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Metals such as Cu2+, Fe3+, and Zn2+ are major contributors to the biology of a brain in stages of health, aging, and disease because of their unique effects on both protein structures (misfolding) and oxidative stress. The relationship between metal ions and neurodegenerative diseases is very complicated. Our study highlights how metal ions influence amyloid formation at low pH and on preformed amyloid fibrils. By using thioflavin T assay, ANS fluorescence, Congo red assay, circular dichroism, and microscopy to elucidate the effects of Cu2+, Fe3+, and Zn2+ on goat brain cystatin (GBC) aggregation at low pH. Results showed that Cu2+ and Fe3+ inhibit fibril formation of GBC by promoting amorphous aggregates. However, Zn2+ exclusively promotes fibril formation at low pH, leading to the formation of more ordered aggregates. Furthermore, the combined results of these complementary methods also suggested that Cu2+ and Fe3+ destabilize the β-sheet secondary structure of preformed amyloid fibrils of GBC. 相似文献
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《Molecular cell》2020,77(2):338-351.e6
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《Cell calcium》2018
Store-operated calcium entry (SOCE) is the flow of calcium ions (Ca2+) into cells in response to the depletion of intracellular Ca2+ stores that reside predominantly in the endoplasmic reticulum (ER). The role of SOCE has been relatively well understood for non-excitable cells. It is mediated mostly by the ER Ca2+ sensor STIM1 and plasma membrane Ca2+ channel Orai1 and serves to sustain Ca2+ signaling and refill ER Ca2+ stores. In contrast, because of the complexity of Ca2+ influx mechanisms that are present in excitable cells, our knowledge about the function of neuronal SOCE (nSOCE) is still nascent. This review summarizes the available data on the molecular components of nSOCE and their relevance to neuronal signaling. We also present evidence of disturbances of nSOCE in neurodegenerative diseases (namely Alzheimer’s disease, Huntington’s disease, and Parkinson’s disease) and traumatic brain injury. The emerging important role of nSOCE in neuronal physiology and pathology makes it a possible clinical target. 相似文献
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《Cell》2022,185(20):3753-3769.e18
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Using antibodies raised against human platelet phenol sulfotransferase (PST), immunohistochemical studies were performed to determine the cellular localization of PST in several areas of human brain. In the hippocampus PST immunoreactivity was localized in both the pyramidal and nonpyramidal neurons and was in greatest abundance in the CA2 and CA3 areas. In the striatum the immunoreactivity was most predominant in the large neurons of the globus pallidus and in the medulla the staining was scattered throughout the neurons of the raphe nucleus and the reticular formation. The selective presence of PST in the neurons of the CNS raises the issue as to the role of this enzyme in sulfating neurotransmitters because PST has been shown to be capable of conjugating a variety of neurotransmitters including the catecholamines as well as the tyrosine moiety of a number of small peptides such as enkephalin and cholecystokinin. 相似文献
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《Cell》2021,184(17):4564-4578.e18
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《Cell》2021,184(23):5807-5823.e14
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Min-Kyoo Shin Edwin Vázquez-Rosa Yeojung Koh Matasha Dhar Kalyani Chaubey Coral J. Cintrón-Pérez Sarah Barker Emiko Miller Kathryn Franke Maria F. Noterman Divya Seth Rachael S. Allen Cara T. Motz Sriganesh Ramachandra Rao Lara A. Skelton Machelle T. Pardue Steven J. Fliesler Chao Wang Andrew A. Pieper 《Cell》2021,184(10):2715-2732.e23