Involvement of Cellular Caveolae in Bacterial Entry into Mast Cells

Shin, Jeoung-Sook; Gao, Zhimin; Abraham, Soman N.

doi:10.1126/science.289.5480.785

Cited by 294 publications

(282 citation statements)

References 24 publications

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“…1, D-F). As a means of further demonstrating lipid raft association with intracellular E. coli, we examined infected BEC using specific probes for the most commonly used markers of lipid rafts: caveolin-1, cholesterol, and the glycolipid GM1 (23,35,36). Shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Bacterial Penetration of Bladder Epithelium through Lipid Rafts

Duncan

Shin

et al. 2004

Journal of Biological Chemistry

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Type 1 fimbriated Escherichia coli represents the most common human uropathogen, owing much of its virulence to invasion of the uroepithelium, which is highly impermeable due to the preponderance of uroplakins and highly ordered lipid components. We sought to elucidate the molecular basis for E. coli invasion of the bladder epithelium by employing human 5637 bladder epithelial cells, and we found the following: (i) intracellular E. coli associated with caveolae and lipid raft components; (ii) RNA i reduction of caveolin-1 expression inhibited bacterial invasion; (iii) a signaling molecule required for E. coli invasion was located in lipid rafts and physically associated with caveolin-1; (iv) bacterial invasion was inhibited by lipid raft disrupting/ usurping agents. In the mouse bladder, the E. coli type 1 fimbrial receptor, uroplakin Ia, was located in lipid rafts, and lipid raft disruptors inhibited E. coli invasion. Cumulatively, E. coli uroepithelial invasion occurs through lipid rafts, which, paradoxically, contribute to bladder impermeability.

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Section: Resultsmentioning

confidence: 99%

Bacterial Penetration of Bladder Epithelium through Lipid Rafts

Duncan

Shin

et al. 2004

Journal of Biological Chemistry

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“…Integrin ␣2␤1 differs from other integrin type virus receptors by being the only integrin known to mediate virus entry through caveolae instead of clathrin-coated vesicles (Marjomäki et al, 2002). Caveolae are also involved in the entry of SV40 (Pelkmans et al, 2001;, mouse polyoma virus (Richterova et al, 2001), filoviruses (Empig and Goldsmith, 2002), and some bacteria (Shin et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Clustering Induces a Lateral Redistribution of α2β1 Integrin from Membrane Rafts to Caveolae and Subsequent Protein Kinase C-dependent Internalization

Upla

Marjomäki

Kankaanpää

et al. 2004

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Integrin ␣2␤1 mediates the binding of several epithelial and mesenchymal cell types to collagen. The composition of the surrounding plasma membrane, especially caveolin-1-and cholesterol-containing membrane structures called caveolae, may be important to integrin signaling. On cell surface ␣2␤1 integrin was located in the raft like membrane domain, rich in GPI-anchored proteins, rather than in caveolae. However, when antibodies were used to generate clusters of ␣2␤1 integrin, they started to move laterally on cell surface along actin filaments. During the lateral movement small clusters fused together. Finally ␣2␤1 integrin was found inside caveolae and subsequently internalized into caveosome-like perinuclear structures. The internalization process, unlike cluster formation or lateral redistribution, was dependent on protein kinase C␣ activity. Caveolae are known to be highly immobile structures and ␣2␤1 integrin clusters represent a previously unknown mechanism to activate endocytic trafficking via caveolae. The process was specific to ␣2␤1 integrin, because the antibody-mediated formation of ␣V integrin clusters activated their internalization in coated vesicles and early endosomes. In addition to natural ligands human echovirus-1 (EV1) gains entry into the cell by binding to ␣2␤1 and taking advantage of ␣2␤1 internalization via caveolae. INTRODUCTIONCaveolae are cave-like invaginations of the cell surface (for reviews see Kurzchalia and Parton, 1999;Parton 2003). They have been described as highly immobile and not involved in constitutive endocytic trafficking (Thomsen et al., 2002). Their internalization can be activated, for example, by the phosphatase inhibitor okadaic acid (Parton et al., 1994). In endothelial cells the interaction of albumin docking protein gp60 and caveolin-1 initiates the endocytosis of caveolae (Minshall et al., 2000). Caveolins are membrane proteins that are molecular markers of caveolae and shown to be crucial for the formation of these structures (Fra et al., 1995). Caveolins can be associated with cell surface growth factor receptors (Couet et al., 1997) and cell adhesion receptors (Wary et al., 1996(Wary et al., , 1998Wei et al., 1999) and caveolae might therefore play a role in cellular signaling. In addition, caveolae have been suggested to participate in the uptake of folate by pinocytosis, but this is still under discussion (Parton, 2003). Caveolin-deficient mice have given novel insight into the function of caveolae. Caveolin-1 gene knockout leads to pulmonary defects, vasoconstriction, or dilatation abnormalities and resistance to diet-induced obesity (Drab et al., 2001;Razani et al., 2001;Schubert et al., 2001;Sotgia et al., 2002;Razani et al., 2002). Simian virus 40 (SV40) has been shown to be internalized through caveolae and detailed studies focused on the virus entry mechanism have produced a lot of new information about the biology of caveolae (Pelkmans et al., 2001. We have recently shown that human echovirus 1 (EV1) is another virus using caveolae in its entry (Mar...

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“…However upon treatment with TNP-E. coli, up to 30% of the IgE/Fc RI complexes were detectable in fractions 3-5, where lipid raft components typically fractionate ( Fig. 2A, two middle panels) (22). Thus, the ligation of IgE/Fc RI complexes in the particulate allergen model induces the association of these complexes with lipid rafts.…”

Section: Fc Ri-mediated MC Phagocytosis Is Lipid Raft-dependentmentioning

confidence: 99%

“…Triton X-100-treated RBL-2H3 cell lysates were prepared before and after exposure to TNP-E. coli. To separate the lipid raft fractions, these samples were fractionated using a sucrose density gradient cell fractionation assay (22). Before the addition of TNP-E. coli, the majority of IgE/Fc RI complexes were found in fractions 8 -10, where soluble proteins normally fractionate ( Fig.…”

Section: Fc Ri-mediated MC Phagocytosis Is Lipid Raft-dependentmentioning

confidence: 99%

Harboring of Particulate Allergens within Secretory Compartments by Mast Cells following IgE/FcεRI-Lipid Raft-Mediated Phagocytosis

Shin

Shelburne

Jin

et al. 2006

The Journal of Immunology

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Although much is known regarding the exocytic responses of mast cells following allergen/IgE-mediated activation, little is currently known of the fate of the activating allergens, many of which are particles. We have found that IgE-bound particulate allergens were phagocytosed by activated mast cells in a lipid raft-dependent manner. The nascent allergen-containing phagosomes were found to transform into granule compartments by acquiring VAMP7 and serotonin and exhibited the capacity to empty their contents upon mast cell activation. When allergen-harboring mast cells were stimulated, the intracellular allergens were expelled intact and shown to activate adjacent mast cells. This capacity of mast cells to phagocytose and retain whole and antigenically intact allergens could potentially contribute to the course of inflammatory diseases such as asthma.

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Involvement of Cellular Caveolae in Bacterial Entry into Mast Cells

Cited by 294 publications

References 24 publications

Bacterial Penetration of Bladder Epithelium through Lipid Rafts

Bacterial Penetration of Bladder Epithelium through Lipid Rafts

Clustering Induces a Lateral Redistribution of α2β1 Integrin from Membrane Rafts to Caveolae and Subsequent Protein Kinase C-dependent Internalization

Harboring of Particulate Allergens within Secretory Compartments by Mast Cells following IgE/FcεRI-Lipid Raft-Mediated Phagocytosis

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