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Vol. 273, Issue 2, 981-988, January 9, 1998
From the Glycobiology Program, La Jolla Cancer Research Center, The
Burnham Institute, La Jolla, California 92037 and
§ Division of Ultrastructural Pathology and Cell Biology,
Institute of Clinical Pathology, University of Vienna, A-1090,
Vienna, Austria
Previously, it has been shown that glycoproteins
with ~130-kDa molecular mass react with antisera from patients with
renal vasculitis (Kain, R., Matsui, K., Exner, M., Binder, S.,
Schaffner, G., Sommer, E. M., and Kerjaschki, D. (1995) J. Exp. Med. 181, 585-597). To search for a molecule that reacts
with the antibodies, we screened a 
gt11 human placental cDNA
library. Two of the isolated clones were found to encode a putative
counterpart of the rodent trans-Golgi network (TGN)
glycoprotein 38, hTGN46, which has the tyrosine containing motif YQRL
shared by mouse and rat TGN38. Moreover, reverse
transcription-polymerase chain reaction analysis of hTGN46
transcripts and genomic analysis of a cDNA deposited as an
expressed sequence tag in dbEST Data Base revealed that additional
cDNAs exist that are produced by alternate usage of 3
-splice sites
of intron III. Alternative splicing results in frame shifts and leads
to novel larger translation products with one (for hTGN48) or two (for
hTGN51) additional tyrosine-containing motifs. hTGN51 expressed in
Chinese hamster ovary cells were localized to the
trans-Golgi network, overlapping with
-1,4-galactosyltransferase even after mutating the
tyrosine-containing motif common to hTGN46. In contrast, mutated hTGN48
and hTGN46 are no longer retrieved to the TGN. These results strongly
suggest that hTGN51 may have a unique function compared with hTGN46 or
hTGN48 in shuttling between the cell surface and the TGN.
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