30 research outputs found
PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells
Pals1/Mpp5 is required for correct localization of Crb1 at the subapical region in polarized Muller glia cells
The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells
In this work, we showed that in Caco-2 cells, a polarized cell line derived from human colon cancer that does not express caveolin 1 (Cav-1), there was no detectable expression of caveolin 2 (Cav-2). When Cav-2 was reintroduced in these cells, it accumulated in the Golgi complex. A chimera, in which the scaffolding domain of Cav-1 was replaced by the one from Cav-2, induced a prominent Golgi staining of Cav-1, strongly indicating that this domain was responsible for the accumulation of Cav-2 in the Golgi complex. Cav-2 was able to interact with Cav-1 in the Golgi complex but this interaction was not sufficient to export it from this compartment. Several chimeras between Cav-1 and 2 were used to show that surface expression of caveolin was necessary but not sufficient to promote caveolae formation. Interestingly, levels of incorporation of the chimeras into Triton insoluble rafts correlated with their ability to trigger caveolae formation raising the possibility that a critical concentration of caveolins to discrete domains of the plasma membrane might be necessary for caveolae formation
PSD95beta regulates plasma membrane Ca2+ pump localization at the photoreceptor synapse
International audienc
Occurrence, Ultrastructure and Developmental Features of Nuclear Inclusions in the Tribe Antirrhineae (Scrophulariaceae). I. Amorphous Inclusion
Occurrence, Ultrastructure and Developmental Features of Nuclear Inclusions in the Tribe Antirrhineae (Scrophulariaceae). II. Tubular Inclusion
Ca2+-binding sites and phosphatase activities in sieve element reticulum and P-protein of chick-pea phloem. A cytochemical and X-ray microanalysis survey
CD146 and its soluble form regulate monocyte transendothelial migration
International audienceObjectives-During inflammation, cell adhesion molecules are modulated or redistributed for leukocyte transmigration. Among molecules at the interendothelial junction, CD146 is involved in cell-cell cohesion and permeability, but its role in monocyte transmigration is unknown.Methods and Results-TNF enhanced CD146 expression at the junction and apical membrane of human umbilical veins endothelial cells (HUVECs) through CD146 synthesis and intracellular store redistribution. In addition, TNF increased the release of a soluble form (sCD146) through a metalloproteinase-dependent mechanism. The redistribution of CD146 to the junction led us to investigate its role in monocyte transmigration using THP1 and freshly isolated monocytes. Evidence that CD146 contributes to monocyte transmigration was provided by inhibition experiments using anti-CD146 antibodies and CD146 siRNA in HUVECs. In addition, sCD146 specifically bound both monocytes and HUVECs and dose-dependently increased monocyte transmigration. Assessment of sCD146 binding on immobilized CD146 failed to evidence any homophilic interaction. Together, our data suggest endothelial CD146 binds heterophilically with a yet unknown ligand on monocytes.Conclusions-Our results demonstrate that CD146 is regulated by the inflammatory cytokine TNF and that CD146 and sCD146 are both involved in monocyte transendothelial migration during inflammatio