Involvement of VIP36 in Intracellular Transport and Secretion of Glycoproteins in Polarized Madin-Darby Canine Kidney (MDCK) Cells

• Published in: The Journal of biological chemistry Vol. 277; no. 18; pp. 16332 - 16339
• Main Authors: Hara-Kuge, Sayuri, Ohkura, Takashi, Ideo, Hiroko, Shimada, Osamu, Atsumi, Saoko, Yamashita, Katsuko
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 03.05.2002; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Biotinylation; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cell Line; Cell Membrane - metabolism; Clusterin; Dogs; Glycoproteins - analysis; Glycoproteins - biosynthesis; Golgi Apparatus - metabolism; Kidney; Kinetics; Mannose-Binding Lectins; Membrane Glycoproteins - metabolism; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membrane Transport Proteins; Molecular Chaperones - analysis; Molecular Chaperones - biosynthesis; Protein Transport; Recombinant Proteins - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M112188200

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).