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Start Over Author "Xiu Xiu Liu" Publisher cell physiol biochem press gmbh & co kg
2 results on '"Xiu Xiu Liu"'

1. Elucidation of the FKBP25-60S Ribosomal Protein L7a Stress Response Signaling During Ischemic Injury

Author

Quan Jiang, Gang Wu, Lin Yang, Ya-Ping Lu, Xiu-Xiu Liu, Feng Han, Ya-Ping Deng, Xu-Chun Fu, Qi-Bing Liu, and Ying-Mei Lu

Subjects
Fkbp25, 60S ribosomal protein L7a, Nitrosative stress, Nuclear translocation, Oxygen-glucose deprivation, Physiology, QP1-981, Biochemistry, QD415-436
Abstract

Background/Aims: Peptidyl-prolyl cis-trans isomerase FKBP25 is a member of the FK506-binding proteins family which has peptidyl-prolyl cis/trans isomerase domain. The biological function and pathophysiologic role of FKBP25 remain elusive. Methods: The spatio-temporal changes in expression of endothelial FKBP25 upon oxygen-glucose deprivation (OGD) treatment were examined by Western blot and immunofluorescence. The immunoprecipitation and fluorescence resonance energy transfer (FRET) were used to address the interacting proteins with FKBP25. Results: In the present study, nuclear translocation of FKBP25 was observed following OGD in cultured endothelial cells. Intriguingly, FKBP25 nuclear translocation was further validated in peroxynitrite (ONOO-)-treated endothelial cells. Coimmunoprecipitation and FRET data indicated that FKBP25 translocated into the nucleus, in which it interacted with 60S ribosomal protein L7a, while overexpression FKBP25 protect endothelial cells against OGD injury. Conclusion: Our findings reveal that the nuclear import of FKBP25 and binding with 60S ribosomal protein L7a are protective stress responses to ischemia/nitrosaive stress injury.

Published
2018
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2. Elucidation of the FKBP25-60S Ribosomal Protein L7a Stress Response Signaling During Ischemic Injury

Author

Ya-ping Lu, Ya-Ping Deng, Xu-Chun Fu, Gang Wu, Xiu-Xiu Liu, Feng Han, Qi-Bing Liu, Ying-Mei Lu, Quan Jiang, and Lin Yang

Subjects
Ribosomal Proteins, 0301 basic medicine, Physiology, Immunoprecipitation, Active Transport, Cell Nucleus, Nuclear translocation, Nitrosative stress, Oxygen-glucose deprivation, Immunofluorescence, lcsh:Physiology, Tacrolimus Binding Proteins, Stress Response Signaling, lcsh:Biochemistry, Mice, 03 medical and health sciences, chemistry.chemical_compound, Western blot, Stress, Physiological, medicine, Animals, lcsh:QD415-436, Cell Nucleus, medicine.diagnostic_test, Fkbp25, lcsh:QP1-981, Chemistry, Ribosome Subunits, Large, Eukaryotic, 60S Ribosomal Protein L7a, Cell Hypoxia, Cell biology, 030104 developmental biology, Förster resonance energy transfer, 60S ribosomal protein L7a, Nuclear transport, Peroxynitrite, Signal Transduction
Abstract

Background/Aims: Peptidyl-prolyl cis-trans isomerase FKBP25 is a member of the FK506-binding proteins family which has peptidyl-prolyl cis/trans isomerase domain. The biological function and pathophysiologic role of FKBP25 remain elusive. Methods: The spatio-temporal changes in expression of endothelial FKBP25 upon oxygen-glucose deprivation (OGD) treatment were examined by Western blot and immunofluorescence. The immunoprecipitation and fluorescence resonance energy transfer (FRET) were used to address the interacting proteins with FKBP25. Results: In the present study, nuclear translocation of FKBP25 was observed following OGD in cultured endothelial cells. Intriguingly, FKBP25 nuclear translocation was further validated in peroxynitrite (ONOO-)-treated endothelial cells. Coimmunoprecipitation and FRET data indicated that FKBP25 translocated into the nucleus, in which it interacted with 60S ribosomal protein L7a, while overexpression FKBP25 protect endothelial cells against OGD injury. Conclusion: Our findings reveal that the nuclear import of FKBP25 and binding with 60S ribosomal protein L7a are protective stress responses to ischemia/nitrosaive stress injury.

Published
2018

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