title: Sialidases in vertebrates: a family of enzymes tailored for several cell functions.
abstract: This review summarizes the recent research development on vertebrate sialidase biology. Sialic acid-containing compounds play important roles in many physiological processes, including cell proliferation, apoptosis and differentiation, control of cell adhesion, immune surveillance, and clearance of plasma proteins. In this context, sialidases, the glycohydrolases that remove the terminal sialic acid at the non-reducing end of various glycoconjugates, perform an equally pivotal function. Sialidases in higher organisms are differentially expressed in cells and tissues/organs, with particular subcellular distribution and substrate specificity: they are the lysosomal (NEU1), the cytosolic (NEU2), and plasma membrane- and intracellular-associated sialidases (NEU3 and NEU4). The molecular cloning of several mammalian sialidases since 1993 has boosted research in this field. Here we summarize the results obtained since 2002, when the last general review on the molecular biology of mammalian sialidases was written. In those few years many original papers dealing with different aspects of sialidase biology have been published, highlighting the increasing relevance of these enzymes in glycobiology. Attention has also been paid to the trans-sialidases, which transfer sialic acid residues from a donor sialoconjugate to an acceptor asialo substrate. These enzymes are abundantly distributed in trypanosomes and employed to express pathogenicity, also in humans. There are structural similarities and strategic differences at the level of the active site between the mammalian sialidases and trans-sialidases. A better knowledge of these properties may permit the design of better anti-pathogen drugs.
authors.affiliation: Department of Biomedical Science and Biotechnology, University of Brescia, Italy.
authors.forename: Eugenio
authors.initials: E
authors.lastname: Monti
authors.forename: Erik
authors.initials: E
authors.lastname: Bonten
authors.forename: Alessandra
authors.initials: A
authors.lastname: D'Azzo
authors.forename: Roberto
authors.initials: R
authors.lastname: Bresciani
authors.forename: Bruno
authors.initials: B
authors.lastname: Venerando
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Borsani
authors.forename: Roland
authors.initials: R
authors.lastname: Schauer
authors.forename: Guido
authors.initials: G
authors.lastname: Tettamanti
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002468:Cell Physiological Phenomena; D019295:Computational Biology; D006801:Humans; D009369:Neoplasms / Q000201:enzymology / Q000473:pathology; D009439:Neuraminidase / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D014714:Vertebrates
chemical_list: D009439:Neuraminidase