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J Biol Chem, Vol. 274, Issue 30, 21375-21386, July 23, 1999
From the Complex Carbohydrate Research Center and the Department of
Biochemistry and Molecular Biology, University of Georgia,
Athens, Georgia 30602
We have isolated a full-length
cDNA clone encoding a human 
1,2-mannosidase that catalyzes the
first mannose trimming step in the processing of mammalian Asn-linked
oligosaccharides. This enzyme has been proposed to regulate the timing
of quality control glycoprotein degradation in the endoplasmic
reticulum (ER) of eukaryotic cells. Human expressed sequence tag clones
were identified by sequence similarity to mammalian and yeast
oligosaccharide-processing mannosidases, and the full-length coding
region of the putative mannosidase homolog was isolated by a
combination of 5'-rapid amplification of cDNA ends and direct
polymerase chain reaction from human placental cDNA. The open
reading frame predicted a 663-amino acid type II transmembrane
polypeptide with a short cytoplasmic tail (47 amino acids), a single
transmembrane domain (22 amino acids), and a large COOH-terminal
catalytic domain (594 amino acids). Northern blots detected a
transcript of ~2.8 kilobase pairs that was ubiquitously expressed in
human tissues. Expression of an epitope-tagged full-length form of the
human mannosidase homolog in normal rat kidney cells resulted in an ER
pattern of localization. When a recombinant protein, consisting of
protein A fused to the COOH-terminal luminal domain of the human
mannosidase homolog, was expressed in COS cells, the fusion protein was
found to cleave only a single 1,2-mannose residue from
Man9GlcNAc2 to produce a unique
Man8GlcNAc2 isomer (Man8B). The mannose
cleavage reaction required divalent cations as indicated by inhibition with EDTA or EGTA and reversal of the inhibition by the addition of
Ca2+. The enzyme was also sensitive to inhibition by
deoxymannojirimycin and kifunensine, but not swainsonine. The results
on the localization, substrate specificity, and inhibitor
profiles indicate that the cDNA reported here encodes an enzyme
previously designated ER mannosidase I. Enzyme reactions using a
combination of human ER mannosidase I and recombinant Golgi mannosidase
IA indicated that that these two enzymes are complementary in their
cleavage of Man9GlcNAc2 oligosaccharides to
Man5GlcNAc2.
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