SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF THE S‐100 PROTEIN BINDING ACTIVITY OF SYNAPTOSOMAL PARTICULATE FRACTIONS<sup>1</sup>

Donato, Rosario

doi:10.1111/j.1471-4159.1977.tb10426.x

Cited by 21 publications

(6 citation statements)

References 19 publications

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“…The kinetics of recombinant S1 000's neurite extension activity suggests a receptor-mediated mechanism ( Winningham-Major et al, 1989). In addition, binding sites for SlOO on neuronal membranes have been reported ( Donato, Michetti, and Miani, 1975;Donato, 1977).…”

Section: Figure 5 Sloo Localization In Both Neurons and Schwann Cellsmentioning

confidence: 97%

S100 is present in developing chicken neurons and schwann cell and promotes motor neuron survival in vivo

et al. 1992

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We used polyclonal antisera recognizing S100, a small acidic protein highly enriched in nervous tissue, to stain sections of embryonic chicken lumbosacral spinal cord and hindlimb. S100 immunoreactivity was detected in developing sensory neurons of the dorsal root ganglia (DRG) and motor neurons of the ventral spinal cord as early as embryonic day (E) 5, and staining persisted through hatching. In contrast, expression of S100 first became apparent in Schwann cells at E13, just before myelination, and was not detected in developing skin or muscle. Since S100 beta was present in motor and sensory neurons and is known to promote neuronal survival and neurite extension in vitro (Winningham-Major, Staecker, Barger, Coats, and Van Eldik, 1989), we tested the ability of S100 to promote neuron survival in an in ovo survival assay. Addition of S100 to chick embryos in ovo during the period of naturally occurring motor neuron cell death resulted in a significant increase in motor neuron survival, but had no effect on the in vivo survival of sensory neurons in the DRG. The findings that S100 is present in spinal motor neurons and that the addition of S100 enhances the survival of these cells in vivo are consistent with the possibility that S100 may act as a naturally occurring neuron survival factor during development.

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Section: Figure 5 Sloo Localization In Both Neurons and Schwann Cellsmentioning

confidence: 97%

S100 is present in developing chicken neurons and schwann cell and promotes motor neuron survival in vivo

et al. 1992

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“…Both membrane proteins and lipids seem to be involved in the binding process (Donato, 1976b). The binding activity of membranes can be solubilized by the nonionic detergent Triton X-100, with the retention in solution of all the properties it has in membranes (Donato, 1977).…”

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confidence: 99%

Heterogeneity of the S‐100 Protein Specific Binding Sites in Synaptosomal Particulate Fractions and Subfractions

Donato

1982

Journal of Neurochemistry

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The specific interaction of S-100 protein with synaptosomal particulate fractions (SYN) was further investigated with special reference to the number of binding components and their localization in synaptosomal subfractions. Binding studies were conducted on SYN from various CNS regions, on synaptosomal subfractions from the cerebral cortex, and on cerebral cortex SYN under various conditions. The results suggest that S-100 binds to two populations of membrane sites: high -affinity sites, which seem to be confined to neuronal membranes (synaptosomal plasma membranes and synaptic vesicles), and low-affinity sites, which are also detected in other membranes. The data are consistent with the view that the biphasic profile of S-100 binding to SYN does not result from heterogeneity of the S-100 molecule, and that the Ca2+ conformation of the protein is as important as the proper conformation of the binding site for full expression of high-affinity binding.

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“…The interaction of the brain-specific S-100 protein (Moore, 1965) with synaptosomal particulate fractions (SYN) has been characterized under several aspects (Donato and Michetti, 1974;Donato et al, 1975;Donato, 1976b;1977;1978). One feature of the S-100 binding to SYN is its partial irreversibility (Donato et al, 1975;Donato, 1976b;1978).…”

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confidence: 99%

The Specific Interaction of S‐100 Protein with Synaptosomal Particulate Fractions. Evidence for the Formation of a Tight Complex Between S‐100 and Its Binding Sites

Donato

1981

Journal of Neurochemistry

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The dissociation of the 125I-labelled S-100 specifically bound to synaptosomal particulate fractions (SYN) has been studied under a variety of conditions after different association times. The results indicate that after a critical association time of about 20 min at 37 degrees C, the bound protein becomes progressively less accessible to the dissociating agents of conditions employed. These findings support the view that the partial irreversibility of the 125I-labelled S-100 binding to SYN could be due to the formation of a tight complex between the protein and its synaptosomal sites. These data are discussed mainly in relation to the particulate-bound fraction of native S-100.

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SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF THE S‐100 PROTEIN BINDING ACTIVITY OF SYNAPTOSOMAL PARTICULATE FRACTIONS¹

Cited by 21 publications

References 19 publications

S100 is present in developing chicken neurons and schwann cell and promotes motor neuron survival in vivo

S100 is present in developing chicken neurons and schwann cell and promotes motor neuron survival in vivo

Heterogeneity of the S‐100 Protein Specific Binding Sites in Synaptosomal Particulate Fractions and Subfractions

The Specific Interaction of S‐100 Protein with Synaptosomal Particulate Fractions. Evidence for the Formation of a Tight Complex Between S‐100 and Its Binding Sites

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SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF THE S‐100 PROTEIN BINDING ACTIVITY OF SYNAPTOSOMAL PARTICULATE FRACTIONS1

Cited by 21 publications

References 19 publications

S100 is present in developing chicken neurons and schwann cell and promotes motor neuron survival in vivo

S100 is present in developing chicken neurons and schwann cell and promotes motor neuron survival in vivo

Heterogeneity of the S‐100 Protein Specific Binding Sites in Synaptosomal Particulate Fractions and Subfractions

The Specific Interaction of S‐100 Protein with Synaptosomal Particulate Fractions. Evidence for the Formation of a Tight Complex Between S‐100 and Its Binding Sites

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SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF THE S‐100 PROTEIN BINDING ACTIVITY OF SYNAPTOSOMAL PARTICULATE FRACTIONS¹