Exocytosis from Neuronal Large Dense-Cored Vesicles

Thureson‐Klein, Åsa; Klein, Richard L.

doi:10.1016/s0074-7696(08)60659-2

Cited by 187 publications

(85 citation statements)

References 355 publications

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“…In junctions with LE-labeled as well as unlabeled terminals, the gold-silver particles for MOR usually were not located along synaptic junctions. Taken together, these results indicate that MOR in the NAC may be activated at a distance from the sites of exocytotic release of LE or other endogenous opioid peptides, as has been suggested in the peripheral nervous system (Jan and Jan, 1983;Kravitz et al, 1983) and from studies of peptide exocytosis (Thureson-Klein and Klein, 1990). Additionally, our data provide anatomical evidence that postsynaptic activation of MOR in the NAC may occur via stimulation by local endogenous opioids.…”

Section: Mor-labeling Is Localized To Nonsynaptic Sites On Dendrites supporting

confidence: 82%

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu⁵-Enkephalin

et al. 1996

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-Opioid receptors and their endogenous ligands, including Leu 5 -enkephalin (LE), are distributed abundantly in the nucleus accumbens (NAC), a region implicated in mechanisms of opiate reinforcement. We used immunoperoxidase and/or immunogoldsilver methods to define ultrastructural sites for functions ascribed to -opioid receptors and potential sites for activation by LE in the NAC. An antipeptide antibody raised against an 18 amino acid sequence of the cloned -opioid receptor (MOR) C terminus showed that MOR-like immunoreactivity (MOR-LI) was localized predominantly to extrasynaptic sites along neuronal plasma membranes. The majority of neuronal profiles containing MOR-LI were dendrites and dendritic spines. The dendritic plasma membranes immunolabeled for MOR were near sites of synaptic input from LE-labeled terminals and other unlabeled terminals forming either inhibitory or excitatory type synapses. Unmyelinated axons and axon terminals were also intensely but less frequently immunoreactive for MOR. Observed sites for potential axonal associations with LE included coexistence of MOR and LE within the same terminal, as well as close appositions between differentially labeled axons. Astrocytic processes rarely contained detectable MOR-LI, but also were sometimes observed in apposition to LE-labeled terminals. We conclude that in the rat NAC, MOR is localized prominently to extrasynaptic neuronal and more rarely to glial plasma membranes that are readily accessible to released LE and possibly other opioid peptides and opiate drugs. The close affiliation of MOR with spines receiving excitatory synapses and dendrites receiving inhibitory synapses provides the first direct morphological evidence that MOR selectively modulates postsynaptic responses to cortical and other afferents.

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Section: Mor-labeling Is Localized To Nonsynaptic Sites On Dendrites supporting

confidence: 82%

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu⁵-Enkephalin

et al. 1996

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“…After 1986, the ultrastructural analysis in several studies strengthened the evidence that large dense core vesicles rich in neuropeptides were preferentially associated with nonsynaptic membranes (Matteoli et al, 1988;Sossin et al, 1989;Thureson-Klein and Klein, 1990;Barinaga, 1993;see Koob et al, 1990). Thus, the release of peptides commonly occurs extrasynaptically (Golding, 1994).…”

Section: Release Of Transmitters Not In Strict Contiguity With Postsymentioning

confidence: 90%

From the Golgi–Cajal mapping to the transmitter-based characterization of the neuronal networks leading to two modes of brain communication: Wiring and volume transmission

Fuxé¹,

Dahlström²,

Höistad³

et al. 2007

Brain Research Reviews

234

219

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After Golgi-Cajal mapped neural circuits, the discovery and mapping of the central monoamine neurons opened up for a new understanding of interneuronal communication by indicating that another form of communication exists. For instance, it was found that dopamine may be released as a prolactin inhibitory factor from the median eminence, indicating an alternative mode of dopamine communication in the brain. Subsequently, the analysis of the locus coeruleus noradrenaline neurons demonstrated a novel type of lower brainstem neuron that monosynaptically and globally innervated the entire CNS.Furthermore, the ascending raphe serotonin neuron systems were found to globally innervate the forebrain with few synapses, and where deficits in serotonergic function appeared to play a major role in depression. We propose that serotonin reuptake This will lead to the unified execution of information handling and trophism for optimal brain function and survival.

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“…During neurite outgrowth, membrane fusion for plasmalemma expansion at the growth cone (10), as well as possibly throughout the extending neurite (39), appears generally targeted to the plasma membrane. Similarly, the regulated secretion of neuromodulatory peptides from secretory granules in neuroendocrine cells and from large dense cored vesicles of axon terminals of neurons also appears diffusely located along the plasma membrane (2,40). This contrasts markedly with the organized, tight clustering of more highly abundant synaptic vesicles at the active zone of presynaptic terminals of most neurons.…”

Section: Discussionmentioning

confidence: 99%

Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development.

Bark

Hahn

Ryabinin

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

218

230

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The presynaptic plasma membrane protein SNAP-25 (synaptosome-associated protein of 25 kDa) has been implicated as one of several neural-specific components that direct constitutive fusion mechanisms to the regulated vesicle trafficking and exocytosis of neurotransmitter release.There exist two alternatively spliced isoforms of a and b, which differ in a putative membrane-interacting domain. We show that these two isoforms have distinct quantitative and anatomical patterns of expression during brain development, in neurons, and in neuroendocrine cells and that the proteins localize differently in neurites of transfected PC12 pheochromocytoma cells. These findings indicate that alternative isoforms of SNAP-25 may play distinct roles in vesicular fusion events required for membrane addition during axonal outgrowth and for release of neuromodulatory peptides and neurotransmitters.In the nervous system, the regulated release of neurotransmitters and neuromodulatory peptides and the addition of proteins and other constituents required for neurite outgrowth proceed through intracellular trafficking and fusion of vesicles at the plasma membrane (for review, see refs. 1-4). This regulated fusion of donor vesicle and acceptor (target) membranes is likely mediated by the same ubiquitious ATPdependent machinery, composed of soluble N-ethylmaleimide-sensitive factor (NSF) and NSF-associated proteins (SNAPs), that is utilized in constitutive pathways of all eukaryotic cells (5). To provide specificity for the fusion process, distinct sets of related proteins have been postulated to serve as membrane receptors, or SNAREs (6). These enable correct recognition between vesicle and target membranes at different intracellular compartments, and they engage the general fusion machinery. It is likely that specific SNAREs, together with additional cell-specific auxiliary proteins, are critical for the specialized sorting, targeting, and final recycling of vesicles which are required for the Ca2+-triggered release of neurotransmitter and modulatory peptides unique to neurons and neuroendocrine cells (7-9). Although evidence suggests that membrane addition to the expanding plasmalemma of axonal growth cones is Ca2+ dependent (10), it is thought that there are independent vesicle-targeting and fusion mechanisms that chiefly support either axon outgrowth or neurotransmitter release. Recent studies do suggest, however, that at least one of the SNAREs, SNAP-25, is a key player in membrane fusion events of both developing and mature neurons.The presynaptic nerve terminal protein SNAP-25 (synaptosome-associated protein of 25 kDa; ref. 11) has been identified as a plasma membrane protein that together with syntaxin and the synaptic vesicle proteins VAMP/synaptobrevin and synaptotagmin are thought to constitute an initial SNARE docking complex for regulated exocytosis (5, 12, 13). After docking, this complex can incorporate into a 20S fusion parThe publication costs of this article were defrayed in part by page charge payment. This a...

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Exocytosis from Neuronal Large Dense-Cored Vesicles

Cited by 187 publications

References 355 publications

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu⁵-Enkephalin

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu⁵-Enkephalin

From the Golgi–Cajal mapping to the transmitter-based characterization of the neuronal networks leading to two modes of brain communication: Wiring and volume transmission

Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development.

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Exocytosis from Neuronal Large Dense-Cored Vesicles

Cited by 187 publications

References 355 publications

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu5-Enkephalin

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu5-Enkephalin

From the Golgi–Cajal mapping to the transmitter-based characterization of the neuronal networks leading to two modes of brain communication: Wiring and volume transmission

Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development.

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Product

Resources

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Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu⁵-Enkephalin

Ultrastructural Immunocytochemical Localization of μ-Opioid Receptors in Rat Nucleus Accumbens: Extrasynaptic Plasmalemmal Distribution and Association with Leu⁵-Enkephalin