Literature DB >> 8463221

Ricin-resistant Madin-Darby canine kidney cells missort a major endogenous apical sialoglycoprotein.

A Le Bivic1, M Garcia, E Rodriguez-Boulan.   

Abstract

gp114 is a major sialoglycoprotein expressed on the apical membrane of Madin-Darby canine kidney (MDCK) II cells. We investigated its distribution in two lectin-resistant mutant cell lines derived from MDCKII cells, MDCKII-RCAr and MDCKII-ConAr cells. gp114 was present on the apical membrane of MDCKII-ConAr cells but was predominantly basolateral in MDCKII-RCAr cells. No change of polarity was observed for several apical and basolateral markers in this cell line. Reversal of polarity of gp114 mainly resulted from a modification of its intracellular sorting. gp114 showed altered endocytosis in MDCKII-RCAr cells. In MDCKII cells gp114 was slowly endocytosed, whereas in MDCKII-RCAr cells endocytosis of gp114 was highly increased. Using mannosidase I and II inhibitors we found that N-glycosylation only slightly affects gp114 sorting and endocytosis. Our results suggest that gp114 or an associated component in MDCK-RCAr fails to express apical information or that a mutation creates a basolateral sorting signal which could be related to endocytic signals.

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Year:  1993        PMID: 8463221

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  9 in total

Review 1.  Role of N-glycosylation in trafficking of apical membrane proteins in epithelia.

Authors:  Olga Vagin; Jeffrey A Kraut; George Sachs
Journal:  Am J Physiol Renal Physiol       Date:  2008-10-29

Review 2.  Apical trafficking in epithelial cells: signals, clusters and motors.

Authors:  Ora A Weisz; Enrique Rodriguez-Boulan
Journal:  J Cell Sci       Date:  2009-12-01       Impact factor: 5.285

Review 3.  Trafficking to the apical and basolateral membranes in polarized epithelial cells.

Authors:  Emily H Stoops; Michael J Caplan
Journal:  J Am Soc Nephrol       Date:  2014-03-20       Impact factor: 10.121

4.  Characterization of Pseudomonas aeruginosa-induced MDCK cell injury: glycosylation-defective host cells are resistant to bacterial killing.

Authors:  G Apodaca; M Bomsel; R Lindstedt; J Engel; D Frank; K E Mostov; J Wiener-Kronish
Journal:  Infect Immun       Date:  1995-04       Impact factor: 3.441

5.  Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer.

Authors:  I R Nabi; E Rodriguez-Boulan
Journal:  Mol Biol Cell       Date:  1993-06       Impact factor: 4.138

6.  Induction of caveolae in the apical plasma membrane of Madin-Darby canine kidney cells.

Authors:  P Verkade; T Harder; F Lafont; K Simons
Journal:  J Cell Biol       Date:  2000-02-21       Impact factor: 10.539

7.  Sialylation of N-linked glycans mediates apical delivery of endolyn in MDCK cells via a galectin-9-dependent mechanism.

Authors:  Di Mo; Simone A Costa; Gudrun Ihrke; Robert T Youker; Nuria Pastor-Soler; Rebecca P Hughey; Ora A Weisz
Journal:  Mol Biol Cell       Date:  2012-08-01       Impact factor: 4.138

8.  Identification of glycosylated marker proteins of epithelial polarity in MDCK cells by homology driven proteomics.

Authors:  Joachim Füllekrug; Anna Shevchenko; Andrej Shevchenko; Kai Simons
Journal:  BMC Biochem       Date:  2006-03-13       Impact factor: 4.059

9.  GalNAc-alpha-O-benzyl inhibits NeuAcalpha2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells.

Authors:  G Huet; S Hennebicq-Reig; C de Bolos; F Ulloa; T Lesuffleur; A Barbat; V Carrière; I Kim; F X Real; P Delannoy; A Zweibaum
Journal:  J Cell Biol       Date:  1998-06-15       Impact factor: 10.539

  9 in total

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