Irreversible Inhibition of [3H]Glycine Transport into Channel Catfish Erythrocytes by Thiol Group Modifiers

Pharmacology ◽  
2004 ◽  
Vol 70 (3) ◽  
pp. 113-117 ◽  
Author(s):  
Sara J. McCormick ◽  
Godfrey Tunnicliff
1996 ◽  
Vol 74 (4) ◽  
pp. 688-692 ◽  
Author(s):  
S. M. Angermeier ◽  
M. D. Shepard ◽  
G. Tunnicliff

In humans, glycine enters the red cell via four distinct plasma membrane carrier systems. The purpose of the present experiments was to measure the mode of transport of glycine by channel catfish (Ictalurus punctatus) red cells. About 54% of the glycine was transported by system L, while 16.1% of the glycine was transported by system Gly. A further 15.6% of transport was via system ASC and system asc together. An unidentified Na+-independent system was responsible for the transport of 7.2% of the glycine. No solute appeared to be carried into the cell by band 3. The remainder of the glycine entered the cell by diffusion. The Na+-independent system exhibited a Kt value of 57 ± 12 (mean ± standard deviation) μM and Vmax of 142 ± 27 nmol∙g hemoglobin−1∙min−1 (this compares with system L, which exhibited a Kt value of 65 ± 21 μM and Vmax of 516 ± 117 nmol∙g hemoglobin−1∙min−1). These results demonstrate that channel catfish red cells are capable of transporting glycine by three of the four transporters involved in human red cells, although the relative contributions differ markedly, and by an additional unidentified transport system not requiring Na+. The differences in glycine transport between human and catfish red cell membranes can be attributed to evolutionary influences.


2009 ◽  
Vol 32 (6) ◽  
pp. 824-831 ◽  
Author(s):  
Jin-Yu LIU ◽  
WU-Ming YANG ◽  
Ai-Hua LI ◽  
Guang-Wen HE

2012 ◽  
Vol 36 (2) ◽  
pp. 314
Author(s):  
Jian-feng LU ◽  
Chang-wei MENG ◽  
Jin LI ◽  
Zi-hui GONG ◽  
Lin LIN ◽  
...  

Author(s):  
Jiko Raut ◽  
Prithidipa Sahoo

Abstract:: Thiol-containing amino acids and peptides play crucial roles in many physiological processses. For example, Cysteine (Cys) and Homocysteine (Hcy) are considered to be related to a number of health disorders such as renal failure, AIDS, Alzheimer’s and Parkinson’s diseases, atherosclerotic cardiovascular diseases, neutral tube defects, and coronary heart disease. Glutathione (GSH), an important tripeptide with a thiol group, performs vital biological functions that are in-volved in combating oxidative stress and maintaining redox homeostasis. Cysteine also plays important roles in our bodies as an antioxidant, a metal cofactor binder in enzymes, and a protein structure stabilizer by disulfide bond formation in the proteins. Hcy are involved in cellular growth and GSH in redox homeostasis. Hence, the rapid, sensitive, and selective de-tection of such biothiols is of considerable importance and significant interest. Different fluorescent chemosensors have been introduced to develop and improve the detection techniques and accuracy of these biothiols. In this review article we have presented some research works to show a guiding principle for the design of effective chemosensors which are highly sensitive and selective for the detection of particular a group of biothiols in aqueous medium. In line with these develop-ments, the researchers have developed novel chemosensors that signal binding events of these above mentioned biothiols through their optical properties. The binding mechanism and properties have also been established with different theoretical studies. Their applications in the form of colorimetric kit, logic gates, live cell imaging, and quantification from different bi-ological samples have also been developed.


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