Changes in the ribosome distribution during incubation of rabbit reticulocytes in vitro

Knopf, Paul M.; Lamfrom, Hildegard

doi:10.1016/0005-2787(65)90186-3

Cited by 73 publications

(17 citation statements)

References 12 publications

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“…Similar findings are reported by several workers [3,10,18,20], namely, a marked shift of polyribosomes toward lighter aggregates after prolonged fasting was observed in rat liver. This shift of polyribosomes occurs independent of new synthesis of messenger RNA, and a change in ribosome spacing on messenger RNA is considered as an interpretation of the result.…”

Section: Discussionsupporting

confidence: 92%

Isolation of Polyribosome from Tobacco Plants Infected with Tobacco Mosaic Virus

Kiho

1968

Japanese Journal of Microbiology

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Section: Discussionsupporting

confidence: 92%

Isolation of Polyribosome from Tobacco Plants Infected with Tobacco Mosaic Virus

Kiho

1968

Japanese Journal of Microbiology

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“…10, 16, 37, 43, 95, and 106). The first steps involve a and b globin gene translation, which takes place on the order of a few minutes per subunit (25,51,63,72,73). Given that a helices and other structural features are capable of forming spontaneously in less than a few microseconds (30,36,41,111), it is plausible that a and b chains could acquire some of their secondary and tertiary structure co-translationally.…”

Section: Pathways For Hemoglobin Assembly In Vivo and In Vitromentioning

confidence: 99%

The Role of Alpha-Hemoglobin Stabilizing Protein in Redox Chemistry, Denaturation, and Hemoglobin Assembly

Mollan

Weiss

et al. 2010

Antioxidants & Redox Signaling

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Hemoglobin biosynthesis in erythrocyte precursors involves several steps. The correct ratios and concentrations of normal alpha (a) and beta (b) globin proteins must be expressed; apoproteins must be folded correctly; heme must be synthesized and incorporated into these globins rapidly; and the individual a and b subunits must be rapidly and correctly assembled into heterotetramers. These events occur on a large scale in vivo, and dysregulation causes serious clinical disorders such as thalassemia syndromes. Recent work has implicated a conserved erythroid protein known as Alpha-Hemoglobin Stabilizing Protein (AHSP) as a participant in these events. Current evidence suggests that AHSP enhances a subunit stability and diminishes its participation in harmful redox chemistry. There is also evidence that AHSP facilitates one or more early-stage post-translational hemoglobin biosynthetic events. In this review, recent experimental results are discussed in light of several current models describing globin subunit folding, heme uptake, assembly, and denaturation during hemoglobin synthesis. Particular attention is devoted to molecular interactions with AHSP that relate to a chain oxidation and the ability of a chains to associate with partner b chains. Antioxid. Redox Signal. 12, 219-232.

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“…However it seems unlikely that even nucleated red blood cells would continue to synthesize hemoglobin for many minutes after immersion in a large volume of ice water containing fluoride and cyanide. Knopf and Lamfrom observed no protein synthesis in rabbit reticulocytes incubated for 4 hr at 0C (16). In addition, the results obtained with sickle thalassemic blood containing no nucleated red blood cells suggest that a resistance of nucleated cells to the method used to stop synthesis cannot completely explain the increased radioactivity of the N-terminal valine in thalassemic cells at 3 min.…”

Section: Methodsmentioning

confidence: 94%

“…Table I lists the patients whose blood was used for the study of P-globin m-RNA translation. Five patients of Italian descent, ages [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] yr, with Cooley's anemia or P-thalassemia major were examined. All had severe anemia and, except for one patient, required blood transfusions at 1-2 month intervals.…”

Section: Methodsmentioning

confidence: 99%

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Translation of β-Globin m-RNA in β-Thalassemia and the S and C Hemoglobinopathies

Rieder¹

1972

J. Clin. Invest.

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A B S T R A C T Genetic and biochemical evidence indicates that in 13-thalassemia there is impaired synthesis of the P-globin chains of hemoglobin A. In patients heterozygous for the hemoglobinopathies, hemoglobin S and hemoglobin C, the mutant 1-chain is produced in smaller amounts than normal PI. Defective m-RNA translation has been suggested as a possible cause of decreased 1-globin polypeptide synthesis in thalassemia and the hemoglobinopathies. In the present study, the ribosomal assembly of 13-globin chains was examined in the peripheral, nucleated red blood cells and reticulocytes of patients with Cooley's anemia, thalassemia intermedia, sickle thalassemia, sickle cell anemia, hemoglobin C disease, and in hemolytic anemias not associated with a hemoglobinopathy. The translation times of PA Ps , and P' did not differ significantly (average times: pA = 75 sec. range 43-114, ps = 69 sec, pc = 92 sec).In thalassemia, no evidence was found for a delay in translation as the cause of the marked impairment of 13-globin synthesis. In several specimens of peripheral blood from thalassemic patients, the translation time of the P-chain was even shorter than in nonthalassemic specimens (average time = 45 sec, range 35-59). The results suggest that the defect in 13-globin synthesis in P-thalassemia is due to impaired initiation of 13-globin chain assembly or a quantitative deficiency in m-RNA.

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Changes in the ribosome distribution during incubation of rabbit reticulocytes in vitro

Cited by 73 publications

References 12 publications

Isolation of Polyribosome from Tobacco Plants Infected with Tobacco Mosaic Virus

Isolation of Polyribosome from Tobacco Plants Infected with Tobacco Mosaic Virus

The Role of Alpha-Hemoglobin Stabilizing Protein in Redox Chemistry, Denaturation, and Hemoglobin Assembly

Translation of β-Globin m-RNA in β-Thalassemia and the S and C Hemoglobinopathies

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