The mechanism of ATP-induced long-term potentiation involves extracellular phosphorylation of membrane proteins in guinea-pig hippocampal CA1 neurons.
The mechanism of ATP-induced long-term potentiation was studied pharmacologically using guinea-pig hippocampal slices. Application of 1-10 microM ATP for 10 min transiently depressed and then slowly augmented the synaptic transmission in CA1 neurons leading to long-term potentiation (LTP). This ATP-induced LTP was blocked by the addition of K-252b, an ecto-protein kinase inhibitor, but was enhanced by the addition of RK682, an ecto-phosphatase inhibitor, both of which do not permeate the cell membrane. These results suggest that ATP applied to the perfusate provides enough substrate for ecto-protein kinase to induce LTP through phosphorylation of extracellular domains of membrane proteins in CA1 neurons.
Fujii
S
S
Department of Physiology, Yamagata University School of Medicine, Japan.
Kato
H
H
Furuse
H
H
Ito
K
K
Osada
H
H
Hamaguchi
T
T
Kuroda
Y
Y
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D002227:Carbazoles / Q000494:pharmacology; D005110:Extracellular Space / Q000378:metabolism*; D006168:Guinea Pigs; D006624:Hippocampus / Q000166:cytology / Q000187:drug effects* / Q000502:physiology*; D066298:In Vitro Techniques; D026121:Indole Alkaloids; D017774:Long-Term Potentiation; D008565:Membrane Proteins / Q000378:metabolism*; D009474:Neurons / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000494:pharmacology; D010766:Phosphorylation; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases
D002227:Carbazoles; D026121:Indole Alkaloids; D008565:Membrane Proteins; D047428:Protein Kinase Inhibitors; C094097:RK 682; D000255:Adenosine Triphosphate; C049985:staurosporine aglycone; D011494:Protein Kinases; C034454:ectoprotein kinase; D010749:Phosphoprotein Phosphatases