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Endoplasmic reticulum stress in periimplantation embryos
Michalak, Marek,Gye, Myung Chan The Korean Society for Reproductive Medicine 2015 Clinical and Experimental Reproductive Medicine Vol.42 No.1
Stress coping mechanisms are critical to minimize or overcome damage caused by ever changing environmental conditions. They are designed to promote cell survival. The unfolded protein response (UPR) pathway is mobilized in response to the accumulation of unfolded proteins, ultimately in order to regain endoplasmic reticulum (ER) homeostasis. Various elements of coping responses to ER stress including Perk, Ask1, Bip, Chop, Gadd34, Ire1, Atf4, Atf6, and Xbp1 have been identified and were found to be inducible in oocytes and preimplantation embryos, suggesting that, as a normal part of the cellular adaptive mechanism, these coping responses, including the UPR, play a pivotal role in the development of preimplantation embryos. As such, the UPR-associated molecules and pathways may become useful markers for the potential diagnosis of stress conditions for preimplantation embryos. After implantation, ER stress-induced coping responses become physiologically important for a normal decidual response, placentation, and early organogenesis. Attenuation of ER stress coping responses by tauroursodeoxycholate and salubrinal was effective for prevention of cell death of cultured embryos. Further elucidation of new and relevant ER stress coping responses in periimplantation embryos might contribute to a comprehensive understanding of the regulation of normal development of embryonic development and potentiation of embryonic development in vitro.
Calcium and bioenergetics: from endoplasmic reticulum to mitochondria
Dukgyu Lee,Marek Michalak 한국통합생물학회 2012 Animal cells and systems Vol.16 No.4
Controlling metabolism throughout life is a necessity for living creatures, and perturbation of energy balance elicits disorders such as type-2 diabetes mellitus and cardiovascular disease. Ca2+ plays a key role in regulating energy generation. Ca2+ homeostasis of the endoplasmic reticulum (ER) lumen is maintained through the action of Ca2+ channels and the Ca2+ ATPase pump. Once released from the ER, Ca2+ is taken up by mitochondria where it facilitates energy metabolism. Mitochondrial Ca2+ serves as a key metabolic regulator and determinant of cell fate, necrosis, and/or apoptosis. Here, we focus on Ca2+ transport from the ER to mitochondria, and Ca2+-dependent regulation of mitochondrial energy metabolism.
Calcium and bioenergetics: from endoplasmic reticulum to mitochondria
Lee, Duk-Gyu,Michalak, Marek The Korean Society for Integrative Biology 2012 Animal cells and systems Vol.16 No.4
Controlling metabolism throughout life is a necessity for living creatures, and perturbation of energy balance elicits disorders such as type-2 diabetes mellitus and cardiovascular disease. $Ca^{2+}$ plays a key role in regulating energy generation. $Ca^{2+}$ homeostasis of the endoplasmic reticulum (ER) lumen is maintained through the action of $Ca^{2+}$ channels and the $Ca^{2+}$ ATPase pump. Once released from the ER, $Ca^{2+}$ is taken up by mitochondria where it facilitates energy metabolism. Mitochondrial $Ca^{2+}$ serves as a key metabolic regulator and determinant of cell fate, necrosis, and/or apoptosis. Here, we focus on $Ca^{2+}$ transport from the ER to mitochondria, and $Ca^{2+}$-dependent regulation of mitochondrial energy metabolism.
Inositol Requiring Enzyme (IRE), a multiplayer in sensing endoplasmic reticulum stress
Zhixin Zhou,Qian Wang,Marek Michalak 한국통합생물학회 2021 Animal cells and systems Vol.25 No.6
The endoplasmic reticulum (ER) can sense a wide variety of external and internal perturbations and responds by mounting stress coping responses, such as the unfolded protein response (UPR). The UPR is composed of three stress sensors, namely IRE1α, PERK, and ATF6 that are activated to reestablish ER homeostasis. IRE1α represents the most ancient branch of the UPR affecting many cellular processes in plant and animal cells. IRE1α is a type I transmembrane protein with kinase/nuclease activities in response to ER stress. Both the ER luminal and cytosolic IRE1α interactomes have been identified revealing a multifunctional role of the ER stress sensor. IRE1α is also associated with organellar membrane contacts to promote rapid communication between intracellular organelles under stress conditions.
Mini Review : Membrane associated Ca2+ buffers in the heart
( Duk Gyu Lee ),( Marek Michalak ) 한국생화학분자생물학회 (구 한국생화학회) 2010 BMB Reports Vol.43 No.3
Ca2+ is a universal signalling molecule that affects a variety of cellular processes including cardiac development. The majority of intracellular Ca2+ is stored in the endoplasmic and sarcoplasmic reticulum of muscle and non-muscle cells. Calreticulin is a well studied Ca2+-buffering protein in the endoplasmic reticulum, and calreticulin deficiency is embryonic lethal due to impaired cardiac development. Despite calsequestrin being the most abundant Ca2+-buffering protein in the sarcoplasmic reticulum, viability is maintained in embryos without calsequestrin and normal Ca2+ release and contractile function is observed. The Ca2+ homeostasis regulated by the endoplasmic and sarcoplasmic reticulum is critical for the development and proper function of the heart. [BMB reports 2010; 43(3): 151-157]
Biology of Endoplasmic Reticulum Stress in the Heart
Groenendyk, Jody,Sreenivasaiah, Pradeep Kumar,Kim, Do Han,Agellon, Luis B.,Michalak, Marek Ovid Technologies Wolters Kluwer -American Heart A 2010 Circulation research Vol.107 No.10
<P>The endoplasmic reticulum (ER) is a multifunctional intracellular organelle supporting many processes required by virtually every mammalian cell, including cardiomyocytes. It performs diverse functions, including protein synthesis, translocation across the membrane, integration into the membrane, folding, posttranslational modification including N-linked glycosylation, and synthesis of phospholipids and steroids on the cytoplasmic side of the ER membrane, and regulation of Ca(2+) homeostasis. Perturbation of ER-associated functions results in ER stress via the activation of complex cytoplasmic and nuclear signaling pathways, collectively termed the unfolded protein response (UPR) (also known as misfolded protein response), leading to upregulation of expression of ER resident chaperones, inhibition of protein synthesis and activation of protein degradation. The UPR has been associated with numerous human pathologies, and it may play an important role in the pathophysiology of the heart. ER stress responses, ER Ca(2+) buffering, and protein and lipid turnover impact many cardiac functions, including energy metabolism, cardiogenesis, ischemic/reperfusion, cardiomyopathies, and heart failure. ER proteins and ER stress-associated pathways may play a role in the development of novel UPR-targeted therapies for cardiovascular diseases.</P>