Calcium Signaling at the Blood–Brain Barrier in Stroke

2012 ◽  
pp. 129-163
Author(s):  
Rachel C. Brown
2006 ◽  
Vol 116 (10) ◽  
pp. 2739-2747 ◽  
Author(s):  
O. V. Nikolskaia ◽  
A. P. C. de A. Lima ◽  
Y. V. Kim ◽  
J. D. Lonsdale-Eccles ◽  
T. Fukuma ◽  
...  

2019 ◽  
Vol 2 ◽  
pp. 165
Author(s):  
Monica Namyanja ◽  
Zhi-Shen Xu ◽  
Claire Mack Mugasa ◽  
Zhao-Rong Lun ◽  
Enock Matovu ◽  
...  

Background: Trypanosoma brucei, a causative agent of African Trypanosomiasis, is known to cross the blood brain barrier during the second stage of the disease. It was previously suggested that this parasite crosses the blood brain barrier in a manner similar to that of lymphocytes. This would imply that trypanosomes possess integrins that are required to interact with adhesion molecules located on the blood brain barrier microvascular endothelial cells, as a first step in traversal. To date, no T. brucei integrin has been described. However, one T. brucei putative FG-GAP repeat containing protein (typical of integrins) encoded by the Tb927.11.720 gene, was predicted to be involved in cell-cell/cell-matrix adhesion. Therefore, this study sought to characterize a putative FG-GAP repeat containing protein (FG-GAP RCP) and to determine its cellular localization as a basis for further exploration of its potential role in cell-cell or cell-matrix adhesion. Methods: In this study, we successfully cloned, characterized, expressed and localized this protein using antibodies we produced against its VCBS domain in T. brucei. Results: Contrary to what we initially suspected, our data showed that this protein is localized to the mitochondria but not the plasma membrane. Our data showed that it contains putative calcium binding motifs within the FG-GAP repeats suggesting it could be involved in calcium signaling/binding in the mitochondrion of T. brucei. Conclusion: Based on its localization we conclude that this protein is unlikely to be a trypanosomal integrin and thus that it may not be involved in traversal of the blood brain barrier. However, it could be involved in calcium signaling in the mitochondrion.


2008 ◽  
Vol 118 (5) ◽  
pp. 1974-1974 ◽  
Author(s):  
Olga V. Nikolskaia ◽  
Ana Paula C. de A. Lima ◽  
Yuri V. Kim ◽  
John D. Lonsdale-Eccles ◽  
Toshihide Fukuma ◽  
...  

2015 ◽  
Vol 36 (6) ◽  
pp. 1098-1110 ◽  
Author(s):  
Hwajin Kim ◽  
Heeyoung Kang ◽  
Rok Won Heo ◽  
Byeong Tak Jeon ◽  
Chin-ok Yi ◽  
...  

Diabetes-induced cognitive decline has been recognized in human patients of type 2 diabetes mellitus and mouse model of obesity, but the underlying mechanisms or therapeutic targets are not clearly identified. We investigated the effect of caloric restriction on diabetes-induced memory deficits and searched a molecular mechanism of caloric restriction-mediated neuroprotection. C57BL/6 mice were fed a high-fat diet for 40 weeks and RNA-seq analysis was performed in the hippocampus of high-fat diet-fed mice. To investigate caloric restriction effect on differential expression of genes, mice were fed high-fat diet for 20 weeks and continued on high-fat diet or subjected to caloric restriction (2 g/day) for 12 weeks. High-fat diet-fed mice exhibited insulin resistance, glial activation, blood–brain barrier leakage, and memory deficits, in that we identified neurogranin, a down-regulated gene in high-fat diet-fed mice using RNA-seq analysis; neurogranin regulates Ca2+/calmodulin-dependent synaptic function. Caloric restriction increased insulin sensitivity, reduced high-fat diet-induced blood–brain barrier leakage and glial activation, and improved memory deficit. Furthermore, caloric restriction reversed high-fat diet-induced expression of neurogranin and the activation of Ca2+/calmodulin-dependent protein kinase II and calpain as well as the downstream effectors. Our results suggest that neurogranin is an important factor of high-fat diet-induced memory deficits on which caloric restriction has a therapeutic effect by regulating neurogranin-associated calcium signaling.


1996 ◽  
Vol 22 (2) ◽  
pp. 118-128 ◽  
Author(s):  
S. Isenmann ◽  
S. Brandner ◽  
G. Kuhne ◽  
J. Boner ◽  
A. Aguzzi

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