The major vault protein (MVP100) is contained in cholinergic nerve terminals of electric ray electric organ

被引:43
作者
Herrmann, C
Volknandt, W
Wittich, B
Kellner, R
Zimmermann, H
机构
[1] UNIV FRANKFURT, INST ZOOL, AK NEUROCHEM, BIOZENTRUM, D-60439 FRANKFURT, GERMANY
[2] EUROPEAN MOLEC BIOL LAB, D-69012 HEIDELBERG, GERMANY
关键词
D O I
10.1074/jbc.271.23.13908
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A protein of M(r) 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 are antibody against phosphotyrosine, and it becomes phosphorylated on incubation with [gamma-P-32]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.
引用
收藏
页码:13908 / 13915
页数:8
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