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Altered Expression of Sialidases in Human Cancer

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Biochemical Roles of Eukaryotic Cell Surface Macromolecules

Part of the book series: Advances in Experimental Medicine and Biology ((volume 749))

Abstract

Sialidases are glycosidases catalyzing the removal of α-glycosidically linked sialic acid residues from carbohydrate groups of glycoproteins and glycolipids, which is the initial step in degradation of the glycoconjugates. Four types of human sialidases have been identified, characterized, and designated as NEU1, NEU2, NEU3, and NEU4, according to their major subcellular localization and enzymatic properties. Each sialidase has been found to play a unique role depending on its particular properties. The present review briefly summarizes mainly our recent results on aberrant expression and pathological roles of human sialidases in cancer.

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References

  • Bigi A, Morosi L, Pozzi C, Forcella M, Tettamanti G, Venerando B, Monti E, Fusi P (2010) Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively. Glycobiology 20:148–157

    Article  PubMed  CAS  Google Scholar 

  • Bonten E, van der Spoel A, Fornerod M, Grosveld G, d’Azzo A (1996) Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis. Genes Dev 10:3156–3169

    Article  PubMed  CAS  Google Scholar 

  • Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S (2005) Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition. J Biol Chem 280:469–475

    PubMed  CAS  Google Scholar 

  • Dennis JW, Granovsky M, Warren CE (1999) Glycoprotein glycosylation and cancer progression. Biochim Biophys Acta 1473:21–34

    Article  PubMed  CAS  Google Scholar 

  • Duca L, Blanchevoye C, Cantarelli B, Ghoneim C, Dedieu S, Delacoux F, Hornebeck W, Hinek A, Martiny L, Debelle L (2007) The elastin receptor complex transduces signals through the catalytic activity of its Neu-1 subunit. J Biol Chem 282:12484–12491

    Article  PubMed  CAS  Google Scholar 

  • Galjart NJ, Gillemans N, Harris A, van der Horst, Verheijen FW, d’Azzo A (1988) Expression of cDNA encoding the human “protective protein” associated with lysosomal β-galactosidase and neuraminidase: homology to yeast proteases. Cell 54:755–764

    Google Scholar 

  • Hakomori S (2002) Glycosylation defining cancer malignancy: new wine in an old bottle. Proc Natl Acad Sci USA 99:10231–10233

    Article  PubMed  CAS  Google Scholar 

  • Hata K, Koseki K, Yamaguchi K, Moriya S, Suzuki Y, Yingsakmongkon S, Hirai G, Sodeoka M, von Itzstein M, Miyagi T (2008) Limited inhibitory effects of oseltamivir and zanamivir on human sialidases. Antimicrob Agent Chemother 52:3484–3491

    Article  CAS  Google Scholar 

  • Hinek A, Pshezhetsky AV, von Itzstein M, Starcher B (2006) Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly. J Biol Chem 281:3698–3710

    Article  PubMed  CAS  Google Scholar 

  • Kakugawa Y, Wada T, Yamaguchi K, Yamanami H, Ouchi K, Sato I, Miyagi T (2002) Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Proc Natl Acad Sci USA 99:10718–10723

    Article  PubMed  CAS  Google Scholar 

  • Kato K, Shiga K, Yamaguchi K, Hata K, Kobayashi T, Miyazaki K, Saijo S, Miyagi T (2006) Plasma membrane-associated sialidase (NEU3) differentially regulates integrin-mediated cell proliferation through laminin- and fibronectin-derived signaling. Biochem J 394:647–656

    Article  PubMed  CAS  Google Scholar 

  • Kawamura S, Sato I, Wada T, Yamaguchi K, Li Y, Li D, Zhao X, Ueno S, Aoki H, Tochigi T, Kuwahara M, Kitagawa T, Takahashi K, Moriya S, Miyagi T (2012) Plasma membrane-associated sialidase (NEU3) regulates progression of prostate cancer to androgen-independent growth through modulation of androgen receptor signaling. Cell Death Differ 19(1):170–179

    Google Scholar 

  • Liang F, Seyrantepe V, Landry K, Ahmad R (2006) 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. J Biol Chem 281:27526–27538

    Article  PubMed  CAS  Google Scholar 

  • Mandal C, Tringali C, Mondal S, Anastasia L, Chandra S, Venerando B, Mandal C (2010) Down regulation of membrane-bound Neu3 constitutes a new potential marker for childhood acute lymphoblastic leukemia and induces apoptosis suppression of neoplastic cells. Int J Cancer 126:337–349

    Article  PubMed  CAS  Google Scholar 

  • Meuillet EJ, Kroes R, Yamamoto H, Warner TG, Ferrari J, Mania-Farnell B, George D, Rebbaa A, Moskal JR, Bremer EG (1999) Sialidase gene transfection enhances epidermal growth factor receptor activity in an epidermoid carcinoma cell line, A431. Cancer Res 59:234–240

    PubMed  CAS  Google Scholar 

  • Milner CM, Smith SV, Carrillo MB, Taylor GL, Hollinshead M, Campbell RD (1997) Identification of a sialidase encoded in the human major histocompatibility complex. J Biol Chem 272: 4549–4558

    Article  PubMed  CAS  Google Scholar 

  • Miyagi T (2008) Aberrant expression of sialidase and cancer progression. Proc Jpn Acad Ser B 84:407–418

    Article  CAS  Google Scholar 

  • Miyagi T, Konno K, Emori Y, Kawasaki H, Suzuki K, Yasui A, Tsuiki S (1993) Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase. J Biol Chem 268:26435–26440

    PubMed  CAS  Google Scholar 

  • Miyagi T, Wada T, Iwamatsu A, Hata K, Yoshikawa Y, Tokuyama S, Sawada M (1999) Molecular cloning and characterization of plasma membrane- associated sialidase specific for gangliosides. J Biol Chem 274:5004–5011

    Article  PubMed  CAS  Google Scholar 

  • Miyagi T, Wada T, Yamaguchi K, Shiozaki K, Sato I, Yamanami H, Kakugawa Y, Fujiya T (2008a) Human sialidase as a cancer marker. Proteomics 8:3303–3311

    Article  PubMed  CAS  Google Scholar 

  • Miyagi T, Wada T, Yamaguchi K, Hata K, Shiozaki K (2008b) Minireview; Plasma membrane-associated sialidase as a crucial regulator of transmembrane signaling. Biochem J 394: 647–656

    Google Scholar 

  • Monti E, Preti A, Rossi E, Ballabio A, Borsani G (1999) Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Genomics 57:137–143

    Article  PubMed  CAS  Google Scholar 

  • Monti E, Bassi MT, Papini N, Riboni M, Manzoni M, Venerando B, Croci G, Preti A, Ballabio A, Tettamanti G, Borsani G (2000) Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane. Biochem J 349:343–351

    Google Scholar 

  • Monti E, Bassi MT, Bresciani R, Civini S, Croci GL, Papini N, Riboni M, Zanchetti G, Ballabio A, Preti A et al (2004) Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family. Genomics 83:445–453

    Article  PubMed  CAS  Google Scholar 

  • Pshezhetsky AV, Richard C, Michaud L, Igdoura S, Wang S, Elsliger MA, Qu J, Leclerc D, Gravel R, Dallaire L, Potier M (1997) Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis. Nat Genet 15:316–320

    Article  PubMed  CAS  Google Scholar 

  • Sawada M, Moriya S, Saito S, Shineha R, Satomi S, Yamori T, Tsuruo T, Kannagi R, Miyagi T (2002) Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression. Int J Cancer 97:180–185

    Article  PubMed  CAS  Google Scholar 

  • Seyrantepe V, Landry S, Trudel JA, Hassan JA, Morales CR, Pshezhetsky AV (2004) Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells. J Biol Chem 279:37021–37029

    Article  PubMed  CAS  Google Scholar 

  • Shiozaki K, Yamaguchi K, Sato I, Miyagi T (2009) Plasma membrane -associated sialidase (NEU3) promotes formation of colonic aberrant crypt foci in azoxymethane-treated transgenic mice. Cancer Sci 100:588–594

    Article  PubMed  CAS  Google Scholar 

  • Shiozaki K, Yamaguchi K, Takahashi K, Moriya S, Miyagi T (2011) Regulation of sialyl Lewis antigen expression in colon cancer cells by sialidase NEU4. J Biol Chem 286(24):21052–61

    Article  PubMed  CAS  Google Scholar 

  • Tokuyama S, Moriya S, Taniguchi S, Yasui A, Miyazaki J, Orikasa S, Miyagi T (1997) Suppression of pulmonary metastasis in murine B16 melanoma cells by transfection of a sialidase cDNA. Int J Cancer 73:410–415

    Article  PubMed  CAS  Google Scholar 

  • Tringali C, Lupo B, Anastasia L, Papini N, Monti E, Bresciani R, Tettamanti G, Venerando B (2007) Expression of sialidase Neu2 in leukemic K562 cells induces apoptosis by impairing Bcr-Abl/Src kinase signaling. J Biol Chem 282:14364–14372

    Article  PubMed  CAS  Google Scholar 

  • Uemura T, Shiozaki K, Yamaguchi K, Miyazaki S, Satomi S, Kato K, Sakuraba H, Miyagi T (2009) Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin β4. Oncogene 28:1218–1229

    Article  PubMed  CAS  Google Scholar 

  • Ueno S, Saito S, Wada T, Yamaguchi K, Satoh M, Arai Y, Miyagi T (2006) Plasma membrane-associated sialidase is up-regulated in renal cell carcinoma and promotes the interleukin-6 -induced apoptosis suppression and cell motility. J Biol Chem 281:7756–7764

    Article  PubMed  CAS  Google Scholar 

  • Wada T, Yoshikawa Y, Tokuyama S, Kuwabara M, Akita H, Miyagi T (1999) Cloning, expression and chromosomal mapping of a human ganglioside sialidase. Biochem Biophys Res Commun 261:21–27

    Article  PubMed  CAS  Google Scholar 

  • Wada T, Hata K, Yamaguchi K, Shiozaki K, Koseki K, Moriya S, Miyagi T (2007) A crucial role of plasma membrane-associated sialidase (NEU3) in the survival of human cancer cells. Oncogene 26:2483–2490

    Article  PubMed  CAS  Google Scholar 

  • Yamaguchi K, Hata K, Koseki K, Shiozaki AH, Wada T, Moriya S, Miyagi T (2005) Evidence for mitochondrial localization of a novel human sialidase (NEU4). Biochem J 390:85–93

    Google Scholar 

  • Yamaguchi K, Hata K, Wada T, Moriya S, Miyagi T (2006) Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles. Biochem Biophys Res Commun 346:484–490

    Article  PubMed  CAS  Google Scholar 

  • Yamanami H, Shiozaki K, Wada T, Yamaguchi K, Uemura T, Kakugawa Y, Fujiya T, Miyagi T (2007) Down-regulation of sialidase NEU4 may contribute to invasive properties of human colon cancers. Cancer Sci 98:299–307

    Article  PubMed  CAS  Google Scholar 

  • Zanchetti G, Colombi P, Manzoni AL, Caimi L, Borsani G, Venerando B, Tettamanti G, Preti A, Monti E, Bresciani R (2007) Sialidase NEU3 is a peripheral membrane protein localized on the cell surface and in endosomal structures. Biochem J 408:211–219

    Google Scholar 

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Authors and Affiliations

  1. Division of Cancer Glycosylation Research, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, 981-8558, Japan

    Taeko Miyagi, K. Takahashi, S. Moriya, K. Hata, K. Yamamoto & T. Wada

  2. Division of Pathology, Miyagi Cancer Centre, 47-1 Nodayama, Shiode, Medeshima, Natori, 981-1293, Japan

    T. Wada

  3. Division of Molecular and Cellular Oncology, Miyagi Cancer Centre Research Institute, 47-1 Nodayama, Shiode, Medeshima, Natori, 981-1293, Japan

    K. Yamaguchi

  4. Division of Marine Biochemistry, Kagoshima University, 4-50-20 Shimo-arata, Kagoshima, 890-0056, Japan

    K. Shiozaki

Authors
  1. Taeko Miyagi
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  2. K. Takahashi
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  3. S. Moriya
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  4. K. Hata
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  5. K. Yamamoto
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  6. T. Wada
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  7. K. Yamaguchi
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  8. K. Shiozaki
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Corresponding author

Correspondence to Taeko Miyagi .

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Editors and Affiliations

  1. Riverside Transit Campus, School of Biological Sciences, Central University of Kerala, Kasargod, 671328, Kerala, India

    Perumana R. Sudhakaran

  2. National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, 110067, Delhi, India

    Avadhesha Surolia

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Miyagi, T. et al. (2012). Altered Expression of Sialidases in Human Cancer. In: Sudhakaran, P., Surolia, A. (eds) Biochemical Roles of Eukaryotic Cell Surface Macromolecules. Advances in Experimental Medicine and Biology, vol 749. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3381-1_17

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