Differential localization of SNARE complex proteins SNAP-25, syntaxin, and VAMP during development of the mammalian retina

SNARE complex proteins have critical functions during regulated vesicular release of neurotransmitter. In addition, they play critical roles during neurite outgrowth and synaptogenesis. Although it is clear that the function of any one SNARE complex protein during release of neurotransmitter is depe...

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Veröffentlicht in:Journal of comparative neurology (1911) 2001-02, Vol.430 (3), p.306-320
Hauptverfasser: Greenlee, M. Heather West, Roosevelt, Corey B., Sakaguchi, Donald S.
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Roosevelt, Corey B.
Sakaguchi, Donald S.
description SNARE complex proteins have critical functions during regulated vesicular release of neurotransmitter. In addition, they play critical roles during neurite outgrowth and synaptogenesis. Although it is clear that the function of any one SNARE complex protein during release of neurotransmitter is dependent on its association with other members of the complex, it is less certain whether their function during development and differentiation is dependent on interaction with one another. Previously, we have observed transient high levels of SNARE complex protein SNAP‐25 in developing cholinergic amacrine cells (West Greenlee et al. [1998] J Comp Neurol 394:374–385). In addition, we detected, high levels of SNAP‐25 in developing and mature photoreceptors. To better understand the functional significance of these high levels of SNAP‐25 expression, we used immunocytochemistry to examine the developmental expression of the three members of the SNARE complex, SNAP‐25, Syntaxin, and vesicle associated membrane protein (VAMP/also Synaptobrevin). Our results demonstrate that the high levels of SNAP‐25 in cholinergic amacrine cells and photoreceptors are not accompanied by the same relatively high levels of other SNARE complex proteins. These results suggest that high levels of SNAP‐25 in specific cell types may function independently of association with Syntaxin and VAMP. In this analysis, we characterized the changing patterns of immunoreactivity for the three SNARE complex proteins during the development and differentiation of the mammalian retina. We have compared the pattern of expression of the core SNARE complex proteins in the Brazilian opossum, Monodelphis domestica, and in the rat and found common patterns of expression between these diverse mammalian species. We observed temporal differences in the onset of immunoreactivity between these three proteins, and differences in their localization within synaptic layers in the developing and mature mammalian retina. This study is the first to characterize the changing expression patterns of the three SNARE complex proteins in the developing central nervous system. The differential distribution of SNAP‐25, Syntaxin, and VAMP may indicate additional roles for these proteins during vesicle trafficking events, which are independent of their association with one another. J. Comp. Neurol. 430:306–320, 2001. © 2001 Wiley‐Liss, Inc.
doi_str_mv 10.1002/1096-9861(20010212)430:3<306::AID-CNE1032>3.0.CO;2-B
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Heather West</creatorcontrib><creatorcontrib>Roosevelt, Corey B.</creatorcontrib><creatorcontrib>Sakaguchi, Donald S.</creatorcontrib><title>Differential localization of SNARE complex proteins SNAP-25, syntaxin, and VAMP during development of the mammalian retina</title><title>Journal of comparative neurology (1911)</title><addtitle>J. Comp. Neurol</addtitle><description>SNARE complex proteins have critical functions during regulated vesicular release of neurotransmitter. In addition, they play critical roles during neurite outgrowth and synaptogenesis. Although it is clear that the function of any one SNARE complex protein during release of neurotransmitter is dependent on its association with other members of the complex, it is less certain whether their function during development and differentiation is dependent on interaction with one another. Previously, we have observed transient high levels of SNARE complex protein SNAP‐25 in developing cholinergic amacrine cells (West Greenlee et al. [1998] J Comp Neurol 394:374–385). In addition, we detected, high levels of SNAP‐25 in developing and mature photoreceptors. To better understand the functional significance of these high levels of SNAP‐25 expression, we used immunocytochemistry to examine the developmental expression of the three members of the SNARE complex, SNAP‐25, Syntaxin, and vesicle associated membrane protein (VAMP/also Synaptobrevin). Our results demonstrate that the high levels of SNAP‐25 in cholinergic amacrine cells and photoreceptors are not accompanied by the same relatively high levels of other SNARE complex proteins. These results suggest that high levels of SNAP‐25 in specific cell types may function independently of association with Syntaxin and VAMP. In this analysis, we characterized the changing patterns of immunoreactivity for the three SNARE complex proteins during the development and differentiation of the mammalian retina. We have compared the pattern of expression of the core SNARE complex proteins in the Brazilian opossum, Monodelphis domestica, and in the rat and found common patterns of expression between these diverse mammalian species. We observed temporal differences in the onset of immunoreactivity between these three proteins, and differences in their localization within synaptic layers in the developing and mature mammalian retina. This study is the first to characterize the changing expression patterns of the three SNARE complex proteins in the developing central nervous system. The differential distribution of SNAP‐25, Syntaxin, and VAMP may indicate additional roles for these proteins during vesicle trafficking events, which are independent of their association with one another. J. Comp. 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Heather West</au><au>Roosevelt, Corey B.</au><au>Sakaguchi, Donald S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential localization of SNARE complex proteins SNAP-25, syntaxin, and VAMP during development of the mammalian retina</atitle><jtitle>Journal of comparative neurology (1911)</jtitle><addtitle>J. Comp. Neurol</addtitle><date>2001-02-12</date><risdate>2001</risdate><volume>430</volume><issue>3</issue><spage>306</spage><epage>320</epage><pages>306-320</pages><issn>0021-9967</issn><eissn>1096-9861</eissn><abstract>SNARE complex proteins have critical functions during regulated vesicular release of neurotransmitter. In addition, they play critical roles during neurite outgrowth and synaptogenesis. Although it is clear that the function of any one SNARE complex protein during release of neurotransmitter is dependent on its association with other members of the complex, it is less certain whether their function during development and differentiation is dependent on interaction with one another. Previously, we have observed transient high levels of SNARE complex protein SNAP‐25 in developing cholinergic amacrine cells (West Greenlee et al. [1998] J Comp Neurol 394:374–385). In addition, we detected, high levels of SNAP‐25 in developing and mature photoreceptors. To better understand the functional significance of these high levels of SNAP‐25 expression, we used immunocytochemistry to examine the developmental expression of the three members of the SNARE complex, SNAP‐25, Syntaxin, and vesicle associated membrane protein (VAMP/also Synaptobrevin). Our results demonstrate that the high levels of SNAP‐25 in cholinergic amacrine cells and photoreceptors are not accompanied by the same relatively high levels of other SNARE complex proteins. These results suggest that high levels of SNAP‐25 in specific cell types may function independently of association with Syntaxin and VAMP. In this analysis, we characterized the changing patterns of immunoreactivity for the three SNARE complex proteins during the development and differentiation of the mammalian retina. We have compared the pattern of expression of the core SNARE complex proteins in the Brazilian opossum, Monodelphis domestica, and in the rat and found common patterns of expression between these diverse mammalian species. We observed temporal differences in the onset of immunoreactivity between these three proteins, and differences in their localization within synaptic layers in the developing and mature mammalian retina. This study is the first to characterize the changing expression patterns of the three SNARE complex proteins in the developing central nervous system. The differential distribution of SNAP‐25, Syntaxin, and VAMP may indicate additional roles for these proteins during vesicle trafficking events, which are independent of their association with one another. J. Comp. Neurol. 430:306–320, 2001. © 2001 Wiley‐Liss, Inc.</abstract><cop>New York</cop><pub>John Wiley &amp; Sons, Inc</pub><pmid>11169469</pmid><doi>10.1002/1096-9861(20010212)430:3&lt;306::AID-CNE1032&gt;3.0.CO;2-B</doi><tpages>15</tpages></addata></record>
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subjects Acetylcholine - metabolism
Animals
Animals, Newborn
ChAT
Choline O-Acetyltransferase - analysis
Female
Membrane Proteins - analysis
Monodelphis domestica
Nerve Tissue Proteins - analysis
Opossums - anatomy & histology
Opossums - metabolism
photoreceptor
Photoreceptor Cells - cytology
Photoreceptor Cells - metabolism
Pregnancy
Qa-SNARE Proteins
R-SNARE Proteins
Rats
Rats, Sprague-Dawley - anatomy & histology
Rats, Sprague-Dawley - metabolism
Retina - cytology
Retina - growth & development
Retina - metabolism
SNARE complex
SNARE Proteins
starburst amacrine cell
Synapses - metabolism
Synapses - ultrastructure
Synaptic Transmission - physiology
Synaptobrevin
Synaptosomal-Associated Protein 25
VAMP protein
Vesicular Transport Proteins
title Differential localization of SNARE complex proteins SNAP-25, syntaxin, and VAMP during development of the mammalian retina
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