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Articles by Xiaoxia Li
Total Records ( 5 ) for Xiaoxia Li
  Jinmiao Lu , Qin Li , Xiaoxia Li and Zhiping Li
  Background and Objective: Ceftriaxone is a frequently used antibiotic in children. This paper is to raise awareness of the challenges in managing ceftriaxone-induced hemolytic anemia and requesting more successful and useful predicting tools in its detection and prevention in pharmacogenomics field. Methodology: An adversary case report of a 5 years old boy who died from ceftriaxone-induced hemolytic anemia within 12 h in children’s hospital though all resuscitation attempt made. Results: Soon after intravenously ceftriaxone, the patient developed acute reaction to ceftriaxone presented with cold and pallor skin with shallow breath etc. Therefore, ceftriaxone infusion was stopped immediately and the patient was moved to emergency room (ER) for resuscitation from hematology outpatient clinic. Until his heart rhythm returned to normal and stabilized, he was then transferred to Pediatric Intensive Care Unit (PICU). Further, the patient developed bradycardia, reduced blood pressure, unconsciousness, under-responsiveness and oliguria. Additionally, his urine was turned from pale yellow to dark red. Urinalysis determined occult blood and trace protein existence. The hemoglobin level was 9.2 g L–1. Coomb’s test came back strong positive accompany with positive anti-C3d antibody. Hemolytic crisis was suspected. Unsuccessfully, the patient died from hemolytic shock, although all emergent resuscitation attempts were made. Conclusion: Ceftriaxone induced autoimmune hemolytic is extremely rare but could be severe as life-threatening condition stressed in pediatric. Its treatment is clinical challenging with poor outcome. Therefore, prevention is the key compared to treatment.
  Angela C. Johnson , Xiaoxia Li and Eric Pearlman
  The adaptor molecule MyD88 is necessary for responses to all Toll-like receptors except TLR3 and a subset of TLR4 signaling events, which are mediated by the adaptor molecule TRIF. To determine the role of TRIF in host inflammatory responses, corneal epithelium of C57BL/6, TLR3-/-, TRIF-/-, and MyD88-/- mice was abraded and stimulated with the synthetic TLR3 ligand poly(I:C). We found that poly(I:C) induced a pronounced cellular infiltration into the corneal stroma, which was TLR3- and TRIF-dependent. Unexpectedly, the inflammatory response was exacerbated in MyD88-/- mice, with enhanced neutrophil and F4/80+ cell infiltration into the corneal stroma and elevated corneal haze, which is an indicator of loss of corneal transparency. To determine whether MyD88-dependent inhibition of TLR3/TRIF responses is a general phenomenon, we examined cytokine production by MyD88-/- bone marrow-derived macrophages; however, no significant difference was observed between MyD88+/+ or MyD88-/- macrophages. Incontrast, human corneal epithelial cells (HCECs) transfected with MyD88 small interfering RNA had significantly increased (2.5-fold) CCL5/RANTES production compared with control HCECs, demonstrating a negative regulatory role for MyD88 in TLR3/TRIF responses in these cells. Finally, knockdown of MyD88 in HCECs resulted in increased phosphorylation of c-Jun N-terminal kinase (JNK), but not p38, IRF-3, or NF-κB. Consistent with this finding, the JNK inhibitor SP600125, but not p38 inhibitor SB203580, ablated this response. Taken together, these findings demonstrate a novel JNK-dependent inhibitory role for MyD88 in the TLR3/TRIF activation pathway.

  Hui Xiao , Wen Qian , Kirk Staschke , Youcun Qian , Grace Cui , Li Deng , Mariam Ehsani , Xiliang Wang , Yue-Wei Qian , Zhijian J. Chen , Raymond Gilmour , Zhengfan Jiang and Xiaoxia Li
  IL-1 receptor-associated kinase (IRAK) is phosphorylated, ubiquitinated, and degraded upon interleukin-1 (IL-1) stimulation. In this study, we showed that IRAK can be ubiquitinated through both Lys-48- and Lys-63-linked polyubiquitin chains upon IL-1 induction. Pellino 3b is the RING-like motif ubiquitin protein ligase that promotes the Lys-63-linked polyubiquitination on IRAK. Pellino 3b-mediated Lys-63-linked IRAK polyubiquitination competed with Lys-48-linked IRAK polyubiquitination for the same ubiquitination site, Lys-134 of IRAK, thereby blocking IL-1-induced IRAK degradation. Importantly, the negative impact of Pellino 3b on IL-1-induced IRAK degradation correlated with the inhibitory effect of Pellino 3b on the IL-1-induced TAK1-dependent pathway, suggesting that a positive role of IRAK degradation in IL-1 induced TAK1 activation. Taken together, our results suggest that Pellino 3b acts as a negative regulator for IL-1 signaling by regulating IRAK degradation through its ubiquitin protein ligase activity.
  Justin Hartupee , Xiaoxia Li and Thomas Hamilton
  Interleukin 1α (IL-1α) is capable of driving pro-inflammatory gene expression through both the initiation of transcription and by prolonging the half-life of short-lived mRNAs. Although the signaling events linking the IL-1 receptor to the activation of NFκB and the initiation of transcription have been well characterized, less is known about the signaling events linking to mRNA stabilization. As a model to study the control of mRNA stability we have used the mouse chemokine KC, expression of which requires both NFκB-driven transcription and stabilization of the constitutively unstable mRNA. We have evaluated the role of signaling adaptors known to play a role in IL-1α-driven NFκB activation in the generation of mRNA stability. Surprisingly, although TRAF6 is essential for NFκB activation, it is not required for IL-1α-induced mRNA stabilization. IRAK1, which is recognized to function upstream of TRAF6, is required for both mRNA stabilization and activation of NFκB. Consistent with the previous findings, the TRAF6 interaction sites in IRAK1 are required for NFκB activation but do not play a role in mRNA stabilization. These findings indicate that signals from the IL-1 receptor segregate into at least two separate pathways at the level of IRAK1; one couples through TRAF6 to NFκB activation while a second utilizes a TRAF6-independent pathway that is responsible for mRNA stabilization.
  Jerzy Frczek , Tae Whan Kim , Hui Xiao , Jianhong Yao , Qian Wen , Yali Li , Jean-Laurent Casanova , Juliusz Pryjma and Xiaoxia Li
  Two parallel interleukin-1 (IL-1)-mediated signaling pathways have been uncovered for IL-1R-TLR-mediated NFκB activation: TAK1-dependent and MEKK3-dependent pathways, respectively. The TAK1-dependent pathway leads to IKKα/β phosphorylation and IKKβ activation, resulting in classic NFκB activation through IκBα phosphorylation and degradation. The TAK1-independent MEKK3-dependent pathway involves IKKγ phosphorylation and IKKα activation, resulting in NFκB activation through dissociation of phosphorylated IκBα from NFκB without IκBα degradation. IL-1 receptor-associated kinase 4 (IRAK4) belongs to the IRAK family of proteins and plays a critical role in IL-1R/TLR-mediated signaling. IRAK4 kinase-inactive mutant failed to mediate the IL-1R-TLR-induced TAK1-dependent NFκB activation pathway, but mediated IL-1-induced TAK1-independent NFκB activation and retained the ability to activate substantial gene expression, indicating a structural role of IRAK4 in mediating this alternative NFκB activation pathway. Deletion analysis of IRAK4 indicates the essential structural role of the IRAK4 death domain in receptor proximal signaling for mediating IL-1R-TLR-induced NFκB activation.
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