Probing the CMP-Sialic Acid Donor Specificity of Two Human ß-d-Galactoside Sialyltransferases (ST3Galâ
I and ST6Galâ
I) Selectively Acting on O- and N-Glycosylproteins.
Chembiochem
; 18(13): 1251-1259, 2017 07 04.
Article
em En
| MEDLINE
| ID: mdl-28395125
ABSTRACT
Sialylation of glycoproteins and glycolipids is catalyzed by sialyltransferases in the Golgi of mammalian cells, whereby sialic acid residues are added at the nonreducing ends of oligosaccharides. Because sialylated glycans play critical roles in a number of human physio-pathological processes, the past two decades have witnessed the development of modified sialic acid derivatives for a better understanding of sialic acid biology and for the development of new therapeutic targets. However, nothing is known about how individual mammalian sialyltransferases tolerate and behave towards these unnatural CMP-sialic acid donors. In this study, we devised several approaches to investigate the donor specificity of the human ß-d-galactoside sialyltransferases ST6Galâ
I and ST3Galâ
I by using two CMP-sialic acids CMP-Neu5Ac, and CMP-Neu5N-(4pentynoyl)neuraminic acid (CMP-SiaNAl), an unnatural CMP-sialic acid donor with an extended and functionalized N-acyl moiety.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Polissacarídeos
/
Ácidos Siálicos
/
Sialiltransferases
/
Glicolipídeos
/
Glicoproteínas
/
Antígenos CD
/
Monofosfato de Citidina
/
Ácido N-Acetilneuramínico do Monofosfato de Citidina
Limite:
Humans
Idioma:
En
Revista:
Chembiochem
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
França