Antibodies to synaptic vesicles purified from Narcine electric organ bind a subclass of mammalian nerve terminals.

Hooper, Judith; Carlson, Steven S.; Kelly, Regis B.

doi:10.1083/jcb.87.1.104

Cited by 41 publications

(18 citation statements)

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“…Alternatively, the rabbit may not exhibit the same plasticity as the rat. The increase in SV levels is consistent with a report of increased immuno- fluorescence labeling in deafferented SCG, using a polyclonal antisera directed against synaptic vesicles (Hooper et al, 1980). However, the investigators did not specify the time after deafferentation that sections were prepared.…”

Section: Discussionsupporting

confidence: 77%

Plasticity of expression of a synaptic vesicle antigen in adult rat superior cervical ganglion

Greif¹

1986

J. Neurosci.

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The effects of deafferentation and alterations of synaptic activity on levels of a synaptic vesicle-specific membrane protein (SV) were studied in the adult rat superior cervical ganglion (SCG) in viva, using a monoclonal antibody directed against the protein. Levels of SV were quantified by radioimmunoassay. Deafferentation of the SCG results in a transient increase in SV levels in the SCG on days 7 and 10 after surgery, with levels then dropping below control levels on days 14, 21, and 30 after surgery. Immunohistochemical labeling of deafferented ganglia indicates that the increase is confined to the perikarya of principal ganglionic neurons. Levels of SV in an SCG target tissue, the iris, do not differ from control levels on day 7 after deafferentation, but are elevated at days 10, 14, and 30 after surgery. After reinnervation of the SCG, levels of SV in the SCG are elevated above control values, but do not differ from control values in the iris. Treatment with chlorisondamine, which blocks synaptic transmission in sympathetic ganglia, produces a significant increase in SV levels in the SCG after 7 d of treatment. Long-term chlorisondamine treatment results in reductions in SV in the SCG after 14 and 28 d. Treatment with phenoxybenzamine for 6 d, which reflexly increases synaptic activity, produces a marked decrease in SV in the SCG. These results suggest that activity, mediated by transsynaptic factors, contributes to the regulation of synthesis of a synaptic vesicle protein in the SCG. The results further suggest that accumulation of synaptic vesicles in terminals of the principal ganglion neurons may help regulate the maintenance of normal synaptic vesicle pools within sympathetic neurons.While ample evidence for neural plasticity exists in the developing nervous system, studies of responses in adult systems have in general shown considerable limitations in the ability to respond to and recover from alterations in connectivity and activity. Among peripheral systems, the adult rat superior cervical ganglion (SCG) is one in which several studies have documented plasticity in response to experimental manipulations. Deafferentation of the SCG by section of the cervical sympathetic trunk (CST) in adult animals has been reported to produce only limited changes in ganglion size in the absence of regeneration of the CST (Gabella, 1976). If the CST is permitted to reinnervate the SCG, recovery of normal numbers of synapses occurs, as assessed by morphometric analysis, and restoration of normal

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Section: Discussionsupporting

confidence: 77%

Plasticity of expression of a synaptic vesicle antigen in adult rat superior cervical ganglion

Greif¹

1986

J. Neurosci.

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“…Synapsin I, which is a substrate for both Ca"-and cAMPdependent protein kinases, is now recognized to be a peripheral membrane protein located at the cytoplasmic surface of synaptic vesicles in many (and possibly all) synapses (10,11,25). Another widely distributed protein exposed at the cytoplasmic surface of synaptic vesicles has been recognized by the use of monoclonal antibodies (33), and one antigen has been localized at the inner surface of the same organelles by polyclonal antibodies (21). Moreover, an internally exposed glycosaminoglycan has been recognized in cholinergic synaptic vesicles (43,44).…”

Section: Stability Of Antibody-toxin-receptor Complexmentioning

confidence: 95%

Specific localization of the alpha-latrotoxin receptor in the nerve terminal plasma membrane.

Valtorta¹,

Madeddu²,

Meldolesi³

et al. 1984

The Journal of Cell Biology

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The receptor for a-latrotoxin, the major protein component of the black widow spider venom, was investigated by the use of the purified toxin and of polyclonal, monospecific anti-a-latrotoxin antibodies . Experiments on rat brain synaptosomes (where the existence of a-latrotoxin receptors was known from previous studies) demonstrated that the toxin-receptor complex is made stable by glutaraldehyde fixation . At saturation, each such complex was found to bind on the average five antitoxin antibody molecules . In frog cutaneous pectoris muscles, the existence of a finite number of high-affinity receptors was revealed by binding experiments with ' 25 1-a-latrotoxin (Kd = 5 x 10-10 M; borax = 1 .36 ± 0.16 [SEJ x 109 sites/mg tissue, dry weight) . Nonpermeabilized muscles were first treated with a-latrotoxin, and then washed, fixed, dissociated into individual fibers, and treated with anti -a-latrotoxin antibodies and finally with rhodamine-conjugated sheep anti-rabbit antibodies. In these preparations, muscle fibers and unmyelinated preterminal nerve branches were consistently negative, whereas bright specific fluorescent images, indicative of concentrated a-latrotoxin binding sites, appeared in the junctional region . These images closely correspond in size, shape, and localization to endplates decorated by the acetylcholinesterase reaction . The presynaptic localization of the specific fluorescence found at frog neuromuscular junctions is supported by two sets of findings: (a) fluorescent endplate images were not seen in muscles that had been denervated ; and (b) the distribution of fluorescence in many fibers treated with alatrotoxin at room temperature was the one expected from swollen terminal branches. Swelling of terminals is a known morphological change induced by a-latrotoxin in this preparation . When muscles were treated with either proteolytic enzymes (trypsin, collagenase) or detergents (Triton X-100) before exposure to a-latrotoxin, the specific fluorescent endplate images failed to appear. Taken together these findings indicate that the a-latrotoxin receptor is an externally exposed protein highly concentrated in the nerve terminal plasma membrane . Its density (number per unit area) at the frog neuromuscular junction can be calculated to be 2,400/um 2.The presynaptic membrane is the portion of the neuronal plasmalemma that surrounds synaptic terminals, where the release of neurotransmitters occurs by fusion of synaptic vesicles (exocytosis) . A number of other important functions (e .g., the recycling of the vesicle membrane, the high-affinity uptake processes of neurotransmitters or transmitter precursors, and the initiation of retrograde transport) are also localized at this level. It is generally agreed that these functional specializations of the presynaptic membrane occur as a consequence ofits molecular dissimilarity with respect to the rest 124 F.

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“…fixed with 2% glutaraldehyde, rinsed overnight, and the peroxidase enzymatic reaction was carried out in 0.1 M Trizma base (pH 7.3) as described (9). The tissue was then osmicated, dehydrated, and embedded in araldite.…”

mentioning

confidence: 99%

A synaptic vesicle antigen is restricted to the junctional region of the presynaptic plasma membrane.

Buckley¹,

Schweitzer²,

Miljanich³

et al. 1983

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

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The plasma membrane of electric organ nerve terminals has two domains that can be distinguished by monoclonal antibodies. A library of 111 mouse monoclonal antibodies raised to nerve terminals from Torpedo californica contains 4 antibodies that bind specifically to the outside of intact synaptosomes. The distribution of the binding sites of these monoclonal antibodies on the outside of intact nerve terminals was examined by immunofluorescence and immunoelectron microscopy. The binding sites of 3 (tor23, 25, and 132) are distributed uniformly over nerve trunks and fine terminal branches. The binding site of the fourth (tor7O) is restricted to synaptic junctional regions. This antibody, but not the other 3, recognizes a major component of synaptic vesicles, a proteoglycan associated with the inner surface of the vesicle membrane. The difference in the pattern of binding of these monoclonal antibodies suggests that the region of the plasma membrane containing active zones is antigenically distinguishable from other nerve terminal plasma membrane. We suggest that the antigen recognized by tor7O is externalized by exocytosis of synaptic vesicles while other plasma antigens take a different route to the surface. The unexpected observation that the vesicle antigen remains on the surface after exocytosis and is prevented from diffusion from the synaptic junctional region would be consistent with an interaction between the vesicle proteoglycan and elements of the synaptic cleft.

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Antibodies to synaptic vesicles purified from Narcine electric organ bind a subclass of mammalian nerve terminals.

Cited by 41 publications

References 54 publications

Plasticity of expression of a synaptic vesicle antigen in adult rat superior cervical ganglion

Plasticity of expression of a synaptic vesicle antigen in adult rat superior cervical ganglion

Specific localization of the alpha-latrotoxin receptor in the nerve terminal plasma membrane.

A synaptic vesicle antigen is restricted to the junctional region of the presynaptic plasma membrane.

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