Biochemical evidence for the presence of NAP-22, a novel acidic calmodulin binding protein, in the synaptic vesicles of rat brain.
NAP-22 is a neuronal tissue-enriched acidic protein which is expressed predominantly in rat brain. In the present study, we quantitated the amount of NAP-22 in a highly purified synaptic vesicle fraction. NAP-22 comprised 1.3 +/- 0.15% of the total protein in the fraction, and NAP-22 was located on the external surface of the synaptic vesicle membrane. The results suggest NAP-22 may be involved in the synaptic vesicle cycling.
Yamamoto
Y
Y
Graduate School, Division of Applied Biology, Kyoto Institute of Technology, Japan.
Sokawa
Y
Y
Maekawa
S
S
D000818:Animals; D001923:Brain Chemistry / Q000502:physiology*; D002148:Calmodulin-Binding Proteins / Q000032:analysis* / Q000302:isolation & purification; D015816:Cell Adhesion Molecules, Neuronal / Q000032:analysis; D003598:Cytoskeletal Proteins; D009419:Nerve Tissue Proteins / Q000032:analysis* / Q000302:isolation & purification; D011233:Precipitin Tests; D017729:Presynaptic Terminals / Q000737:chemistry / Q000201:enzymology; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D013572:Synaptic Vesicles / Q000737:chemistry* / Q000201:enzymology; D016708:Synaptophysin / Q000032:analysis
D002148:Calmodulin-Binding Proteins; D015816:Cell Adhesion Molecules, Neuronal; D003598:Cytoskeletal Proteins; D009419:Nerve Tissue Proteins; D016708:Synaptophysin; C066853:Basp1 protein, rat; D000254:Sodium-Potassium-Exchanging ATPase