we show that 97A6 affinity-purified lysates consist of ectonucleotide pyrophosphatase phosphodiesterase-3 (E-NPP3), also termed phosphodiesterase I/nucleotide pyrophosphatase-3 (PDNP3), an ectoenzyme previously found in uterus, prostate, and glioma. [2][3][4] Study design Affinity purification of 97A6 antigenCoupling of purified MoAb 97A6 to an N-hydroxy succinimide (NHS)-activated Sepharose column (Pharmacia, Freiburg, Germany) was performed according to the manufacturer's recommendations. Lysates from 3 ϫ 10 9 KU-812 cells were loaded on a previously prepared 97A6-Sepharose affinity column equilibrated with washing buffer (10 mM Tris/HCl, 150 mM NaCl, 0.025% NaN 3 , 0.5% Triton X-100, pH 8.0). Bound 97A6 antigen was eluted with 50 mM triethanolamine, 0.1% Triton X-100, 150 mM NaCl, pH 11.5 and collected in tubes containing 1M Tris/HCl, pH 6.7. The collected fractions were screened on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for appearance of specific bands. In the next step, positive fractions were pooled and used for preparative separations on 7.5% SDS-PAGE. The proteins were visualized by silver staining and the resulting bands were cut for commercial microsequencing. This included tryptic digestion of the proteins, peptide mass fingerprint analysis (MALDI-MS), reverse phase-high-performance liquid chromatography (RP-HPLC), sequencing of the purified peptides, and search in the NCBI database (Toplab, Martinsried, Germany). Generation of E-NPP3 transfectant cell lineThe E-NPP3 complementary DNA (cDNA) was prepared and inserted into plasmids as described previously. 2 The calcium phosphate method was used for transfection of 293 embryonic kidney cells with 15 g plasmid. 5 Transfected cells were grown in tissue culture flasks in the presence of 0.5 mg/mL Geneticin. Six days after transfection the cells were stained with MoAb 97A6-phycoerythrin (PE) and the 97A6 ϩ fraction (9% of total cells) was sorted on a FACSVantage cell sorter (Becton Dickinson, Heidelberg, Germany). After 3 sorting rounds the cells stably expressed E-NPP3 on the cell surface. The transfectant cells were stained with MoAb 97A6-PE and analyzed on a FACSCalibur (Becton Dickinson). Purification of peripheral blood basophilsFicoll-Hypaque-selected buffy coat peripheral blood (PB) cells from healthy donors were stained with 97...

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Neural cell surface differentiation antigen gp130^RB13‐6induces fibroblasts and glioma cells to express astroglial proteins and invasive properties

Cited by 43 publications

References 43 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Autotaxin (ATX), a potent tumor motogen, augments invasive and metastatic potential of ras-transformed cells

The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3

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Neural cell surface differentiation antigen gp130RB13‐6induces fibroblasts and glioma cells to express astroglial proteins and invasive properties

Cited by 43 publications

References 43 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Autotaxin (ATX), a potent tumor motogen, augments invasive and metastatic potential of ras-transformed cells

The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3

Contact Info

Product

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About

Neural cell surface differentiation antigen gp130^RB13‐6induces fibroblasts and glioma cells to express astroglial proteins and invasive properties