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Originally published In Press as doi:10.1074/jbc.M004935200 on July 27, 2000

J. Biol. Chem., Vol. 275, Issue 41, 31655-31660, October 13, 2000
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Characterization of a cDNA Encoding a Novel Human Golgi alpha 1,2-Mannosidase (IC) Involved in N-Glycan Biosynthesis*

Linda O. TremblayDagger and Annette Herscovics§

From the McGill Cancer Centre, McGill University, Montréal, Québec H3G 1Y6, Canada

A human cDNA encoding a 70.9-kDa type II membrane protein with sequence similarity to class I alpha 1,2-mannosidases was isolated. The enzymatic properties of the novel alpha 1,2-mannosidase IC were studied by expressing its catalytic domain in Pichia pastoris as a secreted glycoprotein. alpha 1,2-Mannosidase IC sequentially hydrolyzes the alpha 1,2-linked mannose residues of [3H]mannose-labeled Man9GlcNAc to form [3H]Man6GlcNAc and a small amount of [3H]Man5GlcNAc. The enzyme requires calcium for activity and is inhibited by both 1-deoxymannojirimycin and kifunensine. The order of mannose removal was determined by separating oligosaccharide isomers formed from pyridylaminated Man9GlcNAc2 by high performance liquid chromatography. The terminal alpha 1,2-linked mannose residue from the middle branch is the last mannose removed by the enzyme. This residue is the mannose cleaved from Man9GlcNAc2 by the endoplasmic reticulum alpha 1,2-mannosidase I to form Man8GlcNAc2 isomer B. The order of mannose hydrolysis from either pyridylaminated Man9GlcNAc2 or Man8GlcNAc2 isomer B differs from that previously reported for mammalian Golgi alpha 1,2-mannosidases IA and IB. The full-length alpha 1,2-mannosidase IC was localized to the Golgi of MDBK and MDCK cells by indirect immunofluorescence. Northern blot analysis showed tissue-specific expression of a major transcript of 3.8 kilobase pairs. The expression pattern is different from that of human Golgi alpha 1,2-mannosidases IA and IB. Therefore, the human genome contains at least three differentially regulated Golgi alpha 1,2-mannosidase genes encoding enzymes with similar, but not identical specificities.

* This work was supported by an operating grant from the Medical Research Council of Canada.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF261655.

Dagger Recipient of a scholarship for graduate studies from the Medical Research Council of Canada.

§ To whom correspondence should be addressed: McGill Cancer Center, 3655 Promenade Sir-William-Osler, Montréal, Québec, Canada H3G 1Y6. Tel.: 514-398-3533; Fax: 514-398-6769; E-mail: annette@ med.mcgill.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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