Excitatory amino acids and synaptic transmission: the evidence for a physiological function

1990 ◽  
Vol 11 (5) ◽  
pp. 205-211 ◽  
Author(s):  
P.Max Headley ◽  
Sten Grillner
2011 ◽  
Vol 2011 ◽  
pp. 1-6
Author(s):  
Ramón A. Lorca ◽  
Lorena Varela-Nallar ◽  
Nibaldo C. Inestrosa ◽  
J. Pablo Huidobro-Toro

Although the physiological function of the cellular prion protein (PrPC) remains unknown, several evidences support the notion of its role in copper homeostasis. PrPCbinds Cu2+through a domain composed by four to five repeats of eight amino acids. Previously, we have shown that the perfusion of this domain prevents and reverses the inhibition by Cu2+of the adenosine triphosphate (ATP)-evoked currents in the P2X4receptor subtype, highlighting a modulatory role for PrPCin synaptic transmission through regulation of Cu2+levels. Here, we study the effect of full-length PrPCin Cu2+inhibition of P2X4receptor when both are coexpressed. PrPCexpression does not significantly change the ATP concentration-response curve in oocytes expressing P2X4receptors. However, the presence of PrPCreduces the inhibition by Cu2+of the ATP-elicited currents in these oocytes, confirming our previous observations with the Cu2+binding domain. Thus, our observations suggest a role for PrPCin modulating synaptic activity through binding of extracellular Cu2+.


1989 ◽  
Vol 93 (1) ◽  
pp. 195-201 ◽  
Author(s):  
J.D.C Lambert ◽  
R.S.G Jones ◽  
M Andreasen ◽  
M.S Jensen ◽  
U Heinemann

1999 ◽  
Vol 11 (4) ◽  
pp. 1324-1334 ◽  
Author(s):  
Thomas Launey ◽  
Anton Ivanov ◽  
Gàbor Kapus ◽  
Nadine Ferrand ◽  
Istvan Tarnawa ◽  
...  

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