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Gamma-interferon Inducible Lysosomal...
~
Shuang, Shao.
Gamma-interferon Inducible Lysosomal Thiol Reductase, Its Secretion and Role in Bacterial Infection.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
書名/作者:
Gamma-interferon Inducible Lysosomal Thiol Reductase, Its Secretion and Role in Bacterial Infection.
作者:
Shuang, Shao.
面頁冊數:
115 p.
附註:
Source: Dissertation Abstracts International, Volume: 76-11(E), Section: B.
Contained By:
Dissertation Abstracts International76-11B(E).
標題:
Biology.
ISBN:
9781321963120
摘要、提要註:
Gamma-interferon inducible lysosomal thiol reductase (GILT) is a unique thioredoxin that reduces disulfide bonds at acidic pH. GILT can be found in the lysosome in its mature form or secreted as a precursor, both of which are active enzymes. Precursor GILT is constitutively secreted into the murine peritoneal extracellular space. Along with the fully glycosylated precursor, multiple underglycosylated GILT precursors are detected in mouse peritoneal fluid and human ascites, indicating an extracellular mechanism of differential deglycosylation in the peritoneal environment. Bacterial infection induces a time-dependent surge in the peritoneal extracellular GILT levels, which, based on in vitro experiments, is largely contributed by peritoneal macrophages. These findings suggest an extracellular role for GILT both in physiological processes and during inflammation. GILT-deficient peritoneal macrophages produce less reactive oxygen species (ROS) in response to bacterial infection, and exhibit delayed bacterial clearance during the early phase of infection. NADPH oxidase inhibitor treatment negates the difference in bacteria-induced ROS generation, suggesting that GILT regulates NADPH oxidase-dependent ROS production. A proteomics screen has uncovered interesting GILT substrates, offering insights into the potential mechanism for GILT on phagosomal ROS production, as well as its function in the extracellular space.
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3663664
Gamma-interferon Inducible Lysosomal Thiol Reductase, Its Secretion and Role in Bacterial Infection.
Shuang, Shao.
Gamma-interferon Inducible Lysosomal Thiol Reductase, Its Secretion and Role in Bacterial Infection.
- 115 p.
Source: Dissertation Abstracts International, Volume: 76-11(E), Section: B.
Thesis (Ph.D.)--Yale University, 2015.
Gamma-interferon inducible lysosomal thiol reductase (GILT) is a unique thioredoxin that reduces disulfide bonds at acidic pH. GILT can be found in the lysosome in its mature form or secreted as a precursor, both of which are active enzymes. Precursor GILT is constitutively secreted into the murine peritoneal extracellular space. Along with the fully glycosylated precursor, multiple underglycosylated GILT precursors are detected in mouse peritoneal fluid and human ascites, indicating an extracellular mechanism of differential deglycosylation in the peritoneal environment. Bacterial infection induces a time-dependent surge in the peritoneal extracellular GILT levels, which, based on in vitro experiments, is largely contributed by peritoneal macrophages. These findings suggest an extracellular role for GILT both in physiological processes and during inflammation. GILT-deficient peritoneal macrophages produce less reactive oxygen species (ROS) in response to bacterial infection, and exhibit delayed bacterial clearance during the early phase of infection. NADPH oxidase inhibitor treatment negates the difference in bacteria-induced ROS generation, suggesting that GILT regulates NADPH oxidase-dependent ROS production. A proteomics screen has uncovered interesting GILT substrates, offering insights into the potential mechanism for GILT on phagosomal ROS production, as well as its function in the extracellular space.
ISBN: 9781321963120Subjects--Topical Terms:
171887
Biology.
Gamma-interferon Inducible Lysosomal Thiol Reductase, Its Secretion and Role in Bacterial Infection.
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Gamma-interferon inducible lysosomal thiol reductase (GILT) is a unique thioredoxin that reduces disulfide bonds at acidic pH. GILT can be found in the lysosome in its mature form or secreted as a precursor, both of which are active enzymes. Precursor GILT is constitutively secreted into the murine peritoneal extracellular space. Along with the fully glycosylated precursor, multiple underglycosylated GILT precursors are detected in mouse peritoneal fluid and human ascites, indicating an extracellular mechanism of differential deglycosylation in the peritoneal environment. Bacterial infection induces a time-dependent surge in the peritoneal extracellular GILT levels, which, based on in vitro experiments, is largely contributed by peritoneal macrophages. These findings suggest an extracellular role for GILT both in physiological processes and during inflammation. GILT-deficient peritoneal macrophages produce less reactive oxygen species (ROS) in response to bacterial infection, and exhibit delayed bacterial clearance during the early phase of infection. NADPH oxidase inhibitor treatment negates the difference in bacteria-induced ROS generation, suggesting that GILT regulates NADPH oxidase-dependent ROS production. A proteomics screen has uncovered interesting GILT substrates, offering insights into the potential mechanism for GILT on phagosomal ROS production, as well as its function in the extracellular space.
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