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
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.