scholarly journals Syntaxin 4 Mediates NF-κB Signaling and Chemokine Ligand Expression via Specific Interaction with IκBβ

Diabetes ◽  
2021 ◽  
pp. db200868 ◽  
Author(s):  
Rajakrishnan Veluthakal ◽  
Eunjin Oh ◽  
Miwon Ahn ◽  
Diti Chatterjee-Bhowmick ◽  
Debbie C. Thurmond
Keyword(s):  
Specific Interaction ◽  
Chemokine Ligand ◽  
Ligand Expression ◽  
Syntaxin 4

scholarly journals Syntaxin 4 Mediates NF-κB Signaling and Chemokine Ligand Expression via Specific Interaction with IκBβ

2021 ◽  
Author(s):  
Ada Admin ◽  
Rajakrishnan Veluthakal ◽  
Eunjin Oh ◽  
Miwon Ahn ◽  
Diti Chatterjee-Bhowmick ◽  
...  
Keyword(s):  
Specific Interaction ◽  
Cell Mass ◽  
Proteasomal Degradation ◽  
Human Islets ◽  
Β Cells ◽  
Chemokine Ligand ◽  
Ligand Expression ◽  
Syntaxin 4 ◽  
Proteosomal Degradation ◽  
Necrosis Factor

Enrichment of human islets with Syntaxin 4 (STX4) improves functional β-cell mass through a nuclear factor- kB (NF-kB)-dependent mechanism. However, the detailed mechanisms underlying the protective effect of STX4 are unknown. To determine the signaling events linking STX4 enrichment and downregulation of NF-kB activity, STX4 was overexpressed in human islets, EndoC-βH1 and INS-1 832/13 cells in culture, and the cells were challenged with the proinflammatory cytokines interleukin-1β, tumor necrosis factor-a and interferon-g, individually and in combination. STX4 expression suppressed cytokine-induced proteasomal degradation of IkBβ but not IkBa. Inhibition of IKKβ prevented IkBβ degradation, suggesting that IKKβ phosphorylates IkBβ. Moreover, the IKKβ inhibitor, as well as a proteosomal degradation inhibitor, prevented the loss of STX4 caused by cytokines. This suggests that STX4 may be phosphorylated by IKKβ in response to cytokines, targeting STX4 for proteosomal degradation. Expression of a stabilized form of STX4 further protected IkBβ from proteasomal degradation, and like wildtype STX4, stabilized STX4 coimmunoprecipitated with IkBβ and the NF-kB p50 subunit. This work proposes a novel pathway wherein STX4 regulates cytokine-induced NF-kB signaling in β-cells <i>via</i> associating with and preventing IkBβ degradation, suppressing chemokine expression, and protecting islet β-cells from cytokine-mediated dysfunction and demise.

scholarly journals Syntaxin 4 Mediates NF-κB Signaling and Chemokine Ligand Expression via Specific Interaction with IκBβ

2021 ◽  
Author(s):  
Ada Admin ◽  
Rajakrishnan Veluthakal ◽  
Eunjin Oh ◽  
Miwon Ahn ◽  
Diti Chatterjee-Bhowmick ◽  
...  
Keyword(s):  
Specific Interaction ◽  
Cell Mass ◽  
Proteasomal Degradation ◽  
Human Islets ◽  
Β Cells ◽  
Chemokine Ligand ◽  
Ligand Expression ◽  
Syntaxin 4 ◽  
Proteosomal Degradation ◽  
Necrosis Factor

Enrichment of human islets with Syntaxin 4 (STX4) improves functional β-cell mass through a nuclear factor- kB (NF-kB)-dependent mechanism. However, the detailed mechanisms underlying the protective effect of STX4 are unknown. To determine the signaling events linking STX4 enrichment and downregulation of NF-kB activity, STX4 was overexpressed in human islets, EndoC-βH1 and INS-1 832/13 cells in culture, and the cells were challenged with the proinflammatory cytokines interleukin-1β, tumor necrosis factor-a and interferon-g, individually and in combination. STX4 expression suppressed cytokine-induced proteasomal degradation of IkBβ but not IkBa. Inhibition of IKKβ prevented IkBβ degradation, suggesting that IKKβ phosphorylates IkBβ. Moreover, the IKKβ inhibitor, as well as a proteosomal degradation inhibitor, prevented the loss of STX4 caused by cytokines. This suggests that STX4 may be phosphorylated by IKKβ in response to cytokines, targeting STX4 for proteosomal degradation. Expression of a stabilized form of STX4 further protected IkBβ from proteasomal degradation, and like wildtype STX4, stabilized STX4 coimmunoprecipitated with IkBβ and the NF-kB p50 subunit. This work proposes a novel pathway wherein STX4 regulates cytokine-induced NF-kB signaling in β-cells <i>via</i> associating with and preventing IkBβ degradation, suppressing chemokine expression, and protecting islet β-cells from cytokine-mediated dysfunction and demise.

scholarly journals Regulation of FAS Ligand Expression by Chemokine Ligand 2 in Human Endometrial Cells

2006 ◽  
Vol 75 (2) ◽  
pp. 203-209 ◽  
Author(s):  
Belgin Selam ◽  
Umit A. Kayisli ◽  
G. Eda Akbas ◽  
Murat Basar ◽  
Aydin Arici
Keyword(s):  
Fas Ligand ◽  
Endometrial Cells ◽  
Chemokine Ligand ◽  
Ligand Expression ◽  
Chemokine Ligand 2

scholarly journals Polyphenols differentially inhibit degranulation of distinct subsets of vesicles in mast cells by specific interaction with granule-type-dependent SNARE complexes

2013 ◽  
Vol 450 (3) ◽  
pp. 537-546 ◽  
Author(s):  
Yoosoo Yang ◽  
Jung-Mi Oh ◽  
Paul Heo ◽  
Jae Yoon Shin ◽  
Byoungjae Kong ◽  
...  
Keyword(s):  
Mast Cells ◽  
Membrane Trafficking ◽  
Molecular Mechanisms ◽  
Specific Interaction ◽  
Cell Types ◽  
Dietary Polyphenols ◽  
Protein Receptor ◽  
Numerous Cell ◽  
Syntaxin 4 ◽  
Granule Type

Anti-allergic effects of dietary polyphenols were extensively studied in numerous allergic disease models, but the molecular mechanisms of anti-allergic effects by polyphenols remain poorly understood. In the present study, we show that the release of granular cargo molecules, contained in distinct subsets of granules of mast cells, is specifically mediated by two sets of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, and that various polyphenols differentially inhibit the formation of those SNARE complexes. Expression analysis of RBL-2H3 cells for 11 SNARE genes and a lipid mixing assay of 24 possible combinations of reconstituted SNAREs indicated that the only two active SNARE complexes involved in mast cell degranulation are Syn (syntaxin) 4/SNAP (23 kDa synaptosome-associated protein)-23/VAMP (vesicle-associated membrane protein) 2 and Syn4/SNAP-23/VAMP8. Various polyphenols selectively or commonly interfered with ternary complex formation of these two SNARE complexes, thereby stopping membrane fusion between granules and plasma membrane. This led to the differential effect of polyphenols on degranulation of three distinct subsets of granules. These results suggest the possibility that formation of a variety of SNARE complexes in numerous cell types is controlled by polyphenols which, in turn, might regulate corresponding membrane trafficking.

Cytokine and chemokine ligand expression in cutaneous lupus erythematosus

2012 ◽  
Vol 22 (3) ◽  
pp. 319-323 ◽  
Author(s):  
Thilo Gambichler ◽  
Zanna Genc ◽  
Marina Skrygan ◽  
Nina Scola ◽  
Christian Tigges ◽  
...  
Keyword(s):  
Lupus Erythematosus ◽  
Cutaneous Lupus Erythematosus ◽  
Chemokine Ligand ◽  
Ligand Expression ◽  
Cutaneous Lupus

Leptin enhances CC-chemokine ligand expression in cultured murine macrophage

2009 ◽  
Vol 384 (3) ◽  
pp. 311-315 ◽  
Author(s):  
Norikazu Kiguchi ◽  
Takehiko Maeda ◽  
Yuka Kobayashi ◽  
Yohji Fukazawa ◽  
Shiroh Kishioka
Keyword(s):  
Murine Macrophage ◽  
Cc Chemokine ◽  
Chemokine Ligand ◽  
Ligand Expression

Fas ligand expression in rat kupffer cells in response to lipopolysaccharide is mediated by reactive oxygen species

2001 ◽  
Vol 120 (5) ◽  
pp. A361-A361
Author(s):  
K UCHIKURA ◽  
T WADA ◽  
Z SUN ◽  
S HOSHINO ◽  
G BULKLEY ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Kupffer Cells ◽  
Fas Ligand ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Ligand Expression
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