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J. Biol. Chem., Vol. 277, Issue 18, 16332-16339, May 3, 2002
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From the VIP36, an intracellular lectin that recognizes
high mannose-type glycans (Hara-Kuge, S., Ohkura, T., Seko, A., and
Yamashita, K. (1999) Glycobiology 9, 833-839), was shown
to localize not only to the early secretory pathway but also to the
plasma membrane of Madin-Darby canine kidney (MDCK) cells. In the
plasma membrane, VIP36 exhibited an apical-predominant distribution,
the apical/basolateral ratio being ~2. Like VIP36, plasma membrane
glycoproteins recognized by VIP36 were found in the apical and
basolateral membranes in the ratio of ~2 to 1. In addition, secretory
glycoproteins recognized by VIP36 were secreted ~2-fold more
efficiently from the apical membrane than from the basolateral
membrane. Thus, the apical/basolateral ratio of the transport of
VIP36-recognized glycoproteins was correlated with that of VIP36 in
MDCK cells. Upon overproduction of VIP36 in MDCK cells, the
apical/basolateral ratios of both VIP36 and VIP36-recognized
glycoproteins were changed from ~2 to ~4, and the secretion of
VIP36-recognized glycoproteins was greatly stimulated. In contrast to
the overproduction of VIP36, that of a mutant version of VIP36, which
has no lectin activity, was of no effect on the distribution of
glycoproteins to apical and basolateral membranes and inhibited the
secretion of VIP36-recognized glycoproteins. Furthermore, the
overproduction of VIP36 greatly stimulated the secretion of a major
apical secretory glycoprotein of MDCK cells, clusterin, which was found
to carry at least one high mannose-type glycan and to be recognized by
VIP36. In contrast to the secretion of clusterin, that of a
non-glycosylated apical-secretion protein, galectin-3, was not
stimulated through the overproduction of VIP36. These results indicated
that VIP36 was involved in the transport and sorting of glycoproteins
carrying high mannose-type glycan(s).
Involvement of VIP36 in Intracellular Transport and Secretion
of Glycoproteins in Polarized Madin-Darby Canine Kidney
(MDCK) Cells*
§,§,§
Department of Biochemistry, Sasaki
Institute, 2-2 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, § CREST (Core Research for Evolutional Science and
Technology) of the Japan Science and Technology Corporation (JST)
2-3 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, and the
¶ Department of Anatomy, Yamanashi-Medical University, 1110 Tamahocho, Nakakoma-gun, Yamanashi 409-3898, Japan
*
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.
To whom correspondence should be addressed: Dept. of
Biochemistry, Sasaki Institute, 2-2 Kanda-Surugadai, Chiyoda-ku,
Tokyo 101-0062, Japan. Tel.: 3-3294-3286; Fax: 3-3294-2656;
E-mail: yamashita@sasaki.or.jp.
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