Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues

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Standard

Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues. / Ralston, E; Beushausen, S; Ploug, Thorkil.

I: The Journal of Biological Chemistry, Bind 269, Nr. 22, 03.06.1994, s. 15403-6.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Ralston, E, Beushausen, S & Ploug, T 1994, 'Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues', The Journal of Biological Chemistry, bind 269, nr. 22, s. 15403-6.

APA

Ralston, E., Beushausen, S., & Ploug, T. (1994). Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues. The Journal of Biological Chemistry, 269(22), 15403-6.

Vancouver

Ralston E, Beushausen S, Ploug T. Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues. The Journal of Biological Chemistry. 1994 jun. 3;269(22):15403-6.

Author

Ralston, E ; Beushausen, S ; Ploug, Thorkil. / Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues. I: The Journal of Biological Chemistry. 1994 ; Bind 269, Nr. 22. s. 15403-6.

Bibtex

@article{f58a0bf22bba4c01be1f609ec9192201,
title = "Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues",
abstract = "The VAMPs/synaptobrevins (Vp/Sybs) are small integral membrane proteins. Two isoforms, Vp/Syb 1 and Vp/Syb 2, are considered to be specific to neural tissue. They are associated with synaptic vesicles and are believed to play an important role in neurotransmitter release. A third isoform, cellubrevin, has recently been found in non-neural tissues. We now report that the distribution of Vp/Syb 1 and Vp/Syb 2 is wider than previously thought. RNA transcripts for both Vp/Syb 1 and Vp/Syb 2 were found in rat skeletal muscle and in several other rat non-neural tissues, and antibodies specific for Vp/Syb 2 detected a protein in the endoplasmic reticulum-Golgi area of skeletal muscle. Thus Vp/Sybs 1 and 2 are not restricted to the nervous system but appear to be co-expressed with cellubrevin in many different tissues. This redundancy of Vp/Sybs in a single cell may be required to control the specificity of vesicle-target interaction in the several pathways of intracellular vesicle traffic that are operative within each cell.",
keywords = "Adipose Tissue, Brown, Amino Acid Sequence, Animals, Brain, Endoplasmic Reticulum, Fluorescent Antibody Technique, Gene Expression, Golgi Apparatus, Male, Membrane Proteins, Molecular Sequence Data, Muscles, Nerve Tissue Proteins, Polymerase Chain Reaction, R-SNARE Proteins, Rats, Rats, Wistar, Sequence Homology, Amino Acid, Transcription, Genetic",
author = "E Ralston and S Beushausen and Thorkil Ploug",
year = "1994",
month = jun,
day = "3",
language = "English",
volume = "269",
pages = "15403--6",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "22",

}

RIS

TY - JOUR

T1 - Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues

AU - Ralston, E

AU - Beushausen, S

AU - Ploug, Thorkil

PY - 1994/6/3

Y1 - 1994/6/3

N2 - The VAMPs/synaptobrevins (Vp/Sybs) are small integral membrane proteins. Two isoforms, Vp/Syb 1 and Vp/Syb 2, are considered to be specific to neural tissue. They are associated with synaptic vesicles and are believed to play an important role in neurotransmitter release. A third isoform, cellubrevin, has recently been found in non-neural tissues. We now report that the distribution of Vp/Syb 1 and Vp/Syb 2 is wider than previously thought. RNA transcripts for both Vp/Syb 1 and Vp/Syb 2 were found in rat skeletal muscle and in several other rat non-neural tissues, and antibodies specific for Vp/Syb 2 detected a protein in the endoplasmic reticulum-Golgi area of skeletal muscle. Thus Vp/Sybs 1 and 2 are not restricted to the nervous system but appear to be co-expressed with cellubrevin in many different tissues. This redundancy of Vp/Sybs in a single cell may be required to control the specificity of vesicle-target interaction in the several pathways of intracellular vesicle traffic that are operative within each cell.

AB - The VAMPs/synaptobrevins (Vp/Sybs) are small integral membrane proteins. Two isoforms, Vp/Syb 1 and Vp/Syb 2, are considered to be specific to neural tissue. They are associated with synaptic vesicles and are believed to play an important role in neurotransmitter release. A third isoform, cellubrevin, has recently been found in non-neural tissues. We now report that the distribution of Vp/Syb 1 and Vp/Syb 2 is wider than previously thought. RNA transcripts for both Vp/Syb 1 and Vp/Syb 2 were found in rat skeletal muscle and in several other rat non-neural tissues, and antibodies specific for Vp/Syb 2 detected a protein in the endoplasmic reticulum-Golgi area of skeletal muscle. Thus Vp/Sybs 1 and 2 are not restricted to the nervous system but appear to be co-expressed with cellubrevin in many different tissues. This redundancy of Vp/Sybs in a single cell may be required to control the specificity of vesicle-target interaction in the several pathways of intracellular vesicle traffic that are operative within each cell.

KW - Adipose Tissue, Brown

KW - Amino Acid Sequence

KW - Animals

KW - Brain

KW - Endoplasmic Reticulum

KW - Fluorescent Antibody Technique

KW - Gene Expression

KW - Golgi Apparatus

KW - Male

KW - Membrane Proteins

KW - Molecular Sequence Data

KW - Muscles

KW - Nerve Tissue Proteins

KW - Polymerase Chain Reaction

KW - R-SNARE Proteins

KW - Rats

KW - Rats, Wistar

KW - Sequence Homology, Amino Acid

KW - Transcription, Genetic

M3 - Journal article

C2 - 8195178

VL - 269

SP - 15403

EP - 15406

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 22

ER -

ID: 123666177