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You searched for +publisher:"Temple University" +contributor:("Sheu, Shey-Shing;"). Showing records 1 – 2 of 2 total matches.

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Temple University

1. Hoffman, Nicholas. Mitochondrial Calcium Influx is Determined by Multiple Protein Components Including SLC25A23 and MICU1.

Degree: PhD, 2014, Temple University

Biochemistry

Ca2+ control mechanisms employed by the cell at the plasma membrane include receptor operated, voltage-sensitive, and store operated channels for Ca2+ import. Upon entry into the cytosol, Ca2+ is sequestered by Ca2+ binding proteins, the endoplasmic reticulum (ER), or by mitochondria. The largest Ca2+ store in the cell is the ER where Ca2+ levels approach millimolar levels. The ER regulates cytosolic Ca2+ homeostasis by using Ca2+ binding proteins, the SERCA pump, second messenger Ca2+ release upon IP3 receptor activation, and Ca2+-induced Ca2+ release by ryanodine receptors. Basal cytosolic Ca2+ levels are maintained at around 100nM. The mitochondria begins clearing GPRC-depended cytosolic Ca2+elevation after a short time delay during which the cytosolic Ca2+ concentration exceeds 3M. Then, the mitochondria sacrifices a portion of its membrane potential to drive Ca2+ influx across the mitochondrial inner membrane into the matrix. The membrane potential of the mitochondria is created in part by the electron transport, which while transferring electrons, ejects protons from the matrix to the inner membrane space. The rapid mitochondrial Ca2+ uptake decreases mitochondrial membrane potential thus reducing or fully collapsing the mitochondria's ability to generate ATP. This uncoupling of the electron transport chain results in ROS production and decreased cell survival. Mitochondria provide the body with energy that allows a heart to beat, a brain to store memories, and fuels locomotive function. As a stand-alone energy generator, the mitochondria would be interesting, but not dynamic. The dynamic flow of information to the mitochondria through Ca2+ signaling with all the components of symbiotic precision is a true biological phenomenon. In the mitochondria, a complex Ca2+ buffering system of channels, pores, and exchangers directly affects the conversion of chemical potential to ATP. Recent, discoveries of the Ca2+ uniporter (MCU) and other system components have provided the tools to tackle levels of mitochondrion physiologic studies that were not possible only a couple of years ago. There remains a great need for advancement in the understanding of mitochondrial bioenergetics, and undoubtedly, the mitochondria will be viewed as a determinant factor for survival. The mitochondrial inner membrane through its curious construction of 3:1 protein to lipid ratio, carefully regulates the permeability of ions and metabolites. The transport of Ca2+ and other small ions across the inner membrane is an essential signaling pathway for mitochondrial maintenance of metabolic functions, but the mechanisms are still unclear due to a lack of mitochondrial systems biology. For example, the oligomeric MCU with two transmembrane domains is a core component of the major Ca2+ import pathway in mitochondria, and ablation of MCU lowers mitochondrial Ca2+ uptake, however portions such as the highly conserved linker between the two transmembrane was unstudied until recently. Other complex components such as MICU1 and…

Advisors/Committee Members: Muniswamy, Madesh;, Soboloff, Jonathan, Haines, Dale, Elrod, John W., Sheu, Shey-Shing;.

Subjects/Keywords: Biochemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Hoffman, N. (2014). Mitochondrial Calcium Influx is Determined by Multiple Protein Components Including SLC25A23 and MICU1. (Doctoral Dissertation). Temple University. Retrieved from http://digital.library.temple.edu/u?/p245801coll10,287159

Chicago Manual of Style (16th Edition):

Hoffman, Nicholas. “Mitochondrial Calcium Influx is Determined by Multiple Protein Components Including SLC25A23 and MICU1.” 2014. Doctoral Dissertation, Temple University. Accessed April 14, 2021. http://digital.library.temple.edu/u?/p245801coll10,287159.

MLA Handbook (7th Edition):

Hoffman, Nicholas. “Mitochondrial Calcium Influx is Determined by Multiple Protein Components Including SLC25A23 and MICU1.” 2014. Web. 14 Apr 2021.

Vancouver:

Hoffman N. Mitochondrial Calcium Influx is Determined by Multiple Protein Components Including SLC25A23 and MICU1. [Internet] [Doctoral dissertation]. Temple University; 2014. [cited 2021 Apr 14]. Available from: http://digital.library.temple.edu/u?/p245801coll10,287159.

Council of Science Editors:

Hoffman N. Mitochondrial Calcium Influx is Determined by Multiple Protein Components Including SLC25A23 and MICU1. [Doctoral Dissertation]. Temple University; 2014. Available from: http://digital.library.temple.edu/u?/p245801coll10,287159


Temple University

2. Li, Xinyuan. Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-induced Endothelial Cell Activation.

Degree: PhD, 2015, Temple University

Pharmacology

Lysophosphatidylcholines (LPCs) are a class of pro-inflammatory lipids that play important roles in atherogenesis. LPC activates endothelial cells (ECs) to upregulate adhesion molecules, cytokines and chemokines, which is the initiation step of atherogenesis. However, the mechanisms underlying LPC-triggered EC activation are not fully understood. Previously considered as the toxic by-products of cellular metabolism, mitochondrial reactive oxygen species (mtROS) are recently found to directly contribute to both the innate and adaptive immune responses. Here we tested a novel hypothesis that mtROS serve as signaling mediators for LPC-induced EC activation. Using electron spin resonance and flow cytometry with mtROS-specific fluorescence probe MitoSOX, we found that several LPC species including LPC 16:0, 18:0, and 18:1 induced mtROS in human primary aortic ECs (HAECs). Mechanistically, our analysis using confocal microscopy and Seahorse XF96 mitochondrial function analyzer showed that LPC induced mtROS via increasing mitochondrial calcium-mediated increase of mitochondrial respiration. In addition, we found that mtROS scavenger MitoTEMPO abolished LPC-induced EC activation by downregulating Intercellular adhesion molecule 1 (ICAM-1) in HAECs. Moreover, our analysis with mass spectrometer analysis of histone H3 lysine acetylation and electrophoretic mobility shift assay (EMSA) showed that MitoTEMPO acts by blocking LPC-induced histone H3 lysine 14 acetylation (H3K14ac) and nuclear translocation of pro-inflammatory transcription factor activator protein-1 (AP-1). Remarkably, all the above effects can be inhibited by anti-inflammatory cytokines interleukin (IL-35) and IL-10. Our results indicate that mtROS are responsible for LPC-induced EC activation, which can be inhibited by anti-inflammatory cytokines. MtROS targeting therapies and anti-inflammatory cytokines such as IL-35 may serve as novel therapeutic targets for vascular inflammation and cardiovascular diseases. The studies in this dissertation were supported by grants from the National Institutes of Health (NIH) funded to Dr. Xiao-Feng Yang.

Temple University – Theses

Advisors/Committee Members: Yang, Xiao-Feng;, Wang, Hong, Ashby, Barrie, Tilley, Douglas G., Madesh, Muniswamy, Sheu, Shey-Shing;.

Subjects/Keywords: Pharmacology; Immunology; Cellular biology;

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Li, X. (2015). Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-induced Endothelial Cell Activation. (Doctoral Dissertation). Temple University. Retrieved from http://digital.library.temple.edu/u?/p245801coll10,320473

Chicago Manual of Style (16th Edition):

Li, Xinyuan. “Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-induced Endothelial Cell Activation.” 2015. Doctoral Dissertation, Temple University. Accessed April 14, 2021. http://digital.library.temple.edu/u?/p245801coll10,320473.

MLA Handbook (7th Edition):

Li, Xinyuan. “Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-induced Endothelial Cell Activation.” 2015. Web. 14 Apr 2021.

Vancouver:

Li X. Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-induced Endothelial Cell Activation. [Internet] [Doctoral dissertation]. Temple University; 2015. [cited 2021 Apr 14]. Available from: http://digital.library.temple.edu/u?/p245801coll10,320473.

Council of Science Editors:

Li X. Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-induced Endothelial Cell Activation. [Doctoral Dissertation]. Temple University; 2015. Available from: http://digital.library.temple.edu/u?/p245801coll10,320473

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