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(Received for publication, October 17, 1995, and in revised form, March 12, 1996)
From the A protein of Mr 100,000 (MVP100) is highly enriched in the electromotor system of electric
rays. Biochemical analysis indicates that MVP100 is contained in the
cholinergic nerve terminals of Torpedo electric organ as
part of a large cytosolic complex. On sucrose density gradient
centrifugation MVP100 comigrates with synaptic vesicles or
synaptosomes. It can be partially separated from synaptic vesicles by
gel filtration or glycerol velocity gradient centrifugation. Within the
complex MVP100 behaves like a hydrophobic protein and is protected
against proteolytic attack. MVP100 can be immunodetected by an antibody
against phosphotyrosine, and it becomes phosphorylated on incubation
with [
Volume 271, Number 23,
Issue of June 7, 1996
pp. 13908-13915
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
AK Neurochemie, Biozentrum, Zoologisches
Institut der Universität Frankfurt, D-60439 Frankfurt am Main,
Germany, and the ¶ European Molecular Biology Laboratory, Postfach
10-2209, Meyerhofstrasse 1, D-69012 Heidelberg, Germany
-32P]ATP. By screening an electric ray electric
lobe cDNA library the primary structure of MVP100 was analyzed.
MVP100 is highly homologous 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. Immunoelectron microscopic analysis reveals a
close association of MVP100 and synaptic vesicles in the nerve
terminals of the electric organ.
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