Synthesis of S100 Protein on Free and Membrane‐Bound Polysomes of the Rabbit Brain

Cosgrove, James W.; Heikkila, John J.; Marks, Alexander; Brown, Ian R.

doi:10.1111/j.1471-4159.1983.tb08051.x

Cited by 19 publications

(3 citation statements)

References 51 publications

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“…CK, neuron-specific enolase and protein 14-3-3 were identified as products of membrane-bound as well as of free polyribosomes. The synthesis of other proteins, including the glial-cell markers myelin basic protein, S-100 and carbonic anhydrase, has also been reported to occur on both membrane-bound and free polyribosomes in the brain (Hall et al, 1982;Cosgrove et al, 1983;Sapirstein et al, 1983).…”

Section: Resultsmentioning

confidence: 99%

Characterization of translation products of the polyadenylated RNA of free and membrane-bound polyribosomes of rat forebrain

Hall¹,

Mahadevan²,

Whatley³

et al. 1984

Biochemical Journal

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Poly(A)+ RNA (polyadenylated RNA) isolated from membrane-bound and free polyribosomes was translated in reticulocyte lysates, and the products were analysed by two-dimensional gel electrophoresis. Several translation products were specific to membrane-bound polyribosomal mRNA, including polypeptides of 47kDa, 35kDa and 21 kDa, whereas others (e.g. of 37 kDa, 17 kDa and 14 kDa) were specific to free polyribosomal mRNA. Although many products were common to both mRNA species, cross-contamination could be ruled out on the basis of the presence of these and other specific products. The common products included a 68 kDa microtubule-associated protein, tubulin, actin, the brain form of creatine kinase, neuron-specific enolase and protein 14-3-3 and calmodulin, all of which were identified on the basis of two-dimensional gel and peptide analyses. The 35 kDa protein product of membrane-specific mRNA was co-translationally processed in vitro by microsomal membranes, resulting in its cleavage to 33 kDa (and partial glycosylation). The 33 kDa processed protein (but not the 35 kDa precursor) was integrated into both dog pancreas and rat brain microsomal membranes. The occurrence of the enzymes and calmodulin as products of membrane-bound polyribosomal mRNA is discussed in the light of their presence on rat brain synaptic plasma membranes [Lim, Hall, Leung, Mahadevan & Whatley (1983) J. Neurochem. 41, 1177-1182] and their existence in a specific component of axonal flow. It is suggested that some of these translation products of the rough endoplasmic reticulum may represent proteins destined for the plasma membrane. However, the identity and location of the 35 kDa membrane-specific product (or its processed form) still remain unestablished.

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Section: Resultsmentioning

confidence: 99%

Characterization of translation products of the polyadenylated RNA of free and membrane-bound polyribosomes of rat forebrain

Hall¹,

Mahadevan²,

Whatley³

et al. 1984

Biochemical Journal

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“…Proteins synthesized in run-off reactions of these two types of polysomes were analyzed. Peripherin was synthesized in either case (re sults not shown), as found for several other proteins [16,[19][20][21][22].…”

Section: Synthesis O F Peripherin In Vitromentioning

confidence: 99%

Regulation of Peripherin in Mouse Neuroblastoma and Rat PC 12 Pheochromocytoma Cell Lines

Portier¹,

Brachet²,

Croizat³

et al. 1983

Dev Neurosci

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Peripherin (formerly the Y protein) is found in the peripheral nervous system. This Triton-insoluble protein is characterized by its isoelectric point (5.6), its apparent molecular weight (56,000 daltons) and its peptidic map. Peripherin was also observed in a mouse neuroblastoma cell line, NIE 115, where its expression appeared regulated by the presence of an inducer of morphological differentiation. In order to analyze more precisely this control, the presence of peripherin was investigated in several neuroblastoma cell lines which exhibit different morphological patterns of differentiation and in the rat pheochromocytoma PC 12 cell line. Differentiation of these cells was induced with 1-methylcyclohexane carboxylic acid (CCA) and nerve growth factor (NGF), respectively. Peripherin was found in these different cell lines. Moreover, the cellular amount of peripherin appraised by [³⁵S]-methionine incorporation was significatively increased in differentiated cells. In contrast, other cytoskeletal components did not undergo a similar raise. The level at which the control of the peripherin content takes place was studied in a cell-free translation system. Poly(A)-rich RNAs extracted from growing or differentiated NIE 115 cells directed the synthesis of similar amounts of peripherin in a reticulocyte lysate. In contrast, polysomes prepared from differentiated cells and the corresponding polysomal RNA programmed in vitro the synthesis of twice more peripherin than polysomes or polysomal RNA from growth-phase cells. Since peripherin synthesis is enhanced 5 times in living cells, it seems probable that the cellular amount of peripherin is controlled partly at the translational level and partly at the turn-over level.

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“…al., 1974), synaptosomes (Rusca et al, 1972;Donato et al, 1975), and neuronal nuclei (HydCn and McEwen, 1966;Hansson et al, 1975); and specific high affinity binding sites for S-100 have been reported in synaptic membranes (Donato et al, 1975;Donato, 1976). In addition, the major portion of the protein appears to be synthesized on membrane-bound polysomes (Cosgrove et al, 1983), a characteristic of secreted proteins in non-CNS tissue. These observations raise the possibility that S-100 protein is synthesized in glial cells, but has a site of action on or in neurons.…”

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confidence: 99%

Proteins of the Brain Extracellular Fluid: Evidence for Release of S‐100 Protein

Shashoua

Hesse

Moore

1984

Journal of Neurochemistry

175

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Extracellular protein fractions were obtained (1) by mild, isotonic irrigation of freshly perfused brain tissue; (2) by collection of proteins released into superfusing medium by physiologically viable slices of rat hippocampus; and (3) by sampling the CSF of anesthetized rats. Analysis of the S-100 protein content of these fractions gave values of 2.8, 4.2, and 1.8 micrograms S-100/mg protein, respectively. These values were three- to sixfold higher than the S-100 content of the soluble cytoplasmic protein fractions from the same tissue. This several-fold higher S-100 content of the extracellular protein fractions relative to the intracellular cytoplasmic protein fractions indicates that S-100 is selectively released into the extracellular spaces of the brain. We suggest that the biological function of this CNS protein may involve intercellular transfer.

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Synthesis of S100 Protein on Free and Membrane‐Bound Polysomes of the Rabbit Brain

Cited by 19 publications

References 51 publications

Characterization of translation products of the polyadenylated RNA of free and membrane-bound polyribosomes of rat forebrain

Characterization of translation products of the polyadenylated RNA of free and membrane-bound polyribosomes of rat forebrain

Regulation of Peripherin in Mouse Neuroblastoma and Rat PC 12 Pheochromocytoma Cell Lines

Proteins of the Brain Extracellular Fluid: Evidence for Release of S‐100 Protein

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