Brain Ribosomes

Zomzely-Neurath, Claire; Roberts, Sidney

doi:10.1007/978-1-4615-7748-5_5

Cited by 19 publications

(9 citation statements)

References 70 publications

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“…These studies showed that S-100 protein was synthesized predominantly on free polysomes, but did not exclude an absolute requirement of a brainspecific factor for translation of s-100 protein messenger RNA. Although s-100 protein could be synthesized efficiently in a crossed reconstituted system of brain polysomes and a liver enzyme fraction [28] the results of these experiments were inconclusive since initiation and elongation factors are known to be associated with polysomes.…”

Section: Discussionmentioning

confidence: 99%

Synthesis of the Brain‐Specific S‐100 Protein in a Cell‐Free System from Wheat Embryo Programmed with Poly(A)‐Containing RNA from Rabbit Brain

Mahony

Brown

Labourdette

et al. 1976

European Journal of Biochemistry

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Polyadenylated polysonial RNA was prepared from rabbit cerebral hemispheres using phenol extraction and chromatography on oligo(dT)‐cellulose. This RNA directed the synthesis of the brain‐specific S‐100 protein in cell‐free extracts front wheat embryo. S‐100 protein was absent from the products of endogenous incorporation and from a reaction programmed with kidney mRNA. These results suggest that S‐100 protein mRNA contains a poly(adenylic acid) sequence and rule out the necessity of a brain‐specific factor for translation of S‐100 protein mRNA.

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Section: Discussionmentioning

confidence: 99%

Synthesis of the Brain‐Specific S‐100 Protein in a Cell‐Free System from Wheat Embryo Programmed with Poly(A)‐Containing RNA from Rabbit Brain

Mahony

Brown

Labourdette

et al. 1976

European Journal of Biochemistry

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“…A postmicrosomal supernatant, prepared in 10 mM Tris-HC1, pH 7.6, 5.2 mM MgCI2, 0.2 mM EDTA, 1 mM DTT, and 0.3 M sucrose (Falvey and Staehelin, 1970) was diluted with 2 volumes of 1 mM DTT. The pH was then adjusted to 4.7 with 1 M acetic acid (Zomzely-Neurath and Roberts, 1972). After being stirred for 30 rnin at 4"C, the precipitate was collected by centrifugation at 34,500 X g for 15 min.…”

Section: Preparation Of Ph 5 Enzymesmentioning

confidence: 99%

In Vitro Synthesis of the Four Mouse Myelin Basic Proteins: Evidence for the Lack of a Metabolic Relationship

Campagnoni

1982

Journal of Neurochemistry

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Studies on the synthesis of the four immunologically related mouse myelin basic proteins (MBPs) were carried out to determine if these proteins were metabolically related. Two in vitro systems were used: (a) a homologous brain system consisting of free polysomes, pH 5 enzymes, and initiation factors; and (b) a reticulocyte lysate system directed with mRNA and supplemented with brain factors. Incorporation of [35S]methionine into the four MBPs (14K, 17K, 18.5K, and 21.5K) was detected by immunoprecipitation of the in vitro products of synthesis followed by sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis. The four MBPs were identified by cross‐reactivity with purified anti‐MBP antibodies and their apparent molecular weights in SDS gels. Synthesis of all four proteins was detected in both systems soon after the incubations were begun. The kinetics of the labeling of the proteins showed no evidence of a precursor‐product relationship (i.e., 21.5K→ 18.5K; 17K → 14K) in either system. Inhibition studies with puromycin and “chase” experiments with unlabeled methionine demonstrated that neither system contained posttranslational “processing” activity. Thus, the 21.5K and 17K proteins were not being processed into the 18.5K and 14K MBPs by either . in vitro system. Detection of the synthesis of all four proteins in the reticulocyte system programmed with brain mRNA indicates that the four proteins are probably coded for by separate mRNAs. This conclusion was supported by studies using polyribosomes separated into different size classes, which suggest that the mRNAs for the four proteins may be translated on proteins of differing size class. It is proposed, therefore, that the four MBPs are the primary translation products of independent brain mRNAs and are not metabolically related.

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“…Soluble and ribosomal proteins were extracted from five pooled young and five pooled old mouse brains closely following the technique of Zomzely-Neurath and Roberts (42). 1 g of brain was homogenized in 9 ml of 50 niM Trizma-HCl (pH 7.4), 25 triAf KC1, 4 mM MgCI., 250 mM sucrose (TKMS), then centrifuged at 15,000 # for 15 min at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

Electrophoretic Analysis of Brain Proteins from Young Adult and Aged Mice

Vaughan¹,

Calvin²

1977

Gerontology

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The purpose of this study was to electrophoretically examine proteins from mice of different ages to determine whether general changes occurred in protein levels during senescence and to relate the data to specific ageing hypotheses involving proteins. Proteins from whole brain, brain regions, soluble and ribosomal brain fractions, from young adult and senescent mice, were totally solubilized and subjected to polyacrylamide slab gel electrophoresis. The resulting gel patterns were then compared by examining the intensity of gel bands of the same migration distance. Positive controls were used to establish the high sensitivity of the electrophoretic method. For example, band intensity differences were observed when brain proteins from different species, different periods of growth and development, normal and mutant mice, and different brain regions were compared. Virtually all band intensities and, therefore, corresponding brain protein concentrations were unchanged when patterns from senescent mice were compared to patterns from younger adult mice. These results provide evidence against ageing hypotheses involving: (1) progressive programmed ageing; (2) protein cross-linking, and (3) a systematic shutdown of gene activity. The few, select, protein band changes that did occur provide evidence that (1) the volume of the brain vascular system decreases with age, and (2) the brain S-100 protein concentration increases with age.

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Brain Ribosomes

Cited by 19 publications

References 70 publications

Synthesis of the Brain‐Specific S‐100 Protein in a Cell‐Free System from Wheat Embryo Programmed with Poly(A)‐Containing RNA from Rabbit Brain

Synthesis of the Brain‐Specific S‐100 Protein in a Cell‐Free System from Wheat Embryo Programmed with Poly(A)‐Containing RNA from Rabbit Brain

In Vitro Synthesis of the Four Mouse Myelin Basic Proteins: Evidence for the Lack of a Metabolic Relationship

Electrophoretic Analysis of Brain Proteins from Young Adult and Aged Mice

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