Document Detail

Biochemistry and molecular biology of the vesicular monoamine transporter from chromaffin granules.
MedLine Citation:
PMID:  7823026     Owner:  NLM     Status:  MEDLINE    
Prior to secretion, monoamines (catecholamines, serotonin, histamine) are concentrated from the cytoplasm into vesicles by vesicular monoamine transporters (VMAT). These transporters also carry non-physiological compounds, e.g. the neurotoxin methyl-4-phenylpyridinium. VMAT acts as an electrogenic antiporter (exchanger) of protons and monoamines, using a proton electrochemical gradient. Vesicular transport is inhibited by specific ligands, including tetrabenazine, ketanserin and reserpine. The mechanism of transport and the biochemistry of VMAT have been analyzed with the help of these tools, using mainly the chromaffin granules from bovine adrenal glands as a source of transporter. Although biochemical studies did not suggest a multiplicity of VMATs, two homologous but distinct VMAT genes have recently been cloned from rat, bovine and human adrenal glands. The VMAT proteins are predicted to possess 12 transmembrane segments, with both extremities lying on the cytoplasmic side. They possess N-glycosylation sites in a putative luminal loop and phosphorylation sites in cytoplasmic domains. In rat, VMAT1 is expressed in the adrenal gland whereas VMAT2 is expressed in the brain. In contrast, we found that the bovine adrenal gland expressed both VMAT1 and VMAT2. VMAT2 corresponds to the major transporter of chromaffin granules, as shown by partial peptidic sequences of the purified protein and by a pharmacological analysis of the transport obtained in transfected COS cells (COS cells are monkey kidney cells possessing the ability to replicate SV-40-origin-containing plasmids). We discuss the possibility that VMAT1 may be specifically addressed to large secretory granules vesicles, whereas VMAT2 may also be addressed to small synaptic vesicles; species differences would then reflect the distinct physiological roles of the small synaptic vesicles in the adrenal gland.
J P Henry; D Botton; C Sagne; M F Isambert; C Desnos; V Blanchard; R Raisman-Vozari; E Krejci; J Massoulie; B Gasnier
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  The Journal of experimental biology     Volume:  196     ISSN:  0022-0949     ISO Abbreviation:  J. Exp. Biol.     Publication Date:  1994 Nov 
Date Detail:
Created Date:  1995-02-16     Completed Date:  1995-02-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0243705     Medline TA:  J Exp Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  251-62     Citation Subset:  IM    
CNRS URA 1112, Neurobiologie Physico-Chimique, Institut de Biologie Physico-Chimique, Paris, France.
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MeSH Terms
Adrenal Medulla / metabolism*
Biological Transport
Cell Line
Cercopithecus aethiops
Chromaffin Granules / metabolism*
Gene Expression
Glycoproteins / biosynthesis,  genetics*,  metabolism*
Membrane Glycoproteins*
Membrane Transport Proteins*
Models, Biological
Neurons / metabolism
Neurotransmitter Agents / metabolism*
Vesicular Biogenic Amine Transport Proteins
Vesicular Monoamine Transport Proteins
Reg. No./Substance:
0/Glycoproteins; 0/Membrane Glycoproteins; 0/Membrane Transport Proteins; 0/Neuropeptides; 0/Neurotransmitter Agents; 0/SLC18A1 protein, human; 0/SLC18A2 protein, human; 0/Slc18a1 protein, rat; 0/Slc18a2 protein, rat; 0/Vesicular Biogenic Amine Transport Proteins; 0/Vesicular Monoamine Transport Proteins

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