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1.
Figure 4

Figure 4. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Comparison of effect of TAPI-2 and EDTA on release of sTNFR1 (gray bars) versus sICAM-1 (black bars) from IOBA-NHC cells (A; n = 2) and primary HCECs (B; n = 2).

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.
2.
Figure 3

Figure 3. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Percentage inhibition of PMA-stimulated release of sTNFR1 by EDTA (dashed line [■]) and TAPI-2 (solid line [◆]) from IOBA-NHC cells (A; n = 2) and primary HCECs (B; n = 2).

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.
3.
Figure 2

Figure 2. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Effect of PMA stimulation on sTNFR1 release from unprimed (gray bars) versus TAPI-2–primed (black bars) IOBA-NHC cells (A; n = 4, P < 0.05) and primary HCECs (B; n = 2).

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.
4.
Figure 5

Figure 5. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Representative overlay histograms (n = 4) showing upregulation of staining for TNFR1 (x-axis) on primary HCECs after priming with TAPI-2 and IFNγ (black) compared with unstimulated HCECs (gray). MFI was increased by of 2.7 ± 0.9 units (P < 0.05).

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.
5.
Figure 1

Figure 1. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Representative overlay histograms (n = 3) showing upregulation of staining for TNFR1 (x-axis) on primary HCECs after incubation with supernates from anti-IgE–stimulated purified conjunctival mast cells (black) compared with unstimulated HCECs (gray). MFI was increased by 2 ± 0.4 units (P < 0.05).

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.
6.
Figure 6

Figure 6. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Effect of TAPI-2/IFNγ priming on TNFα-mediated upregulation of ICAM-1 expression on IOBA-NHC cells (A) and primary HCECs (B). (A) Dose–response curves to TNFα with and without TAPI-2/IFNγ priming (left y-axis; percentage ICAM-1 expression greater than unstimulated cells; *P < 0.05 for comparisons between unprimed and primed treatments, including slopes; n = 4). Also shown is the lack of effect of TAPI-2/IFNγ priming on TNFα-stimulated release of sICAM-1 into supernates from the same experiments (right y-axis; sICAM-1 concentration [minus unstimulated] in pg/mL). (B) In primary HCECs, TAPI-2/IFNγ priming resulted in a similar enhanced response to TNFα-mediated ICAM-1 upregulation (5 ng/mL concentration of TNFα shown; n = 2).

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.
7.
Figure 7

Figure 7. From: Regulation of the Receptor for TNFα, TNFR1, in Human Conjunctival Epithelial Cells.

Schematic representation of regulation of TNFR1 shedding and its role in TNFα regulation. Regulation of the availability of TNFα receptors provides a protective mechanism against excessive TNFα activity. Proteolytic cleavage of TNFR1 is facilitated by TACE, which can be activated in vivo by the release of reactive oxygen species (ROS) and inhibited by TIMP-3. Shedding of TNFR1 results in the downregulation of receptor numbers on the cell surface, which decreases cellular sensitivity to TNFα. Soluble forms of TNFR1 can also bind to circulating TNFα, resulting in neutralization of TNFα-mediated responses. In our in vitro studies, PMA was used to stimulate ROS, and TAPI-2 was used to inhibit TACE. TAPI-2, a derivative of hydroxamic acid, inhibits TACE by interfering with zinc-dependent activation in the catalytic site of the metalloprotease.

Ellen B. Cook, et al. Invest Ophthalmol Vis Sci. ;49(9):3992-3998.

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