NDLI: Extracellular Interconversion of Nucleotides Reveals an Ecto-Adenylate Kinase Activity in the Rat Hippocampus

Content Provider	Springer Nature Link
Author	Sperlágh, Beáta Vizi, E. Sylvester
Copyright Year	2007
Abstract	Here, the extracellular interconversion of nucleotides and nucleosides was investigated in rat hippocampal slices and synaptosomes by an HPLC-UV technique. Adenosine 5′-triphosphate (ATP) was converted to adenosine 5′-diphosphate (ADP), adenosine 5′-monophosphate (AMP), adenosine, inosine, and hypoxanthine in the slices, whereas ADP elicited parallel and concentration-dependent formation of ATP and AMP. The specific adenylate kinase inhibitor diadenosine pentaphosphate decreased the rate of decomposition of ADP and inhibited the formation of ATP. No substantial changes in the interconversion of ADP to ATP and AMP were found in the presence of dipyridamole, flufenamic acid, the P2 receptor antagonist pyridoxal-5-phosphate-6-azophenyl-2′,4′-disulphonic acid tetrasodium (PPADS), and the alkaline phosphatase substrate para-nitrophenylphosphate. Negligible levels of nucleotides were generated when uridine 5′-diphosphate (UDP), AMP or adenosine were used as substrates. Ecto-adenylate kinase activity was also observed in purified synaptosomes. In summary, we demonstrate the presence of an ecto-adenylate kinase activity in the hippocampus, which is a previously unrecognized pathway that influences the availability of purines in the central nervous system.
Starting Page	1978
Ending Page	1989
Page Count	12
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	32
Issue Number	11
e-ISSN	15736903
Language	English
Publisher	Springer US
Publisher Date	2007-08-25
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	ADP ATP Hippocampus Ecto-adenylate kinase Diadenosine pentaphosphate NTPDase Neurology Biochemistry Neurosciences
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

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