Abstract
Soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (SNAP) plays an essential role in vesicular transport and the release of neurotransmitters and hormones through associations with NSF and SNAP receptors (SNAREs). Three isoforms (α, β and γ) of SNAP are expressed in mammals. We have generated isoform-specific antibodies and studied the expression and distribution of these SNAP isoforms in the rat nervous system. Each antibody specifically recognized α-, β- or γ-SNAP in an isoform-specific manner in immunoblots of brain homogenate. α- And γ-SNAP were ubiquitously expressed in various tissues, whereas β-SNAP was expressed only in brain. After subcellular fractionation of brain homogenates, all three isoforms were recovered in both soluble and particulate fractions. Immunohistochemistry revealed that α- and β-SNAP were generally differentially distributed both in synaptic and non-synaptic regions, including brain white matter. The presynaptic location of both α- and β-SNAP was confirmed by immunoelectron microscopy. At the neuromuscular junction, immunoreactive α-SNAP was identified in synaptic vesicles, while in the cerebellum, β-SNAP was present in the presynaptic membranes of basket neuron and mossy fiber terminals. From these results we suggest that both α- and β-SNAP may play an important role in neurotransmitter release as well as in constitutive vesicular transport.
| Original language | English |
|---|---|
| Pages (from-to) | 363-371 |
| Number of pages | 9 |
| Journal | Neuroscience |
| Volume | 107 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 23 2001 |
| Externally published | Yes |
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Keywords
- Exocytosis
- Neurotransmitter release
- NSF
- SNARE
- Synaptic transmission
ASJC Scopus subject areas
- Neuroscience(all)
Cite this
Distribution of soluble N-ethylmaleimide fusion protein attachment proteins (SNAPS) in the rat nervous system. / Nishiki, Tei-ichi; Nihonmatsu, I.; Tsuhara, Y.; Kawasaki, M.; Sekiguchi, M.; Sato, K.; Mizoguchi, A.; Takahashi, M.
In: Neuroscience, Vol. 107, No. 3, 23.11.2001, p. 363-371.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Distribution of soluble N-ethylmaleimide fusion protein attachment proteins (SNAPS) in the rat nervous system
AU - Nishiki, Tei-ichi
AU - Nihonmatsu, I.
AU - Tsuhara, Y.
AU - Kawasaki, M.
AU - Sekiguchi, M.
AU - Sato, K.
AU - Mizoguchi, A.
AU - Takahashi, M.
PY - 2001/11/23
Y1 - 2001/11/23
N2 - Soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (SNAP) plays an essential role in vesicular transport and the release of neurotransmitters and hormones through associations with NSF and SNAP receptors (SNAREs). Three isoforms (α, β and γ) of SNAP are expressed in mammals. We have generated isoform-specific antibodies and studied the expression and distribution of these SNAP isoforms in the rat nervous system. Each antibody specifically recognized α-, β- or γ-SNAP in an isoform-specific manner in immunoblots of brain homogenate. α- And γ-SNAP were ubiquitously expressed in various tissues, whereas β-SNAP was expressed only in brain. After subcellular fractionation of brain homogenates, all three isoforms were recovered in both soluble and particulate fractions. Immunohistochemistry revealed that α- and β-SNAP were generally differentially distributed both in synaptic and non-synaptic regions, including brain white matter. The presynaptic location of both α- and β-SNAP was confirmed by immunoelectron microscopy. At the neuromuscular junction, immunoreactive α-SNAP was identified in synaptic vesicles, while in the cerebellum, β-SNAP was present in the presynaptic membranes of basket neuron and mossy fiber terminals. From these results we suggest that both α- and β-SNAP may play an important role in neurotransmitter release as well as in constitutive vesicular transport.
AB - Soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (SNAP) plays an essential role in vesicular transport and the release of neurotransmitters and hormones through associations with NSF and SNAP receptors (SNAREs). Three isoforms (α, β and γ) of SNAP are expressed in mammals. We have generated isoform-specific antibodies and studied the expression and distribution of these SNAP isoforms in the rat nervous system. Each antibody specifically recognized α-, β- or γ-SNAP in an isoform-specific manner in immunoblots of brain homogenate. α- And γ-SNAP were ubiquitously expressed in various tissues, whereas β-SNAP was expressed only in brain. After subcellular fractionation of brain homogenates, all three isoforms were recovered in both soluble and particulate fractions. Immunohistochemistry revealed that α- and β-SNAP were generally differentially distributed both in synaptic and non-synaptic regions, including brain white matter. The presynaptic location of both α- and β-SNAP was confirmed by immunoelectron microscopy. At the neuromuscular junction, immunoreactive α-SNAP was identified in synaptic vesicles, while in the cerebellum, β-SNAP was present in the presynaptic membranes of basket neuron and mossy fiber terminals. From these results we suggest that both α- and β-SNAP may play an important role in neurotransmitter release as well as in constitutive vesicular transport.
KW - Exocytosis
KW - Neurotransmitter release
KW - NSF
KW - SNARE
KW - Synaptic transmission
UR - http://www.scopus.com/inward/record.url?scp=0035940839&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035940839&partnerID=8YFLogxK
U2 - 10.1016/S0306-4522(01)00370-0
DO - 10.1016/S0306-4522(01)00370-0
M3 - Article
C2 - 11718992
AN - SCOPUS:0035940839
VL - 107
SP - 363
EP - 371
JO - Neuroscience
JF - Neuroscience
SN - 0306-4522
IS - 3
ER -