Calcium- and ATP-dependent regulation of Na/Ca exchange function in BHK cells: Comparison of NCX1 and NCX3 exchangers

Cell Calcium ◽  
2018 ◽  
Vol 73 ◽  
pp. 95-103 ◽  
Author(s):  
Vincenzo Lariccia ◽  
Salvatore Amoroso
Keyword(s):  
1971 ◽  
Vol 246 (8) ◽  
pp. 2721-2723 ◽  
Author(s):  
Halina Den ◽  
Alan M. Schultz ◽  
Manju Basu ◽  
Saul Roseman
Keyword(s):  

2007 ◽  
Vol 98 (4) ◽  
pp. 825-841 ◽  
Author(s):  
Toey Nivitchanyong ◽  
Amanda Martinez ◽  
Adiba Ishaque ◽  
John E. Murphy ◽  
Konstantin Konstantinov ◽  
...  

2013 ◽  
Vol 94 (7) ◽  
pp. 1486-1495 ◽  
Author(s):  
Graham J. Belsham

The foot-and-mouth disease virus (FMDV) Leader (L) protein is produced in two forms, Lab and Lb, differing only at their amino-termini, due to the use of separate initiation codons, usually 84 nt apart. It has been shown previously, and confirmed here, that precise deletion of the Lab coding sequence is lethal for the virus, whereas loss of the Lb coding sequence results in a virus that is viable in BHK cells. In addition, it is now shown that deletion of the ‘spacer’ region between these two initiation codons can be tolerated. Growth of the virus precisely lacking just the Lb coding sequence resulted in a previously undetected accumulation of frameshift mutations within the ‘spacer’ region. These mutations block the inappropriate fusion of amino acid sequences to the amino-terminus of the capsid protein precursor. Modification, by site-directed mutagenesis, of the Lab initiation codon, in the context of the virus lacking the Lb coding region, was also tolerated by the virus within BHK cells. However, precise loss of the Lb coding sequence alone blocked FMDV replication in primary bovine thyroid cells. Thus, the requirement for the Leader protein coding sequences is highly dependent on the nature and extent of the residual Leader protein sequences and on the host cell system used. FMDVs precisely lacking Lb and with the Lab initiation codon modified may represent safer seed viruses for vaccine production.


2004 ◽  
Vol 32 (5) ◽  
pp. 1240-1241
Author(s):  
John G. Laffey ◽  
Brian P. Kavanagh

1989 ◽  
Vol 11 (12) ◽  
pp. 830-836 ◽  
Author(s):  
M. Kiremitçi ◽  
M. Özilgen ◽  
E. Pişkin

1982 ◽  
Vol 208 (2) ◽  
pp. 473-478 ◽  
Author(s):  
D D McAbee ◽  
F Grinnell

Studies were carried out to learn more about the critical SH groups involved in cell spreading. Pretreatment of suspended baby hamster kidney (BHK) cells with 3 mM-iodoacetate or iodoacetamide for 10 min at 4 degrees C completely inhibited the ability of the cells to spread on fibronectin-coated substrata. If, however, BHK cells were permitted to attach and spread before being treated with the SH-binding reagents, and then harvested by trypsinization and assayed for spreading on fibronectin-coated substrata, there was no inhibition of cell spreading. The extent of prior attachment required before the cells became insensitive to the SH-binding reagents was tested and was found to occur early during the cell adhesion process, before any cell spreading was observed. In analytical experiments, there did not appear to be any difference in the total number of SH groups between suspended or spread cells as determined with 5,5′-dithiobis-(2-nitrobenzoic acid). The uptake of radiolabelled iodoacetate into intact spread cells, however, was found to be 3.5 times less than that found with suspended cells. On the other hand, the distribution of incorporated radioactivity into suspended and spread cells was similar. Most of the radioactivity (approximately 70%) was incorporated into small molecules (e.g. glutathione and cysteine), less (approximately 20%) was incorporated into cytoplasmic proteins, and the least incorporation (approximately 10%) was into the cell cytoskeleton. The data are interpreted to indicate there is a decreased permeability of spread cells to the SH-binding reagents.


Sign in / Sign up

Export Citation Format

Share Document