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Involvement of VIP36 in Intracellular Transport and Secretion of Glycoproteins in Polarized Madin-Darby Canine Kidney (MDCK) Cells
- Source :
- Journal of Biological Chemistry. 277:16332-16339
- Publication Year :
- 2002
- Publisher :
- Elsevier BV, 2002.
-
Abstract
- 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 approximately 2. Like VIP36, plasma membrane glycoproteins recognized by VIP36 were found in the apical and basolateral membranes in the ratio of approximately 2 to 1. In addition, secretory glycoproteins recognized by VIP36 were secreted approximately 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 approximately 2 to approximately 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).
- Subjects :
- Glycan
Golgi Apparatus
Kidney
Biochemistry
Cell Line
Dogs
Animals
Biotinylation
Secretion
Molecular Biology
Secretory pathway
Glycoproteins
Epithelial polarity
chemistry.chemical_classification
Membrane Glycoproteins
biology
Cell Membrane
Membrane Proteins
Membrane Transport Proteins
Lectin
Cell Biology
Apical membrane
Recombinant Proteins
Cell biology
Kinetics
Protein Transport
Membrane glycoproteins
Clusterin
Mannose-Binding Lectins
chemistry
biology.protein
Carrier Proteins
Glycoprotein
Molecular Chaperones
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 277
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....0d378fb2509689025ca981c5ce6d554a