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Control of calcium(2+) dynamics in T...
~
Bautista, Diana Michele.
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Control of calcium(2+) dynamics in T cells: A new role for the plasma membrane calcium(2+)-ATPase.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Control of calcium(2+) dynamics in T cells: A new role for the plasma membrane calcium(2+)-ATPase./
作者:
Bautista, Diana Michele.
面頁冊數:
116 p.
附註:
Adviser: Richard S. Lewis.
Contained By:
Dissertation Abstracts International63-04B.
標題:
Biology, Animal Physiology. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048490
ISBN:
0493628215
Control of calcium(2+) dynamics in T cells: A new role for the plasma membrane calcium(2+)-ATPase.
Bautista, Diana Michele.
Control of calcium(2+) dynamics in T cells: A new role for the plasma membrane calcium(2+)-ATPase.
- 116 p.
Adviser: Richard S. Lewis.
Thesis (Ph.D.)--Stanford University, 2002.
The amplitude and dynamic structure of Ca<super>2+</super> signals in T cells play an important role in determining the efficiency and specificity of signal transduction. This dissertation explores the role of the PMCA in shaping Ca<super>2+</super>, signals in Jurkat human leukemic T cells. The introductory Chapter provides an overview of the mechanisms and functions of Ca<super>2+</super> signals in T cells. The second chapter describes the materials and methods used in the experiments discussed herein. The third chapter examines the role of Ca<super>2+</super> clearance mechanisms in shaping Ca<super>2+</super> responses in Jurkat T cells. Single-cell voltage-clamp and calcium imaging experiments reveal that the PMCA is the primary extrusion mechanism in these cells and that its activity is slowly modulated by changes in [Ca<super>2+</super>]<sub>i</sub>. As the primary Ca<super>2+</super> clearance mechanism, PMCA activity and modulation play a major role in determining the spatiotemporal profile of Ca<super>2+</super> signals in T cells. The fourth chapter discusses a novel Ca<super>2+</super>-clamp technique designed to quantitatively control the concentration of cytosolic calcium. The Ca<super> 2+</super>-clamp generates [Ca<super>2+</super>]<sub>i</sub> steps ranging from 0.3–1.5μM with a risetime of a few seconds and duration >5 min. Using the Ca<super>2+</super>-clamp, PMCA activity was measured in single cells in order to characterize the Ca<super>2+</super>-dependence of PMCA modulation. The fifth and final Chapter examines the functional organization of PMCA and Ca<super>2+</super>-release activated Ca<super>2+</super> (CRAC) channels in T cells. I provide the first evidence that there is a close functional coupling between PMCAs and CRAC channels. This dissertation thus demonstrates that the Plasma Membrane Ca<super>2+</super>-pump actively contributes to the complexity of Ca<super>2+</super> signaling in T cells and constitutes an important part of a complex and highly interconnected Ca<super>2+</super> signaling machine.
ISBN: 0493628215Subjects--Topical Terms:
1017835
Biology, Animal Physiology.
Control of calcium(2+) dynamics in T cells: A new role for the plasma membrane calcium(2+)-ATPase.
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The amplitude and dynamic structure of Ca<super>2+</super> signals in T cells play an important role in determining the efficiency and specificity of signal transduction. This dissertation explores the role of the PMCA in shaping Ca<super>2+</super>, signals in Jurkat human leukemic T cells. The introductory Chapter provides an overview of the mechanisms and functions of Ca<super>2+</super> signals in T cells. The second chapter describes the materials and methods used in the experiments discussed herein. The third chapter examines the role of Ca<super>2+</super> clearance mechanisms in shaping Ca<super>2+</super> responses in Jurkat T cells. Single-cell voltage-clamp and calcium imaging experiments reveal that the PMCA is the primary extrusion mechanism in these cells and that its activity is slowly modulated by changes in [Ca<super>2+</super>]<sub>i</sub>. As the primary Ca<super>2+</super> clearance mechanism, PMCA activity and modulation play a major role in determining the spatiotemporal profile of Ca<super>2+</super> signals in T cells. The fourth chapter discusses a novel Ca<super>2+</super>-clamp technique designed to quantitatively control the concentration of cytosolic calcium. The Ca<super> 2+</super>-clamp generates [Ca<super>2+</super>]<sub>i</sub> steps ranging from 0.3–1.5μM with a risetime of a few seconds and duration >5 min. Using the Ca<super>2+</super>-clamp, PMCA activity was measured in single cells in order to characterize the Ca<super>2+</super>-dependence of PMCA modulation. The fifth and final Chapter examines the functional organization of PMCA and Ca<super>2+</super>-release activated Ca<super>2+</super> (CRAC) channels in T cells. I provide the first evidence that there is a close functional coupling between PMCAs and CRAC channels. This dissertation thus demonstrates that the Plasma Membrane Ca<super>2+</super>-pump actively contributes to the complexity of Ca<super>2+</super> signaling in T cells and constitutes an important part of a complex and highly interconnected Ca<super>2+</super> signaling machine.
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