Translocation of cytosolic annexin 2 to a Triton‐insoluble membrane subdomain upon nicotine stimulation of chromaffin cultured cells

Sagot, Isabelle; Regnouf, Françoise; Henry, Jean‐Pierre; Pradel, Louise‐Anne

doi:10.1016/s0014-5793(97)00594-2

Cited by 36 publications

(27 citation statements)

References 22 publications

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“…The observations presented here document the only known trigger for redistribution of A2 and p11 to the HUVEC exterior and provide insight into the mechanism since thrombin induces signaling through G proteins. Like thrombin, the effects of nicotine and nerve growth factor (Rakhit et al, 2001) domains (Sagot et al, 1997); (2) A2 has been identified as a component of caveolae (Stahlhut et al, 2000;Harder and Gerke, 1994;Stan et al, 1997); (3) cell-surface A2 has been colocalized with caveolin (van der Goot, 1997); and (4) nerve growth factor induces exposure of A2 on the neurite surface (Jacovina et al, 2001), we propose that A2 transport to the cell surface may involve G-protein-linked control of caveolae.…”

Section: Discussionmentioning

confidence: 90%

“…An interesting property of A2 cellular distribution is that it has no secretory signal, but has nevertheless been identified on the surface of various cell types (Chung and Erickson, 1994;Hajjar et al, 1994;Kassam et al, 1998;Wright et al, 1995). The mechanism by which A2 is shuttled to the cell surface is not known, but might involve localization to caveolae (Sagot et al, 1997;Stahlhut et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2

Peterson

Sutherland

Nesheim

et al. 2003

Journal of Cell Science

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Cell-surface annexin 2 (A2) and its ligand p11 have been implicated in fibrinolysis because of their ability to accelerate tissue plasminogen activator (tPA)-mediated activation of plasminogen to plasmin. Because thrombin is a potent cell modulator obligately produced at the site of clot formation, we hypothesized that the amount of cell-surface A2 and p11 might be altered by thrombin with consequent effects on plasmin generation. In support of this hypothesis, immunofluorescence microscopy and hydrophilic biotinylation experiments showed that both A2 and p11 were significantly increased on the surface of human umbilical vein endothelial cells (HUVECs)treated with thrombin (0.8-8 nM) for 5 minutes followed by 1 hour at 37°C. Intracellular immunofluorescence microscopy and immunoblot analyses of whole cell extracts revealed increased p11 but unchanged A2 in response to thrombin,suggesting that transbilayer trafficking of A2 might be controlled by p11. The thrombin receptor-activating peptide (TRAP) similarly affected cells,demonstrating that cell signaling at least involved the type-1 protease activated receptor (PAR-1). An effect on the fibrinolysis pathway after treatment of HUVECs with thrombin was shown by increased fluorescein-labeled plasminogen binding to cells, which was inhibited by an antibody specific for p11. This was confirmed by observing that thrombin pretreatment of HUVECs increased biotin-modified plasminogen binding. Utilizing a chromogenic assay,pretreatment of HUVECs by thrombin further enhanced activation of the Glu and Lys forms of plasminogen by tPA. These data suggest a novel mechanism that links the coagulation and fibrinolysis pathways by thrombin-mediated feedback.

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Section: Discussionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2

Peterson

Sutherland

Nesheim

et al. 2003

Journal of Cell Science

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“…There is precedent for translocation of cytoplasmic proteins to vesicular and cell surface membranes. For example, in chromaffin cells on nicotine stimulation, annexin 2, a cytoplasmic protein, has been shown to be translocated to a membrane fraction containing chromaffin granule membrane and plasma membrane (Sagot et al 1997). However, surface staining for stefin A was not observed in the hepatoma cells.…”

Section: Discussionmentioning

confidence: 99%

Differential Localization of Cysteine Protease Inhibitors and a Target Cysteine Protease, Cathepsin B, by Immuno-Confocal Microscopy

Calkins

Sameni

Koblinski

et al. 1998

J Histochem Cytochem.

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SUMMARYThe cystatin superfamily of cysteine protease inhibitors and target cysteine proteases such as cathepsin B have been implicated in malignant progression. The respective cellular/extracellular localization of cystatins and cysteine proteases in tumors may be critical in regulating activity of the enzymes. Confocal microscopy has enabled us to demonstrate the differential localization of cystatins and cathepsin B in an embryonic liver cell line and an invasive hepatoma cell line. In both, stefins A and B were distributed diffusely throughout the cytoplasm, whereas cystatin C was distributed in juxtanuclear vesicles. Stefin A and cystatin C, but not stefin B, were present on the cell surface. Cystatin C was found on the top surfaces of both cell lines, whereas stefin A was found only on the top surface of the embryonic liver cells. Cathepsin B staining was concentrated in perinuclear vesicles in the embryonic liver cells. In the hepatoma cells, staining for cathepsin B was also present in vesicles adjacent to the cell membrane and on localized regions of the bottom surface. Such a disparate distribution of cathepsin B and its endogenous inhibitors may facilitate proteolysis by the hepatoma cells and thereby contribute to their invasive phenotype.

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“…Membrane anchoring could also occur through an intrinsic membrane protein such as CD44, which was recently found to anchor Ax II to detergentresistant, cholesterol-rich membranes (rafts) in mammary epithelial EpH4 cells (27). Both Ax II (27)(28)(29)(30) and SHP-2 (31) have been identified in rafts in cultured cells, and cholesterolsequestering reagents have been found to dissociate Ax II from both chromaffin granules (26) and endosomes (32). Alternatively, it is conceivable that the localization of either Ax II or SHP-2 to sites of cell-cell attachment could occur through direct binding to actin, since both Ax II (33,34) and SHP-2 (35) have been reported to bind to actin filaments in vitro, and both proteins were found along stress fibers in subconfluent endothelial cells (Fig.…”

Section: Localization Of Shp-2 and Ax II To Adhesion Bands And Stressmentioning

confidence: 99%

Regulation of the SHP-2 Tyrosine Phosphatase by a Novel Cholesterol- and Cell Confluence-dependent Mechanism

Burkart

Samii

Corvera

et al. 2003

Journal of Biological Chemistry

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Endothelial cells approaching confluence exhibit marked decreases in tyrosine phosphorylation of receptor tyrosine kinases and adherens junctions proteins, required for cell cycle arrest and adherens junctions stability. Recently, we demonstrated a close correlation in endothelial cells between membrane cholesterol and tyrosine phosphorylation of adherens junctions proteins. Here, we probe the mechanistic basis for this correlation. We find that as endothelial cells reach confluence, the tyrosine phosphatase SHP-2 is recruited to a low-density membrane fraction in a cholesterol-dependent manner. Binding of SHP-2 to this fraction was not abolished by phenyl phosphate, strongly suggesting that this binding was mediated by other regions of SHP-2 beside its SH2 domains. Annexin II, previously implicated in cholesterol trafficking, was associated in a complex with SHP-2, and both proteins localized to adhesion bands in confluent endothelial monolayers. These studies reveal a novel, cholesterol-dependent mechanism for the recruitment of signaling proteins to specific plasma membrane domains via their interactions with annexin II.Endothelial cells approaching confluence in culture undergo profound morphological and functional alterations, including the formation of intercellular junctions and the cessation of cell growth. These changes are associated with reductions in tyrosine phosphorylation levels of both receptor tyrosine kinases (1, 2) and cadherins and catenins (3), the major components of adherens junctions. The dephosphorylation of adherens junctions proteins appears to be necessary for the formation of stable, confluent endothelial monolayers, since increased tyrosine phosphorylation of adherens junctions proteins leads to the disruption of adherens junctions (4 -6). The mechanisms by which cell density decreases tyrosine phosphorylation of endothelial membrane proteins are unknown.One possible mechanism is that increased cell confluence modulates the local environment of signaling proteins in the plasma membrane, thereby altering their response to extracellular ligands. Recently (7), we identified membrane cholesterol as a potential determinant of tyrosine phosphorylation levels in growing endothelial monolayers. Membrane cholesterol increased markedly with cell density in cultures of growing endothelial cells, exhibiting levels 3-4-fold higher upon reaching confluence. Depletion of cholesterol from confluent monolayers of CPAE 1 cells induced the tyrosine phosphorylation of multiple membrane proteins, including the adherens junctions proteins ␥-catenin and pp120, and disrupted adherens junctions.Cholesterol might regulate tyrosine phosphorylation levels through the localization of tyrosine kinases or phosphatases to specific plasma membrane loci. To begin to identify such kinases or phosphatases, we have used very low (0.01%) levels of the sterol-containing detergent digitonin to identify proteins bound to membranes in a cholesterol-dependent manner (8). At these concentrations, digitonin complexes specifica...

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Translocation of cytosolic annexin 2 to a Triton‐insoluble membrane subdomain upon nicotine stimulation of chromaffin cultured cells

Cited by 36 publications

References 22 publications

Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2

Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2

Differential Localization of Cysteine Protease Inhibitors and a Target Cysteine Protease, Cathepsin B, by Immuno-Confocal Microscopy

Regulation of the SHP-2 Tyrosine Phosphatase by a Novel Cholesterol- and Cell Confluence-dependent Mechanism

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