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Human Sialidase As A Cancer Marker.

T. Miyagi, T. Wada, K. Yamaguchi, K. Shiozaki, Ikuro Sato, Y. Kakugawa, H. Yamanami, T. Fujiya
Published 2008 · Biology, Medicine

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Altered sialylation of cell surface glycoproteins and glycolipids is closely related to the malignant phenotype of cancer cells, including the metastatic potential and invasiveness. Many cancer-related antigens in clinical use contain sialic acids at the terminal position of sugar chains in the molecules. To elucidate the molecular mechanism, we focused our investigation on sialidase, which catalyzes the removal of sialic acid residues from the glycoconjugates. Four types of human sialidases identified to date behave in different manners during carcinogenesis. One of the sialidases, found in the lysosomes, showed downregulation in cancers, promoting anchorage-independent growth, and metastatic ability, while another, found in the plasma membrane, showed marked upregulation, causing apoptosis suppression. It was found that estimation of the mRNA levels of sialidases by real-time PCR allowed discrimination of cancerous from noncancerous tissues and even determination of the pathological stage in some cancers. Immunohistochemistry of cancer tissues using the antibody against the plasma membrane sialidase was useful for clinical diagnosis. This paper briefly summarizes our findings of the altered sialidase expression in cancers and the possibility of their clinical application as cancer markers. Human sialidases are indeed related to malignancy and may be potential targets for cancer diagnosis and therapy.
This paper references
10.1074/JBC.M212200200
Overexpression of Plasma Membrane-associated Sialidase Attenuates Insulin Signaling in Transgenic Mice*
A. Sasaki (2003)
10.1016/S0304-4165(99)00167-1
Glycoprotein glycosylation and cancer progression.
J. Dennis (1999)
10.1016/0378-4347(92)80384-3
Determination of sialic acids in human serum by reversed-phase liquid chromatography with fluorimetric detection.
K. Li (1992)
10.1523/JNEUROSCI.21-21-08387.2001
Plasma Membrane Ganglioside Sialidase Regulates Axonal Growth and Regeneration in Hippocampal Neurons in Culture
J. Rodríguez (2001)
10.1111/j.1349-7006.1990.tb02667.x
Neoplastic Alteration of a Membrane‐associated Sialidase of Rat Liver
T. Miyagi (1990)
10.1023/B:GLYC.0000024250.48506.bf
Sialidase and malignancy: A minireview
T. Miyagi (2004)
10.1016/J.BBRC.2006.05.136
Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles.
K. Yamaguchi (2006)
10.1101/gad.10.24.3156
Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis.
E. Bonten (1996)
10.1042/BJ20050017
Evidence for mitochondrial localization of a novel human sialidase (NEU4).
K. Yamaguchi (2005)
10.1016/S0092-8674(88)90999-3
Expression of cDNA encoding the human “protective protein≓ associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases
N. Galjart (1988)
10.1074/JBC.M400881200
The Plasma Membrane-associated Sialidase MmNEU3 Modifies the Ganglioside Pattern of Adjacent Cells Supporting Its Involvement in Cell-to-Cell Interactions*
N. Papini (2004)
10.1016/J.YGENO.2003.08.019
Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family.
E. Monti (2004)
10.1042/BJ20070503
Sialidase NEU3 is a peripheral membrane protein localized on the cell surface and in endosomal structures.
G. Zanchetti (2007)
10.1074/jbc.M605633200
Monocyte Differentiation Up-regulates the Expression of the Lysosomal Sialidase, Neu1, and Triggers Its Targeting to the Plasma Membrane via Major Histocompatibility Complex Class II-positive Compartments*
F. Liang (2006)
10.1074/JBC.M110515200
A Close Association of the Ganglioside-specific Sialidase Neu3 with Caveolin in Membrane Microdomains*
Y. Wang (2002)
10.1023/A:1020269326825
Modulation of Neuritogenesis by Ganglioside-Specific Sialidase (Neu 3) in Human Neuroblastoma NB-1 Cells
S. Proshin (2004)
Sialidase activity in transformed cells.
C. Schengrund (1973)
10.1111/j.1349-7006.2007.00403.x
Down‐regulation of sialidase NEU4 may contribute to invasive properties of human colon cancers
H. Yamanami (2007)
10.1074/jbc.M609505200
The Elastin Receptor Complex Transduces Signals through the Catalytic Activity of Its Neu-1 Subunit*
L. Duca (2007)
10.1016/0014-5793(94)00682-2
Metastatic potential of transformed rat 3Y1 cell lines is inversely correlated with lysosomal‐type sialidase activity
T. Miyagi (1994)
10.1074/jbc.M508736200
Lysosomal Sialidase (Neuraminidase-1) Is Targeted to the Cell Surface in a Multiprotein Complex That Facilitates Elastic Fiber Assembly*
A. Hinek (2006)
10.1038/ng0397-316
Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis
A. Pshezhetsky (1997)
10.1016/B978-044451967-2/00055-6
3.17 – Sialic Acids
T. Miyagi (2007)
10.1111/j.1349-7006.1990.tb02692.x
Tumor‐promoting Phorbol Ester Induces Alterations of Sialidase and Sialyltransferase Activities of JB6 Cells
T. Miyagi (1990)
10.1021/bi00681a017
Cell contact-dependent ganglioside changes in mouse 3T3 gibroblasts and a suppressed sialidase activity on cell contact.
G. Yogeeswaran (1975)
Purification and characterization of cytosolic sialidase from rat liver.
T. Miyagi (1985)
10.1186/1471-2156-2-20
Fusion of the NUP98 gene with the LEDGF/p52 gene defines a recurrent acute myeloid leukemia translocation
D. Hussey (2001)
10.1093/oxfordjournals.jbchem.a123126
Biochemical and immunological studies on two distinct ganglioside-hydrolyzing sialidases from the particulate fraction of rat brain.
T. Miyagi (1990)
10.1042/0264-6021:3490343
Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane.
E. Monti (2000)
10.1073/pnas.152597199
Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
Y. Kakugawa (2002)
10.1111/j.1432-1033.1984.tb08159.x
Rat-liver lysosomal sialidase. Solubilization, substrate specificity and comparison with the cytosolic sialidase.
T. Miyagi (1984)
10.1038/sj.onc.1210341
A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells
T. Wada (2007)
10.1073/pnas.172380699
Glycosylation defining cancer malignancy: New wine in an old bottle
S. Hakomori (2002)
10.1038/nn1442
Asymmetric membrane ganglioside sialidase activity specifies axonal fate
Jorge Santos Da Silva (2005)
10.1006/GENO.1999.5749
Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases.
E. Monti (1999)
10.1006/BBRC.1999.0973
Cloning, expression, and chromosomal mapping of a human ganglioside sialidase.
T. Wada (1999)
10.1074/jbc.272.7.4549
Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex*
C. Milner (1997)
10.1074/jbc.M509668200
Plasma Membrane-associated Sialidase Is Up-regulated in Renal Cell Carcinoma and Promotes Interleukin-6-induced Apoptosis Suppression and Cell Motility*
S. Ueno (2006)
10.1074/JBC.M404531200
Neu4, a Novel Human Lysosomal Lumen Sialidase, Confers Normal Phenotype to Sialidosis and Galactosialidosis Cells*
V. Seyrantepe (2004)
10.1002/ijc.1268
Overexpression of lysosomal‐type sialidase leads to suppression of metastasis associated with reversion of malignant phenotype in murine B16 melanoma cells
T. Kato (2001)
10.1007/BF01047853
Conserved sequences in bacterial and viral sialidases
P. Roggentin (2005)
10.3727/000000006783981035
Expression of NEU3 (plasma membrane-associated sialidase) in clear cell adenocarcinoma of the ovary: its relationship with T factor of pTNM classification.
H. Nomura (2006)
10.1002/ijc.1598
Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression
Masashi Sawada (2002)



This paper is referenced by
10.1007/978-4-431-54836-2_189-1
Mammalian Sialidase Assays
T. Miyagi (2014)
10.2741/3951
Mechanisms of cancer-associated glycosylation changes.
F. Dall'Olio (2012)
10.1007/978-1-4614-0650-1
Sphingolipids and metabolic disease
L. Cowart (2011)
10.1016/S0065-2318(10)64007-3
Sialidases in vertebrates: a family of enzymes tailored for several cell functions.
E. Monti (2010)
Structural studies on the sialidases from Streptococcus pneumoniae and Pseudomonas aeruginosa
Guogang Xu (2009)
10.1007/978-1-4939-1154-7_10
Gangliosides and cell surface ganglioside glycohydrolases in the nervous system.
M. Aureli (2014)
10.1007/978-94-007-7742-2_11-1
Serum Sialic Acid as a Biomarker in Liver Disease
Ewa Gruszewska (2015)
10.1074/jbc.M111.231191
Regulation of Sialyl Lewis Antigen Expression in Colon Cancer Cells by Sialidase NEU4*
K. Shiozaki (2011)
10.1016/bs.pmbts.2017.10.003
Gangliosides in Cancer Cell Signaling.
S. Groux-Degroote (2018)
10.1007/s11064-010-0360-7
Remodeling of Sphingolipids by Plasma Membrane Associated Enzymes
M. Aureli (2010)
10.4081/DTS.2011.E12
Antimetastatic therapy targeting aberrant sialylation profiles in cancer cells
D. Lu (2011)
10.3724/SP.J.1206.2009.00622
Glycoprofiling Investigation of Hepatocellular Carcinoma Cell Surface With Lectin Microarray*: Glycoprofiling Investigation of Hepatocellular Carcinoma Cell Surface With Lectin Microarray*
Qun He (2010)
10.1016/j.bbamem.2017.01.012
Membrane restructuring following in situ sialidase digestion of gangliosides: Complex model bilayers by synchrotron radiation reflectivity.
V. Rondelli (2017)
10.1016/bs.accb.2018.09.001
Exploration of the Sialic Acid World
R. Schauer (2018)
10.23937/2377-3634/1410005
Novel Insulin Receptor-Signaling Platform
Fiona Haxho (2014)
10.1007/978-94-007-7742-2_19-1
Interaction of Sialyltransferases, Sialidases, and Sialic Acids in Liver Diseases and Applications to Biomarker Discovery
Ahmet Ata Alturfan (2016)
10.3390/molecules23102714
Sialic Acid-Binding Lectin from Bullfrog Eggs Exhibits an Anti-Tumor Effect Against Breast Cancer Cells Including Triple-Negative Phenotype Cells
Takeo Tatsuta (2018)
10.1016/j.fsi.2016.12.018
Naringenin suppresses Edwardsiella tarda infection in GAKS cells by NanA sialidase inhibition
Sayaka Shinyoshi (2017)
10.1186/2044-5040-2-23
Implications for the mammalian sialidases in the physiopathology of skeletal muscle
A. Fanzani (2012)
10.1016/j.yexcr.2013.10.017
Sialic acid attenuates puromycin aminonucleoside-induced desialylation and oxidative stress in human podocytes.
I. Pawluczyk (2014)
10.1371/journal.pone.0099405
Sialidase NEU3 Dynamically Associates to Different Membrane Domains Specifically Modifying Their Ganglioside Pattern and Triggering Akt Phosphorylation
D. Bonardi (2014)
10.3797/scipharm.1205-01
Development of Antimetastatic Drugs by Targeting Tumor Sialic Acids
Da-yong Lu (2012)
10.4267/2042/44984
NEU3 (sialidase 3 (membrane sialidase))
K. Yamaguchi (2011)
10.1016/j.bbagen.2009.07.027
Sialic acids in T cell development and function.
S. Bi (2009)
10.1155/2014/421415
Leczyme: A New Candidate Drug for Cancer Therapy
Takeo Tatsuta (2014)
10.3233/CBM-170548
Deregulation of sialidases in human normal and tumor tissues.
M. Forcella (2018)
10.1002/pmic.201100519
Advances in membrane proteomics and cancer biomarker discovery: current status and future perspective.
Hem D Shukla (2012)
10.1101/369314
Glycosylation enzyme mRNA expression in dorsolateral prefrontal cortex of elderly patients with schizophrenia: Evidence for dysregulation of multiple glycosylation pathways
Toni M. Mueller (2018)
10.1007/s00535-017-1398-y
Activation of apoptosis inhibitor of macrophage is a sensitive diagnostic marker for NASH-associated hepatocellular carcinoma
N. Koyama (2017)
10.4137/GBI.S13916
Role of Galectin-3 in Cancer Metastasis
Joana Oliveira (2015)
10.1002/ijc.27450
NEU4L sialidase overexpression promotes β‐catenin signaling in neuroblastoma cells, enhancing stem‐like malignant cell growth
C. Tringali (2012)
10.1074/jbc.M113.542688
An Oncogenic Protein Golgi Phosphoprotein 3 Up-regulates Cell Migration via Sialylation*
T. Isaji (2014)
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