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Remodeling of the ryanodine receptor...
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Columbia University.
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Remodeling of the ryanodine receptor complex during muscle stress.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Remodeling of the ryanodine receptor complex during muscle stress./
作者:
Bellinger, Andrew Martin.
面頁冊數:
126 p.
附註:
Adviser: Andrew R. Marks.
Contained By:
Dissertation Abstracts International68-11B.
標題:
Biology, Molecular. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3290504
ISBN:
9780549338956
Remodeling of the ryanodine receptor complex during muscle stress.
Bellinger, Andrew Martin.
Remodeling of the ryanodine receptor complex during muscle stress.
- 126 p.
Adviser: Andrew R. Marks.
Thesis (Ph.D.)--Columbia University, 2008.
Over the past century the mechanisms underlying muscle fatigue have been the subject of much investigation. These investigations have met with limited success, in part due to the failure of the field's dominant theory, introduced by A.V. Hill and Otto Meyerhof in the 1920's, which held that lactic acidosis causes muscle fatigue. The fact that numerous unrelated chronic diseases are associated with muscle fatigue---despite the absence of a clear unifying principle---has formed an additional challenge to developing a unifying theory that explains muscle fatigue.
ISBN: 9780549338956Subjects--Topical Terms:
1017719
Biology, Molecular.
Remodeling of the ryanodine receptor complex during muscle stress.
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Over the past century the mechanisms underlying muscle fatigue have been the subject of much investigation. These investigations have met with limited success, in part due to the failure of the field's dominant theory, introduced by A.V. Hill and Otto Meyerhof in the 1920's, which held that lactic acidosis causes muscle fatigue. The fact that numerous unrelated chronic diseases are associated with muscle fatigue---despite the absence of a clear unifying principle---has formed an additional challenge to developing a unifying theory that explains muscle fatigue.
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A promising line of research has yielded new understanding of the impaired muscle function associated with chronic stress by exploring the regulation of sarcoplasmic reticulum (SR) calcium (Ca2+) release and reuptake in skeletal muscle. SR Ca2+ release and reuptake are the key components of excitationcontraction coupling (E-C coupling) which is required for skeletal muscle contraction. Stress signals modulate SR Ca2+ handling. In particular, the major SR Ca2+ release channel, the type 1 ryanodine receptor (RyR1) is a target of multiple stress signaling pathways. During repeated exercise, PKA phosphorylation of RyR1 results in depletion of a stabilizing subunit calstabin1 (FKBP12) from the RyR1 macromolecular complex, resulting in leaky channels. The RyR1 macromolecular defect is associated with a reduction in exercise capacity and muscle damage. In a mouse model of Duchenne Muscular Dystrophy (mdx mouse) RyR1 is nitrosylated on free cysteine thiols, which also results in depletion of calstabin1 from the RyR1 complex. Rebinding of calstabin1 to RyR1 with small molecules (∼300 MW) that bind to RyR1 and enhance the binding affinity of calstabin1 to nitrosylated or PKA phosphorylated channels improve muscle function and reduce muscle damage. Therefore, we have proposed that RyR1 is a central target of stress signaling and that dysfunction of RyR1 may play an important role in stress-induced muscle disorders associated with impaired exercise capacity.
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