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The role of endoplasmic reticulum quality control system in the biology of the major myelin glycoproteins
DownloadFall 2011
ABSTRACT Endoplasmic reticulum (ER) plays an essential role in the proper folding, maturation and quality control of newly synthesized membrane and secretory proteins. The ER contains molecular chaperones and unique enzymes that assist in protein folding and catalyze co- and post-translational...
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Fall 2018
Sudden unexplained death (SUD) is a term used when comprehensive medical examination and autopsy fail to find a conclusive cause of sudden death. In cases of SUD, post-mortem molecular and genetic evaluation methods have helped identify ion channel abnormalities leading to arrhythmias as cause....
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Fall 2020
Cellular responses to stress are an integral part of cardiovascular physiology and pathology, and endoplasmic reticulum (ER) stress is the key component in the development and progression of various heart diseases. However, the relative contribution of ER stress pathways to muscle damage and...
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Fall 2015
Calcium (Ca2+) ions serve a crucial role in numerous intracellular signaling pathways, controlling physiological functions as diverse as cell proliferation, immune system function, and muscular contraction. As such, the cell has evolved many different mechanisms to precisely control the movement...
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Exploring the Role of Endoplasmic Reticulum Calcium Dynamics in Maintaining Cholesterol Homeostasis
DownloadFall 2018
Calreticulin is an endoplasmic reticulum (ER) protein chaperone and calcium (Ca2+) binding protein and is therefore important for maintaining ER homeostasis. Calreticulin deficiency is embryonic lethal in mice due to inadequate inositol trisphosphate receptor (InsP3R)-mediated Ca2+ signaling and...
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Fall 2022
Calnexin is a type 1 integral endoplasmic reticulum (ER) membrane protein and molecular chaperone involved in the folding and quality control of membrane associated and secreted proteins. The ER luminal domain of calnexin is responsible for the chaperone function, whereas the C-terminal domain is...