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
Download PDFAnalyze on Scholarcy
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
Overexpression of Plasma Membrane-associated Sialidase Attenuates Insulin Signaling in Transgenic Mice*
A. Sasaki (2003)
Glycoprotein glycosylation and cancer progression.
J. Dennis (1999)
Determination of sialic acids in human serum by reversed-phase liquid chromatography with fluorimetric detection.
K. Li (1992)
Plasma Membrane Ganglioside Sialidase Regulates Axonal Growth and Regeneration in Hippocampal Neurons in Culture
J. Rodríguez (2001)
Neoplastic Alteration of a Membrane‐associated Sialidase of Rat Liver
T. Miyagi (1990)
Sialidase and malignancy: A minireview
T. Miyagi (2004)
Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles.
K. Yamaguchi (2006)
Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis.
E. Bonten (1996)
Evidence for mitochondrial localization of a novel human sialidase (NEU4).
K. Yamaguchi (2005)
Expression of cDNA encoding the human “protective protein≓ associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases
N. Galjart (1988)
The Plasma Membrane-associated Sialidase MmNEU3 Modifies the Ganglioside Pattern of Adjacent Cells Supporting Its Involvement in Cell-to-Cell Interactions*
N. Papini (2004)
Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family.
E. Monti (2004)
Sialidase NEU3 is a peripheral membrane protein localized on the cell surface and in endosomal structures.
G. Zanchetti (2007)
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)
A Close Association of the Ganglioside-specific Sialidase Neu3 with Caveolin in Membrane Microdomains*
Y. Wang (2002)
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)
Down‐regulation of sialidase NEU4 may contribute to invasive properties of human colon cancers
H. Yamanami (2007)
The Elastin Receptor Complex Transduces Signals through the Catalytic Activity of Its Neu-1 Subunit*
L. Duca (2007)
Metastatic potential of transformed rat 3Y1 cell lines is inversely correlated with lysosomal‐type sialidase activity
T. Miyagi (1994)
Lysosomal Sialidase (Neuraminidase-1) Is Targeted to the Cell Surface in a Multiprotein Complex That Facilitates Elastic Fiber Assembly*
A. Hinek (2006)
Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis
A. Pshezhetsky (1997)
3.17 – Sialic Acids
T. Miyagi (2007)
Tumor‐promoting Phorbol Ester Induces Alterations of Sialidase and Sialyltransferase Activities of JB6 Cells
T. Miyagi (1990)
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)
Fusion of the NUP98 gene with the LEDGF/p52 gene defines a recurrent acute myeloid leukemia translocation
D. Hussey (2001)
Biochemical and immunological studies on two distinct ganglioside-hydrolyzing sialidases from the particulate fraction of rat brain.
T. Miyagi (1990)
Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane.
E. Monti (2000)
Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
Y. Kakugawa (2002)
Rat-liver lysosomal sialidase. Solubilization, substrate specificity and comparison with the cytosolic sialidase.
T. Miyagi (1984)
A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells
T. Wada (2007)
Glycosylation defining cancer malignancy: New wine in an old bottle
S. Hakomori (2002)
Asymmetric membrane ganglioside sialidase activity specifies axonal fate
Jorge Santos Da Silva (2005)
Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases.
E. Monti (1999)
Cloning, expression, and chromosomal mapping of a human ganglioside sialidase.
T. Wada (1999)
Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex*
C. Milner (1997)
Plasma Membrane-associated Sialidase Is Up-regulated in Renal Cell Carcinoma and Promotes Interleukin-6-induced Apoptosis Suppression and Cell Motility*
S. Ueno (2006)
Neu4, a Novel Human Lysosomal Lumen Sialidase, Confers Normal Phenotype to Sialidosis and Galactosialidosis Cells*
V. Seyrantepe (2004)
Overexpression of lysosomal‐type sialidase leads to suppression of metastasis associated with reversion of malignant phenotype in murine B16 melanoma cells
T. Kato (2001)
Conserved sequences in bacterial and viral sialidases
P. Roggentin (2005)
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)
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
Mammalian Sialidase Assays
T. Miyagi (2014)
Mechanisms of cancer-associated glycosylation changes.
F. Dall'Olio (2012)
Sphingolipids and metabolic disease
L. Cowart (2011)
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)
Gangliosides and cell surface ganglioside glycohydrolases in the nervous system.
M. Aureli (2014)
Serum Sialic Acid as a Biomarker in Liver Disease
Ewa Gruszewska (2015)
Regulation of Sialyl Lewis Antigen Expression in Colon Cancer Cells by Sialidase NEU4*
K. Shiozaki (2011)
Gangliosides in Cancer Cell Signaling.
S. Groux-Degroote (2018)
Remodeling of Sphingolipids by Plasma Membrane Associated Enzymes
M. Aureli (2010)
Antimetastatic therapy targeting aberrant sialylation profiles in cancer cells
D. Lu (2011)
Glycoprofiling Investigation of Hepatocellular Carcinoma Cell Surface With Lectin Microarray*: Glycoprofiling Investigation of Hepatocellular Carcinoma Cell Surface With Lectin Microarray*
Qun He (2010)
Membrane restructuring following in situ sialidase digestion of gangliosides: Complex model bilayers by synchrotron radiation reflectivity.
V. Rondelli (2017)
Exploration of the Sialic Acid World
R. Schauer (2018)
Novel Insulin Receptor-Signaling Platform
Fiona Haxho (2014)
Interaction of Sialyltransferases, Sialidases, and Sialic Acids in Liver Diseases and Applications to Biomarker Discovery
Ahmet Ata Alturfan (2016)
Sialic Acid-Binding Lectin from Bullfrog Eggs Exhibits an Anti-Tumor Effect Against Breast Cancer Cells Including Triple-Negative Phenotype Cells
Takeo Tatsuta (2018)
Naringenin suppresses Edwardsiella tarda infection in GAKS cells by NanA sialidase inhibition
Sayaka Shinyoshi (2017)
Implications for the mammalian sialidases in the physiopathology of skeletal muscle
A. Fanzani (2012)
Sialic acid attenuates puromycin aminonucleoside-induced desialylation and oxidative stress in human podocytes.
I. Pawluczyk (2014)
Sialidase NEU3 Dynamically Associates to Different Membrane Domains Specifically Modifying Their Ganglioside Pattern and Triggering Akt Phosphorylation
D. Bonardi (2014)
Development of Antimetastatic Drugs by Targeting Tumor Sialic Acids
Da-yong Lu (2012)
NEU3 (sialidase 3 (membrane sialidase))
K. Yamaguchi (2011)
Sialic acids in T cell development and function.
S. Bi (2009)
Leczyme: A New Candidate Drug for Cancer Therapy
Takeo Tatsuta (2014)
Deregulation of sialidases in human normal and tumor tissues.
M. Forcella (2018)
Advances in membrane proteomics and cancer biomarker discovery: current status and future perspective.
Hem D Shukla (2012)
Glycosylation enzyme mRNA expression in dorsolateral prefrontal cortex of elderly patients with schizophrenia: Evidence for dysregulation of multiple glycosylation pathways
Toni M. Mueller (2018)
Activation of apoptosis inhibitor of macrophage is a sensitive diagnostic marker for NASH-associated hepatocellular carcinoma
N. Koyama (2017)
Role of Galectin-3 in Cancer Metastasis
Joana Oliveira (2015)
NEU4L sialidase overexpression promotes β‐catenin signaling in neuroblastoma cells, enhancing stem‐like malignant cell growth
C. Tringali (2012)
An Oncogenic Protein Golgi Phosphoprotein 3 Up-regulates Cell Migration via Sialylation*
T. Isaji (2014)See more