THE MAJOR VAULT PROTEIN (MVP100) IS CONTAINED IN CHOLINERGIC NERVE-TERMINALS OF ELECTRIC RAY ELECTRIC ORGAN

Citation
C. Herrmann et al., THE MAJOR VAULT PROTEIN (MVP100) IS CONTAINED IN CHOLINERGIC NERVE-TERMINALS OF ELECTRIC RAY ELECTRIC ORGAN, The Journal of biological chemistry, 271(23), 1996, pp. 13908-13915
Citations number
32
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
271
Issue
23
Year of publication
1996
Pages
13908 - 13915
Database
ISI
SICI code
0021-9258(1996)271:23<13908:TMVP(I>2.0.ZU;2-F
Abstract
A protein of M(r) 100,000 (MVP100) is highly enriched in the electromo tor system of electric rays, Biochemical analysis indicates that MVP10 0 is contained in the cholinergic nerve terminals of Torpedo electric organ as part of a large cytosolic complex. On sucrose density gradien t centrifugation MVP100 comigrates with synaptic vesicles or synaptoso mes. It can be partially separated from synaptic vesicles by gel filtr ation or glycerol velocity gradient centrifugation. Within the complex MVP100 behaves like a hydrophobic protein and is protected against pr oteolytic attack. MVP100 can be immunodetected by are antibody against phosphotyrosine, and it becomes phosphorylated on incubation with [ga mma-P-32]ATP. By screening an electric ray electric lobe cDNA library the primary structure of MVP100 was analyzed MVP100 is highly homologo us to the major vault proteins of slime mold and rat and to the human lung resistance-related protein. Compared with non-neural tissues the expression of MVP100 is highest in brain and enriched in the electric lobe that contains the somata of the electromotor neurons. Immunoelect ron microscopic analysis reveals a close association of MVP100 and syn aptic vesicles in the nerve terminals of the electric organ.