Structural heterogeneity and subcellular distribution of nicotinic synapse-associated proteins.

Gysin, Reinhard; Wirth, Manfred; Flanagan, Steven D.

doi:10.1016/s0021-9258(19)68403-6

Cited by 65 publications

(58 citation statements)

References 33 publications

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“…This component is composed ofisoelectríc variants (pI = 7.0-8.0), all ofwhich have identical peptide mabs. It is tightly associated with the membrane and can be removed by pH 11 treatment or with LIS (12,21). A second component is found in some but not all preparations and has been called PZ (12) .…”

Section: Characterization Of Monoclonal Antibodiesmentioning

confidence: 99%

“…Membranes highly-enriched in the acetylcholine receptor (AChR)' can be isolated from the electric organ of Torpedo . In addition to the subunits of the AChR, these preparations contain a number ofother proteins, including two prominent ones of apparent molecular weights of 43,000 (43K protein) and 90,000 (90K protein) and numerous other components present in smaller amounts (8,12,14,19,21,28,29). It is important to identify those that are synapse specific since they may participate in the function of the postsynaptic membrane.…”

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confidence: 99%

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Peripheral proteins of postsynaptic membranes from Torpedo electric organ identified with monoclonal antibodies.

Froehner¹

1984

The Journal of Cell Biology

100

101

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Highly purified postsynaptic membranes from Torpedo electric organ contain the acetylcholine receptor as well as other proteins . To identify synapse-specific components, we prepared monoclonal antibodies (mabs) to proteins extracted from the membranes with either lithium diiodosalicylate or alkaline treatment . 10 mabs specific for three different proteins were obtained . Seven mabs reacted with a major 43,000-mol-wt protein (43K protein) . This protein is composed of isoelectric variants (pl = 7.2-7.8) and each of the mabs reacted with all of the variants. Analysis of these mabs by competition for binding to 43K protein and by reaction with proteolytic fragments of 43K protein in immunoblots showed that they recognize at least five different epitopes. Two mabs reacted with a protein of 90,000 mol wt (90K protein) and one with a protein of 58,000 mol wt composed of isoelectric variants (pl = 6.4-6.7) (58K protein) . The 43K and 58K proteins appeared to co-purify with the receptorcontaining membranes while the 90K protein did not . Immunofluorescence experiments indicated that the anti-43K mabs bind to the innervated face of Torpedo electrocytes and that a component related to the 43K protein is found at the rat neuromuscular junction . The anti-58K mab stained the innervated face, although rather weakly, while the anti-90K mabs reacted intensely with the non-innervated membrane . Thus, the 43K protein and possibly also the 58K protein are synaptic components while the 90K protein is predominantly nonsynaptic .

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Section: Characterization Of Monoclonal Antibodiesmentioning

confidence: 99%

mentioning

confidence: 99%

Peripheral proteins of postsynaptic membranes from Torpedo electric organ identified with monoclonal antibodies.

Froehner¹

1984

The Journal of Cell Biology

100

101

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“…The supernatam was aspirated to 0.8 ml and mixed with 2.4 ml H20 and centrifuged again as above but without the sucrose underlayer. The pellet was resuspended in a twofold concentrate of modified Laemmli sample buffer (17,22) and electrophoresis performed as described previously (17). Assessment of the relative proportion of protein bands was performed using an ACD-18 automated microdensitometer (Gelman Instrument Co., Ann Arbor, MI).…”

Section: Preparation and Analysis Of 5ubcellular Fractionsmentioning

confidence: 99%

“…Assessment of the relative proportion of protein bands was performed using an ACD-18 automated microdensitometer (Gelman Instrument Co., Ann Arbor, MI). Peptide analysis of selected bands from the SDS polyaerylamide gels was performed as described previously (13,17).…”

Section: Preparation and Analysis Of 5ubcellular Fractionsmentioning

confidence: 99%

Putative 51,000-Mr protein marker for postsynaptic densities is virtually absent in cerebellum.

Flanagan¹,

Yost²,

Crawford³

1982

The Journal of Cell Biology

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Cerebrum and cerebellum contain numerous asymmetric synapses characterized by the presence of a postsynaptic thickening prominently stained by phosphotungstic acid and other electron-dense stains suitable for electron microscopy. A 51,000-Mr protein, copurified in postsynaptic density-enriched fractions from cerebrum, is considered to be a well established marker for the postsynaptic density. On the basis of two criteria, our studies demonstrate that the 51,000-Mr protein marker for postsynaptic densities is virtually absent in cerebellum. First, it is present in negligible amounts in deoxycholate-insoluble fractions from cerebellum but abundant in parallel fractions from cerebrum. Secondly, the 51,000-Mr protein, which binds 12Sl-calmodulin after SDS PAGE, is readily visualized in membrane samples from cerebrum but is virtually undetectable in cerebellar samples. It is apparent that these results require reexamination of the role of the 51,000-Mr protein in postsynaptic density structures.

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“…Επιπλέον αυτών βρέθηκε μία ομάδα πρωτεϊνών μοριακού βά ρους 43-kd η οποία είναι ειδική γιά τους σκελετικούς μύες και γιά το ηλεκτρικό όργανο του Torpedo. Την ομάδα των 43-kd πρωτεϊνών απαρτίζουν: η vi η οποία είναι βασική, η \ζ η οποία είναι ενδιάμεση και η V3 η οποία είναι όξινη (Gysin et al 1981). Η V2 έχει βρεθεί ότι είναι κινάση της κρεατινίνης, η V3 βρέθηκε ότι είναι ακτίνη (Gysin et al 1983).…”

Section: θέση πρόσδεσης της α-Bungarotoxin (Ccbgt)unclassified

Μελετη Της Βαρειας Μυασθενειας Και Του Υποδοχεα Της Ακετυλοχολινης Με Την Βοηθεια Μονοκλωνικων Αντισωματων

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Structural heterogeneity and subcellular distribution of nicotinic synapse-associated proteins.

Cited by 65 publications

References 33 publications

Peripheral proteins of postsynaptic membranes from Torpedo electric organ identified with monoclonal antibodies.

Peripheral proteins of postsynaptic membranes from Torpedo electric organ identified with monoclonal antibodies.

Putative 51,000-Mr protein marker for postsynaptic densities is virtually absent in cerebellum.

Μελετη Της Βαρειας Μυασθενειας Και Του Υποδοχεα Της Ακετυλοχολινης Με Την Βοηθεια Μονοκλωνικων Αντισωματων

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