Sialidase significance for cancer progression.
Aberrant glycosylation is a characteristic feature of cancer cells. In particular, altered sialylation is closely associated with malignant properties, including invasiveness and metastatic potential. To elucidate the molecular mechanisms underlying the aberrancy, our studies have focused on mammalian sialidase, which catalyzes the removal of sialic acid residues from glycoproteins and glycolipids. The four types of mammalian sialidase identified to date show altered expression and behave in different manners during carcinogenesis. The present review briefly summarizes results on altered expression of sialidases and their possible roles in cancer progression. These enzymes are indeed factors defining cancer malignancy and thus potential targets for cancer diagnosis and therapy.
Division of Cancer Glycosylation Research, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan. tmiyagi@tohoku-pharm.ac.jp
Taeko
T
Miyagi
Kohta
K
Takahashi
Keiko
K
Hata
Kazuhiro
K
Shiozaki
Kazunori
K
Yamaguchi
D000818:Animals; D015972:Gene Expression Regulation, Neoplastic; D006017:Glycolipids / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D009369:Neoplasms / Q000201:enzymology*; D009439:Neuraminidase / Q000235:genetics / Q000378:metabolism*
D006017:Glycolipids; D006023:Glycoproteins; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid