The polymeric immunoglobulin receptor. A model protein to study transcytosis.

Apodaca, Gerard; Bomsel, Morgane; Arden, James; Breitfeld, Philip P.; Tang, Kitty; Mostov, Keith E.

doi:10.1172/jci115211

Cited by 68 publications

(40 citation statements)

References 41 publications

(28 reference statements)

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“…HGF also reduces transcytosis of the pIgR (33). Basolateral recycling of dIgA by the pIgR was not affected by HGF treatment, suggesting that HGF treatment specifically alters the machinery necessary for efficient basolateral to apical translocation of dIgA.…”

Section: Discussionmentioning

confidence: 92%

Hepatocyte Growth Factor Alters the Polarity of Madin-Darby Canine Kidney Cell Monolayers

Balkovetz

Pollack²,

Mostov

1997

Journal of Biological Chemistry

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Hepatocyte growth factor (HGF) and E-cadherin are important for epithelial morphogenetic events. We examined the effects of HGF on E-cadherin localization and interaction with ␤-catenin in polarized MadinDarby canine kidney (MDCK) cell monolayers grown on filters. Surface biotinylation experiments showed that HGF increases apically accessible E-cadherin. Confocal immunofluorescence microscopy of HGF-treated cells showed localization of E-cadherin at membrane domains contacting the apical compartment and an increase in accessibility of apically applied antibodies to lateral E-cadherin below the tight junction. Coimmunoprecipitation of ␤-catenin/E-cadherin complexes showed that the amount of E-cadherin associated with ␤-catenin increased during the first 24 h of HGF treatment with a return to baseline values after 48 and 72 h. Metabolic labeling showed that HGF increased the synthetic rate of ␤-catenin and the amount of newly synthesized E-cadherin associated with immunoprecipitated ␤-catenin, with the peak effect occurring after 12 h of treatment and returning to baseline after 24 h. HGF treatment inhibited transcytosis of immunoglobulin A by the polymeric immunoglobulin receptor. We conclude that HGF treatment of polarized MDCK cells grown on filters decreases cell polarity and alters E-cadherin/␤-catenin interaction and synthesis.

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Section: Discussionmentioning

confidence: 92%

Hepatocyte Growth Factor Alters the Polarity of Madin-Darby Canine Kidney Cell Monolayers

Balkovetz

Pollack²,

Mostov

1997

Journal of Biological Chemistry

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“…Transcytosis is an important membrane trafficking process in polarized cells because it allows the exchange of molecules from one cell surface to the other in either direction (7,8). One example of apical to basolateral transcytosis is the Fc receptor (FcRn), which is delivered to the apical membrane of enterocytes and is then transcytosed to the basolateral domain.…”

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confidence: 99%

Detergent Insoluble Microdomains are not Involved in Transcytosis of Polymeric Ig Receptor in FRT and MDCK Cells

Sarnataro

Nitsch

Hunziker

et al. 2000

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In polarized epithelial cells, sorting of proteins and lipids to the apical or basolateral domain of the plasma membrane can occur via direct or indirect (transcytotic) pathways from the trans Golgi network (TGN). The 'rafts' hypothesis postulates that the key event for direct apical sorting of some transmembrane proteins and the majority of GPI-anchored proteins depends on their association with glycosphingolipid and cholesterol enriched microdomains (rafts). However, the mechanism of indirect sorting to the apical membrane is not clear. The polyimmunoglobulin receptor (pIgR) is one of the best studied proteins that follow the transcytotic pathway. It is normally delivered from the TGN to the basolateral surface of polarized Madin-Darby Canine Kidney (MDCK) cells from where it transports dIgA or dIgM to the apical surface. We have studied the intracellular trafficking of pIgR in Fischer rat thyroid cells (FRT), and have investigated the sorting machinery involved in transcytosis of this receptor in both FRT and MDCK cells. We found that, in contrast with MDCK cells, a significant amount ( 30%) of pIgR reaches the apical surface by a direct pathway. Furthermore, in both cell lines it does not associate with Triton X-100 insoluble microdomains, suggesting that at least in these cells 'rafts' are not involved in basolateral to apical transcytosis.

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“…For example, polyimmunoglobulin (Ig) receptors have been implicated in the transcytosis and secretion of polymeric IgA and IgM in mucosal epithelial cells (6,7). Further, neonatal FcR (FcRn) expressed on the apical cell surface binds IgG in milk for endocytosis and subsequent transcytosis to the basolateral cell surface (8 -12).…”

mentioning

confidence: 99%

Human IgGFc Binding Protein (FcγBP) in Colonic Epithelial Cells Exhibits Mucin-like Structure

Harada¹,

Iijima²,

Kobayashi³

et al. 1997

Journal of Biological Chemistry

104

127

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The polymeric immunoglobulin receptor. A model protein to study transcytosis.

Cited by 68 publications

References 41 publications

Hepatocyte Growth Factor Alters the Polarity of Madin-Darby Canine Kidney Cell Monolayers

Hepatocyte Growth Factor Alters the Polarity of Madin-Darby Canine Kidney Cell Monolayers

Detergent Insoluble Microdomains are not Involved in Transcytosis of Polymeric Ig Receptor in FRT and MDCK Cells

Human IgGFc Binding Protein (FcγBP) in Colonic Epithelial Cells Exhibits Mucin-like Structure

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