Sialobiology: Structure, Biosynthesis and Function Sialic Acid Glycoconjugates in Health and Disease

by

Joe Tiralongo, Ivan Martinez-Duncker

DOI: 10.2174/97816080538651130101
eISBN: 978-1-60805-386-5, 2013
ISBN: 978-1-60805-067-3



Indexed in: Scopus, EBSCO.

This eBook presents a summary of central aspects of sialobiology (i.e., the study of sialic acid and its relevance to biology). The im...[view complete introduction]
US $
Buy Personal eBook
89
Order Library eBook
356
Order Printed Copy
*206
Order PDF + Printed Copy (Special Offer)
*250

*(Excluding Mailing and Handling)

🔒Secure Checkout Personal information is secured with SSL technology
Download Flyer

CMP-Sialic Acid Transporter

- Pp. 115-138 (24)

Andrea Maggioni, Ivan Martinez-Duncker and Joe Tiralongo

Abstract

Sialylation reactions take place in the lumen of the Golgi apparatus where sialyltransferases (STs) decorate glycan moieties of both the cell surfaces associated and secreted proteins and lipids with sialic acids (Sia) predominantly, but not exclusively employing, CMP-Neu5Ac as donor substrate. Because of its physical and chemical properties, CMP-Neu5Ac is unable to diffuse across the Golgi membrane and must be translocated from the cell cytosol into the lumen of the Golgi apparatus. Such translocation is performed by the CMP-Sia transporter, a member of an evolutionary conserved family of proteins together referred to as nucleotide sugar transporters. Although several nucleotide sugar transporters, including the CMP-Sia transporter, have been biochemically characterized over the last 30 years, the lack of a three-dimensional structure of any nucleotide sugar transporter requires alternative approaches to elucidating the structure-function relationship of this class of protein. We describe in this chapter the latest data reporting the elucidation of CMP-Sia transporter structurefunction relationship.

Purchase Chapter  Book Details

Advertisement


Webmaster Contact: info@benthamscience.net Copyright © 2019 Bentham Science