Document Detail


Sialidases in vertebrates: a family of enzymes tailored for several cell functions.
MedLine Citation:
PMID:  20837202     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
Eugenio Monti; Erik Bonten; Alessandra D'Azzo; Roberto Bresciani; Bruno Venerando; Giuseppe Borsani; Roland Schauer; Guido Tettamanti
Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Advances in carbohydrate chemistry and biochemistry     Volume:  64     ISSN:  0065-2318     ISO Abbreviation:  Adv Carbohydr Chem Biochem     Publication Date:  2010  
Date Detail:
Created Date:  2010-09-14     Completed Date:  2011-01-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0240537     Medline TA:  Adv Carbohydr Chem Biochem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  403-79     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
Affiliation:
Department of Biomedical Science and Biotechnology, University of Brescia, Italy.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Cell Physiological Processes*
Computational Biology
Humans
Neoplasms / enzymology,  pathology
Neuraminidase / chemistry,  genetics,  immunology,  metabolism*
Vertebrates*
Chemical
Reg. No./Substance:
EC 3.2.1.18/Neuraminidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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