Localization of the Cl(-)-ATPase activity on NAP-22 enriched membrane microdomain (raft) of rat brain.
Much attention has been paid to the membrane microdomain enriched in cholesterol and sphingolipids called raft. In the central nervous system, however, the physiological role of this domain is not so evident at present, partly because of the complexity of the protein components in the raft fraction. In this study we surveyed ATPase activities in the raft fraction obtained from the synaptic plasma membrane of rat brain and found the enrichment of an ethacrynic acid-sensitive ATPase (Cl(-)-pump) activity. Immunoprecipitation experiments using antibodies to raft-localized proteins showed the co-precipitation of the ATPase activity with NAP-22, a major raft-localized protein. This result suggests the participation of the raft in the regulation of ion transport in addition to the presence of heterogeneity of raft domains in neurons.
Maekawa
Shohei
S
Division of Bioinformation, Department of Biosystems Science, Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan. smaekawa@kobe-u.ac.jp
Taguchi
Katsutoshi
K
D000251:Adenosine Triphosphatases / Q000032:analysis / Q000378:metabolism*; D000818:Animals; D027321:Anion Transport Proteins; D001921:Brain / Q000201:enzymology* / Q000378:metabolism; D021962:Membrane Microdomains / Q000201:enzymology* / Q000378:metabolism; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D012097:Repressor Proteins / Q000378:metabolism*; D013570:Synaptic Membranes / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism
D027321:Anion Transport Proteins; C104089:BASP1 protein, human; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D012097:Repressor Proteins; D000251:Adenosine Triphosphatases; C031652:anion-sensitive ATPases