scholarly journals Authors’ Reply: Pyridine nucleotide regulation of hepatic endoplasmic reticulum calcium uptake

2019 ◽  
Vol 7 (19) ◽  
Author(s):  
Kenneth L. McCormick
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Uptake ◽  
Pyridine Nucleotide ◽  
Endoplasmic Reticulum Calcium ◽  
Nucleotide Regulation

scholarly journals Both WFS1 and CISD2 are required for endoplasmic reticulum calcium uptake, which controls mitochondrial function in neurons

IBRO Reports ◽  
2019 ◽  
Vol 6 ◽  
pp. S228
Author(s):  
Allen Kaasik ◽  
Mailis Liiv ◽  
Annika Vaarmann ◽  
Malle Kuum ◽  
Dzamilja Safiulina ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mitochondrial Function ◽  
Calcium Uptake ◽  
Endoplasmic Reticulum Calcium

scholarly journals Bid agonist regulates murine hepatocyte proliferation by controlling endoplasmic reticulum calcium homeostasis

Hepatology ◽  
2010 ◽  
Vol 52 (1) ◽  
pp. 338-348 ◽  
Author(s):  
Hong-Min Ni ◽  
Catherine J. Baty ◽  
Na Li ◽  
Wen-Xing Ding ◽  
Wentao Gao ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Homeostasis ◽  
Hepatocyte Proliferation ◽  
Endoplasmic Reticulum Calcium ◽  
Murine Hepatocyte

Presenilin 1 is a direct regulator of the cardiac sarco/endoplasmic reticulum calcium pump

Cell Calcium ◽  
2021 ◽  
pp. 102468
Author(s):  
Elisa Bovo ◽  
Roman Nikolaienko ◽  
Daniel Kahn ◽  
Ellen Cho ◽  
Seth L. Robia ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Pump ◽  
Presenilin 1 ◽  
Endoplasmic Reticulum Calcium ◽  
Direct Regulator

scholarly journals Endoplasmic reticulum calcium pool depletion-induced apoptosis is coupled with activation of the death receptor 5 pathway

Oncogene ◽  
2002 ◽  
Vol 21 (17) ◽  
pp. 2623-2633 ◽  
Author(s):  
Qin He ◽  
Dong Ik Lee ◽  
Rong Rong ◽  
Myounghee Yu ◽  
Xiuquan Luo ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Death Receptor ◽  
Death Receptor 5 ◽  
Endoplasmic Reticulum Calcium ◽  
Induced Apoptosis ◽  
Calcium Pool

scholarly journals Overexpression of CALNUC (Nucleobindin) Increases Agonist and Thapsigargin Releasable Ca2+ Storage in the Golgi

1999 ◽  
Vol 145 (2) ◽  
pp. 279-289 ◽  
Author(s):  
Ping Lin ◽  
Yong Yao ◽  
Robert Hofmeister ◽  
Roger Y. Tsien ◽  
Marilyn Gist Farquhar
Keyword(s):  
Endoplasmic Reticulum ◽  
Cho Cells ◽  
Binding Capacity ◽  
Binding Protein ◽  
Ip3 Receptor ◽  
Transfected Cells ◽  
Permeabilized Cells ◽  
Endoplasmic Reticulum Calcium ◽  
Golgi Protein

We previously demonstrated that CALNUC, a Ca2+-binding protein with two EF-hands, is the major Ca2+-binding protein in the Golgi by 45Ca2+ overlay (Lin, P., H. Le-Niculescu, R. Hofmeister, J.M. McCaffery, M. Jin, H. Henneman, T. McQuistan, L. De Vries, and M. Farquhar. 1998. J. Cell Biol. 141:1515–1527). In this study we investigated CALNUC's properties and the Golgi Ca2+ storage pool in vivo. CALNUC was found to be a highly abundant Golgi protein (3.8 μg CALNUC/mg Golgi protein, 2.5 × 105 CALNUC molecules/NRK cell) and to have a single high affinity, low capacity Ca2+-binding site (Kd = 6.6 μM, binding capacity = 1.1 μmol Ca2+/μmol CALNUC). 45Ca2+ storage was increased by 2.5- and 3-fold, respectively, in HeLa cells transiently overexpressing CALNUC-GFP and in EcR-CHO cells stably overexpressing CALNUC. Deletion of the first EF-hand α helix from CALNUC completely abolished its Ca2+-binding capability. CALNUC was correctly targeted to the Golgi in transfected cells as it colocalized and cosedimented with the Golgi marker, α-mannosidase II (Man II). Approximately 70% of the 45Ca2+ taken up by HeLa and CHO cells overexpressing CALNUC was released by treatment with thapsigargin, a sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA) (Ca2+ pump) blocker. Stimulation of transfected cells with the agonist ATP or IP3 alone (permeabilized cells) also resulted in a significant increase in Ca2+ release from Golgi stores. By immunofluorescence, the IP3 receptor type 1 (IP3R-1) was distributed over the endoplasmic reticulum and codistributed with CALNUC in the Golgi. These results provide direct evidence that CALNUC binds Ca2+ in vivo and together with SERCA and IP3R is involved in establishment of the agonist-mobilizable Golgi Ca2+ store.

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