Identification of a heparan sulphate-containing proteoglycan as a specific core component of cholinergic synaptic vesicles from Torpedo marmorata.

Stadler, H.; Dowe, G. H. C.

doi:10.1002/j.1460-2075.1982.tb01326.x

Cited by 83 publications

(44 citation statements)

References 24 publications

(24 reference statements)

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“…Evidently the proteoglycan epitope recognized by our antiserum is unchanged by the arrival of the synaptic vesicle at the terminal and its maturation into a fully charged vesicle. This is in contrast to the results reported by Kiene and Stadler (1987) and Stadler and Kiene (1987), using a different serum, but would not preclude the loss, on maturation, of a (to our sera) nonimmunoreactive portion of the vesicular proteoglycan, such as part of its glucosaminoglycan, which is known to be readily detached by dialysis-induced hypoosmotic shock (Stadler and Dowe, 1982). By contrast, the axonal vesicles have a lower Mg2+-dependent ATPase, a lower density, and a much lower acetylcholine content than terminal vesicles.…”

Section: Implications Of Results For the Axonal Transport Of Storage contrasting

confidence: 92%

Isolation and Characterization of Secretory Granules Storing a Vasoactive Intestinal Polypeptide‐Like Peptide in Torpedo Cholinergic Electromotor Neurones

Ägoston

Dowe

Whittaker

1989

Journal of Neurochemistry

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Previous immunocytochemical work showed that the cholinergic electromotor neurones of Torpedo marmorata contain a vasoactive intestinal polypeptide-like immunoreactivity (VIPLI) that is conveyed to the terminals by axonal transport from the cell bodies where it is presumably synthesized. In extension of this work, we have now succeeded in isolating the VIPLI storage granules from both the terminals and the axons of these neurones and characterizing them morphologically and biochemically. They were readily separated from synaptic vesicles but contained several components in common that had previously been regarded as specific for synaptic vesicles. Among these were a heparan sulphate type of proteoglycan, synaptophysin, and a Mg2+-dependent ATPase. The VIPLI concentration in lobe tissue and the amount of tissue available were both insufficient to permit the isolation of granules from the electromotor cell bodies by the same technique but it was possible to establish the presence of such granules by particle-exclusion chromatography, using the stable markers mentioned above. In contrast to the VIPLI-containing granules, axonal synaptic vesicles differed from their terminal counterparts in having a very low acetylcholine content relative to stable vesicle markers: they presumably fill up on reaching the terminal where they are exposed to higher concentrations of cytoplasmic acetylcholine.

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Section: Implications Of Results For the Axonal Transport Of Storage contrasting

confidence: 92%

Isolation and Characterization of Secretory Granules Storing a Vasoactive Intestinal Polypeptide‐Like Peptide in Torpedo Cholinergic Electromotor Neurones

Ägoston

Dowe

Whittaker

1989

Journal of Neurochemistry

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“…We found previously that the chains of SV2H are incompletely digested by keratanase I, or keratanase II, or endo-␤-galactosidase, or all three enzymes (2). 3 Presumably some modification of the keratan sulfate chains makes them partially resistant to these enzymes.…”

Section: Discussionmentioning

confidence: 99%

The Synaptic Vesicle Protein SV2 Is Complexed with an α5-Containing Laminin on the Nerve Terminal Surface

Son¹,

Scranton²,

Sunderland³

et al. 2000

Journal of Biological Chemistry

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Interactions between growing axons and synaptic basal lamina components direct the formation of neuromuscular junctions during nerve regeneration. Isoforms of laminin containing ␣5 or ␤2 chains are potential basal lamina ligands for these interactions. The nerve terminal receptors are unknown. Here we show that SV2, a synaptic vesicle transmembrane proteoglycan, is complexed with a 900-kDa laminin on synaptosomes from the electric organ synapse that is similar to the neuromuscular junctions. Although two laminins are present on synaptosomes, only the 900-kDa laminin is associated with SV2. Other nerve terminal components are absent from this complex. The 900-kDa laminin contains an ␣5, a ␤1, and a novel ␥ chain. To test whether SV2 directly binds the 900-kDa laminin, we looked for interaction between purified SV2 and laminin-1, a laminin isoform with a similar structure. We find SV2 binds with high affinity to purified laminin-1. Our results suggest that a synaptic vesicle component may act as a laminin receptor on the presynaptic plasma membrane; they also suggest a mechanism for activity-dependent adhesion at the synapse.

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“…Biochemical and molecular genetic approaches using the electric organs of electric rays as a model system lead to the identification of numerous proteins of cholinergic synaptic vesicles. These include VAMP (synaptobrevin) [ 11, svp25 [2], synaptophysin [3], p65 (synaptotagmin) [3], synapsin [4], SV2 [5], proteoglycan [6] and the proton pumping vacuolar ATPase [7]. Many of these proteins are shared with synaptic vesicles derived from mammalian brain.…”

Section: Introductionmentioning

confidence: 99%

Association of three small GTP‐binding proteins with cholinergic synaptic vesicles

et al. 1993

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Several small (low molecular weight) GTP-binding proteins are associated with cholinergic synaptic vesicles derived from the electric organ of electric ray. Using GTP overlay techniques and direct micro sequencing we analyzed the association of small GTP-binding proteins with synaptic vesicles. Both experimental procedures revealed the specific occurrence of multiple small GTP-binding proteins with this organelle. Moreover, direct amino acid sequence analysis assigned at least three different small GTP-binding proteins, ora3, o-ral and o-rab3, to the vesicular compartment. Furthermore, the data reflect the relative abundance of these three proteins on the vesicle membrane, thereby demonstrating the predominant occurrence of o-rab3, the only exclusively synaptic vesicle specific small GTP-binding protein.GTP-binding protein; Cholinergic synaptic vesicle; Electric ray electric organ

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Identification of a heparan sulphate-containing proteoglycan as a specific core component of cholinergic synaptic vesicles from Torpedo marmorata.

Cited by 83 publications

References 24 publications

Isolation and Characterization of Secretory Granules Storing a Vasoactive Intestinal Polypeptide‐Like Peptide in Torpedo Cholinergic Electromotor Neurones

Isolation and Characterization of Secretory Granules Storing a Vasoactive Intestinal Polypeptide‐Like Peptide in Torpedo Cholinergic Electromotor Neurones

The Synaptic Vesicle Protein SV2 Is Complexed with an α5-Containing Laminin on the Nerve Terminal Surface

Association of three small GTP‐binding proteins with cholinergic synaptic vesicles

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