Sialylation processes in mitochondria: evidence for two distinct sialyltransferases located in the outer membrane.

Abstract:

:Previous studies have shown that purified mitochondrial outer membrane is able to catalyze the transfer of sialic acid from CMP-Neu5Ac to an exogenous asialoglycoprotein acceptor, asialofetuin. Considering the heterogeneity of the glycan chains borne by this glycoprotein, an investigation of mitochondrial sialyltransferase activities was undertaken. Our data provide evidence for the existence of two distinct sialyltransferases in purified mitochondrial outer membranes. The use of different acceptor substrates, the temperature dependence of these enzymes, and their different sensitivity towards a sulfhydryl reagent, p-CMB, allowed us to discriminate between a galactoside alpha(2-3) sialyltransferase and a galactoside alpha(2-6) sialyltransferase presumably involved in the sialylation of O- and N-glycan chains of glycoprotein, respectively. These results are discussed in terms of mitochondrial autonomy for post-translational events.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Gasnier F,Baubichon-Cortay H,Louisot P,Gateau-Roesch O

doi

10.1093/oxfordjournals.jbchem.a123644

subject

Has Abstract

pub_date

1991-11-01 00:00:00

pages

702-7

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

110

pub_type

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