Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes.

Apodaca, Gerard; Katz, L A; Mostov, Keith E.

doi:10.1083/jcb.125.1.67

Cited by 358 publications

(490 citation statements)

References 47 publications

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“…Neutralizing Ab D47A (anti-gp120), stained green with FITC, was distributed through all three horizontal sections (apical and middle more than basal) with the most intensity in the middle section. As shown in the merged images, HIV gp160 and D47A IgA were prominently colocalized in the apical and especially the middle sections (orange to yellow), suggesting the principle site, perhaps in the apical recycling endosome (16,46), of interaction between IgA Ab and HIV protein. Both non-neutralizing D10A (anti-gp41) and irrelevant IgA (anti-measles hemagglutinin) showed no colocalization with HIV protein, suggesting little or no interaction with HIV protein even though both IgAs were transported efficiently to the apical side.…”

Section: Intracellular Colocalization Of Iga Ab and Viral Agmentioning

confidence: 91%

Intraepithelial Cell Neutralization of HIV-1 Replication by IgA

Huang

Wright

Gao

et al. 2005

The Journal of Immunology

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HIV is transmitted sexually through mucosal surfaces where IgA Abs are the first line of immune defense. In this study, we used paired IgA and IgG mAbs against HIV gp160 to study intraepithelial cell neutralization and inhibition of HIV replication. African green monkey kidney cells, Vero C1008, polarizable epithelial cells transfected to express the polymeric Ig receptor (pIgR), were transfected with HIV proviral DNA, and intracellular neutralization mediated by the mAbs was assessed. D47A and D19A IgA, which neutralized HIV in a conventional assay, potently inhibited intracellular HIV replication as assessed by infecting HeLa-CD4-long terminal repeat/β-galactosidase cells (human cervical carcinoma cell line) and CEMx174 cells (human T cell line) with apical supernatant, basolateral medium, and cell lysate from transfected cells. D47A also inhibited the production of virus as assessed by direct assay of p24. In contrast, D47 and D19 IgG, sharing the same V regions, but which were not transcytosed by the pIgR, did not inhibit intracellular HIV replication, nor did D47A and D19A IgA in pIgR− cells, incapable of transcytosing IgA. Confocal immunofluorescence microscopy showed prominent colocalization of HIV protein and D47A, in agreement with the intracellular neutralization data. D10A, which did not neutralize HIV in the conventional assay, and irrelevant IgA did not show intracellular neutralization or colocalization. Control studies with two kinds of conditioned medium confirmed that HIV neutralization had indeed occurred inside the cells. Thus, during its transcytosis through epithelial cells, HIV-specific IgA can neutralize HIV replication.

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Section: Intracellular Colocalization Of Iga Ab and Viral Agmentioning

confidence: 91%

Intraepithelial Cell Neutralization of HIV-1 Replication by IgA

Huang

Wright

Gao

et al. 2005

The Journal of Immunology

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“…It has been previously shown that basolateral to apical transcytosed proteins such as pIgA receptors or DPPIV transit in the apical recycling endosomes (4,40). Caco-2 cells do not express pIgA receptors, but express DPPIV.…”

Section: Truncated Bbmi Proteins Affect Delivery Of Basolateral Intermentioning

confidence: 99%

“…It has been previously shown that MDCK cells and Caco-2 cells exhibit apical endosomes that are accessible to basolaterally and apically internalized molecules (4,5,11). These endosomes display a tubulo-vesicular morphology in MDCK cells, while they display a multivesicular structure in Caco-2 cells (5,42).…”

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confidence: 99%

Truncated Brush Border Myosin I Affects Membrane Traffic in Polarized Epithelial Cells

Dürrbach

Raposo

Tenza

et al. 2000

Traffic

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We investigate, in this study, the potential involvement of an acto-myosin-driven mechanism in endocytosis of polarized cells. We observed that depolymerization of actin filaments using latrunculin A decreases the rate of transferrin recycling to the basolateral plasma membrane of Caco-2 cells, and increases its delivery to the apical plasma membrane. To analyze whether a myosin was involved in endocytosis, we produced, in this polarized cell line, truncated, non-functional, brush border, myosin I proteins (BBMI) that we have previously demonstrated to have a dominant negative effect on endocytosis of unpolarized cells. These non-functional proteins affect the rate of transferrin recycling and the rate of transepithelial transport of dipeptidyl-peptidase IV from the basolateral plasma membrane to the apical plasma membrane. They modify the distribution of internalized endocytic tracers in apical multivesicular endosomes that are accessible to fluid phase tracers internalized from apical and basolateral plasma membrane domains. Altogether, these observations suggest that an acto-myosin-driven mechanism is involved in the trafficking of basolaterally internalized molecules to the apical plasma membrane.

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“…After arrival at the cell surface, apical and basolateral membrane proteins are internalized into separate apical sorting endosomes and basal sorting endosomes (Figure 2), (Breitfeld et al, 1989;Mostov et al, 2003;Rodriguez-Boulan et al, 2005), mixed in common recycling endosomes and sorted into distinct recycling routes back to their original PM domain. The apical recycling route includes the apical recycling endosome (Apodaca et al, 1994;Brown et al, 2000). More recent work has shown that some newly synthesized PM proteins move from TGN to common recycling endosomes and are sorted there in not fully polarized MDCK cells (Futter et al, 1995;Leitinger et al, 1995;Orzech et al, 2000;Ang et al, 2004;Cancino et al, 2007;Gravotta et al, 2007; reviewed by Ellis et al, 2006 Figure 1 The epithelial polarity program (EPP).…”

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

The epithelial polarity program: machineries involved and their hijacking by cancer

2008

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The Epithelial Polarity Program (EPP) adapts and integrates three ancient cellular machineries to construct an epithelial cell. The polarized trafficking machinery adapts the cytoskeleton and ancestral secretory and endocytic machineries to the task of sorting and delivering different plasma membrane (PM) proteins to apical and basolateral surface domains. The domain-identity machinery builds a tight junctional fence (TJ) between apical and basolateral PM domains and adapts ancient polarity proteins and polarity lipids on the cytoplasmic side of the PM, which have evolved to perform a diversity of polarity tasks across cells and species, to provide 'identity' to each epithelial PM domain. The 3D organization machinery utilizes adhesion molecules as positional sensors of other epithelial cells and the basement membrane and small GTPases as integrators of positional information with the activities of the domain-identity and polarized trafficking machineries. Cancer is a disease mainly of epithelial cells (90% of human cancers are carcinomas that derive from epithelial cells) that hijacks the EPP machineries, resulting in loss of epithelial polarity, which often correlates in extent with the aggressiveness of the tumor. Here, we review how the EPP integrates its three machineries and the strategies used by cancer to hijack them.

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Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes.

Cited by 358 publications

References 47 publications

Intraepithelial Cell Neutralization of HIV-1 Replication by IgA

Intraepithelial Cell Neutralization of HIV-1 Replication by IgA

Truncated Brush Border Myosin I Affects Membrane Traffic in Polarized Epithelial Cells

The epithelial polarity program: machineries involved and their hijacking by cancer

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