NCAM (CD56)-Positive Malignant Lymphoma

Kern, W. F.; Spier, Catherine M.; Miller, Thomas P.; Grogan, Thomas M.

doi:10.3109/10428199309059565

Cited by 39 publications

(15 citation statements)

References 45 publications

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“…These studies are underway in our laboratory. PolySia is also expressed on numerous tumor cells (41)(42)(43)(44)(45) and is considered to be involved in metastasis via its anti-adhesive effect. Tumor cells with polySia are occasionally reported to re-express STX genes (40), and polySia on tumor cell surfaces might affect tumor cell growth via growth factors such as FGF2.…”

Section: Discussionmentioning

confidence: 99%

Novel Regulation of Fibroblast Growth Factor 2 (FGF2)-mediated Cell Growth by Polysialic Acid

Ono

Hane

Kitajima

et al. 2012

Journal of Biological Chemistry

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Background: Polysialic acid (polySia) binds neurological factors, BDNF and dopamine. Results: PolySia specifically binds FGF2 and inhibits the cell growth facilitated by signaling through a ternary complex of FGF2, FGFR, and heparan sulfate (HS). Conclusion: PolySia regulates the FGF2-mediated cell growth differently from HS. Significance: A new function of polySia to regulate the action of neurological factors is established.

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Section: Discussionmentioning

confidence: 99%

Novel Regulation of Fibroblast Growth Factor 2 (FGF2)-mediated Cell Growth by Polysialic Acid

Ono

Hane

Kitajima

et al. 2012

Journal of Biological Chemistry

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“…CMP-NeuAc synthetase-deficient mutants do not express sialylated glycoconjugates and can be complemented with functional CMP-NeuAc synthetase in both mammalian (1) and bacterial systems (2). Sialic acids participate in a myriad of signaling, recognition, and cell-cell adhesion phenomena in mammalian cells (3) and are overexpressed in some highly malignant tumors (4). Genetic disorders that lead to altered physiological levels of sialic acids have many consequences in humans and can be fatal (5).…”

mentioning

confidence: 99%

Structure of a Sialic Acid-activating Synthetase, CMP-acylneuraminate Synthetase in the Presence and Absence of CDP

Mosimann

Gilbert²,

Dombroswki

et al. 2001

Journal of Biological Chemistry

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The x-ray crystallographic structure of selenomethionyl cytosine-5-monophosphate-acylneuraminate synthetase (CMP-NeuAc synthetase) from Neisseria meningitidis has been determined at 2.0-Å resolution using multiple-wavelength anomalous dispersion phasing, and a second structure, in the presence of the substrate analogue CDP, has been determined at 2.2-Å resolution by molecular replacement. This work identifies the active site residues for this class of enzyme for the first time. The detailed interactions between the enzyme and CDP within the mononucleotide-binding pocket are directly observed, and the acylneuraminate-binding pocket has also been identified. A model of acylneuraminate bound to CMP-NeuAc synthetase has been constructed and provides a structural basis for understanding the mechanism of production of "activated" sialic acids. Sialic acids are key saccharide components on the surface of mammalian cells and can be virulence factors in a variety of bacterial species (e.g. Neisseria, Haemophilus, group B streptococci, etc.). As such, the identification of the bacterial CMP-NeuAc synthetase active site can serve as a starting point for rational drug design strategies.Cytosine-5Ј-monophosphate-acylneuraminate synthetase (cytosine-5Ј-monophosphate-N-acetyl neuraminic acid synthetase, CMP-NeuAc synthetase) 1 catalyzes the penultimate step in the addition of sialic acids to the oligosaccharide component of glycoconjugates and is a required component of sialylation pathways. CMP-NeuAc synthetase-deficient mutants do not express sialylated glycoconjugates and can be complemented with functional CMP-NeuAc synthetase in both mammalian (1) and bacterial systems (2). Sialic acids participate in a myriad of signaling, recognition, and cell-cell adhesion phenomena in mammalian cells (3) and are overexpressed in some highly malignant tumors (4). Genetic disorders that lead to altered physiological levels of sialic acids have many consequences in humans and can be fatal (5). In bacterial systems, sialic acids are less common and frequently have roles as virulence factors (6). In Neisseria gonorrhoeae, sialylated glycoconjugates protect the organism from phagocytosis and increase serum resistance (7). In Haemophilus ducreyi the presence of 2-keto-3-deoxy-manno-octulosonate-containing glycoconjugates correlate with the organism's pathogenicity (8). Likewise, the sialylated capsule of Neisseria meningitidis, Escherichia coli K1, and group B streptococci are virulence factors (9-11). It has been suggested that bacterial species produce sialylated glycoconjugates to mimic the host and escape detection by the immune system (12). Clearly, the mechanism of production of sialic acid-containing glycoconjugates is of clinical interest. Although bacterial and eucaryotic CMPNeuAc synthetase enzymes share many catalytic properties, several important differences have been reported, including substrate specificity, tertiary structure, inhibitor sensitivity, and cellular localization (13). As a result, bacterial CMP-NeuAc synthetase en...

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“…The ␣2,8-linked polySia glycotope is one such oncodevelopmental, tumor-associated antigen. The cell surface expression of polysialylated neural cell adhesion molecules is positively correlated with increased malignancy in a number of human tumors, including Wilms tumor (5), human neuroblastomas, some of which are metastatic to bone and brain (6,7), malignant lymphoma (8,9), acute myeloid leukemia (10), and in head and neck malignancies (11). The importance of the polySia glycotope in normal and malignantly transformed human tissues was recently reviewed (12).…”

mentioning

confidence: 99%

Identification of Free Deaminated Sialic Acid (2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid) in Human Red Blood Cells and Its Elevated Expression in Fetal Cord Red Blood Cells and Ovarian Cancer Cells

Inoue¹,

Lin²,

Chang³

et al. 1998

Journal of Biological Chemistry

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NCAM (CD56)-Positive Malignant Lymphoma

Cited by 39 publications

References 45 publications

Novel Regulation of Fibroblast Growth Factor 2 (FGF2)-mediated Cell Growth by Polysialic Acid

Novel Regulation of Fibroblast Growth Factor 2 (FGF2)-mediated Cell Growth by Polysialic Acid

Structure of a Sialic Acid-activating Synthetase, CMP-acylneuraminate Synthetase in the Presence and Absence of CDP

Identification of Free Deaminated Sialic Acid (2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid) in Human Red Blood Cells and Its Elevated Expression in Fetal Cord Red Blood Cells and Ovarian Cancer Cells

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