Protein Synthesis in Erythroid Cells, I. Reticulocyte Ribosomes Active in Stimulating Amino Acid Incorporation

Marks, Paul A.; Burka, Edward R.; Schlessinger, David

doi:10.1073/pnas.48.12.2163

Cited by 177 publications

(37 citation statements)

References 19 publications

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“…These free a-chains have been shown not to be present in HbA (4,6,7). This report demonstrates that the free a-chains produced by the cells of patients with 8- Ringer bicarbonate solution and with either leucine-'H, leucine-'4C, or "C-amino acid mixture, as described previ-ously (4,8). Incorporation into globin was always linear during the hour of incubation.…”

Section: Introductionmentioning

confidence: 54%

Hemoglobin synthesis in β-thalassemia: the properties of the free α-chains

Bank¹

1968

J. Clin. Invest.

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Section: Introductionmentioning

confidence: 54%

Hemoglobin synthesis in β-thalassemia: the properties of the free α-chains

Bank¹

1968

J. Clin. Invest.

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“…Numerous studies (7)(8)(9)(11)(12)(13)(14)(15)(16)(17) implicate the polyribosome as the site of protein synthesis. The loss in protein-synthesizing capacity which accompanies erythroid cell maturation appears to be related to the observed fall in polyribosome content.…”

Section: Discussionmentioning

confidence: 99%

Alterations in Polyribosomes During Erythroid Cell Maturation

Rifkind

Danon

Marks

1964

The Journal of Cell Biology

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107

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This communication presents a morphological study of the changes in ribosome content and organization which occur during the maturation of erythroid cells of the phenylhydrazinetreated rabbit. Electron micrographs of thin sectioned nucleated and non-nucleated erythroid cells have been subjected to a quantitative analysis of the distribution of ribosomes as polyribosomes of various sizes and as single ribosomes. The ribosomes of nucleated erythroid cells of marrow are virtually all arranged in the polyribosome configuration consisting of clusters of 2 to 6 individual ribosomes. These cells are the most active in the erythroid series in protein biosynthesis. During maturation to the non-nucleated reticulocyte stage, found in the circulating blood, there is a decrease in protein synthesizing capacity, a fall in total ribosome content, and, more significantly, a decrease in the number and size of polyribosomes. Maturation to the ribosome-free erythrocyte, either under in vitro or in vivo conditions, entails a further decrease in protein synthesis which correlates with a progressive disaggregation of the biosynthetically active polyribosomes into smaller clusters and inactive single ribosomes. Possible models which may account for the stability of the polyribosome and for the mechanism of polyribosome dissociation are discussed.

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“…The increase in mean cell age which occurred during the recovery phase was thus accompanied by a progressive increase in the proportion of RNA which was soluble RNA. Since the reticulocyte does not synthesize RNA (21), and high molecular weight degradation products of ribosomal RNA do not accumulate within the cell (11,15), these data indicate that during erythroid cell maturation soluble RNA is degraded at a rate slower than that of ribosomal RNA.…”

Section: Methodsmentioning

confidence: 97%

Characteristics of RNA degradation in the erythroid cell

Burka¹

1969

J. Clin. Invest.

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A B S T R A C TRNA within the cell fluxes freely back and forth between the free and membrane-bound forms. The rate of loss of RNA in the membrane-bound compartment, both in the intact cell and in isolated membranes, is approximately threefold that found in the cell as a whole.During maturation the proportion of total cell RNA which is bound to the membrane decreases. The bulk of RNA destroyed is derived from the free compartment, but bound is also destroyed. The cell membrane participates in RNA metabolism and may be a site of RNA degradation in the erythroid cell.

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Protein Synthesis in Erythroid Cells, I. Reticulocyte Ribosomes Active in Stimulating Amino Acid Incorporation

Abstract: The synthesis of hemoglobin proceeds in nonnucleated erythrocytes.' Studies with reticulocytes indicate specifically that the biosynthesis of globin is initiated on the ribosomes.24 Tissieres and co-workers5 demonstrated that in E. coli nascent protein synthesis

Cited by 177 publications

References 19 publications

Hemoglobin synthesis in β-thalassemia: the properties of the free α-chains

Hemoglobin synthesis in β-thalassemia: the properties of the free α-chains

Alterations in Polyribosomes During Erythroid Cell Maturation

Characteristics of RNA degradation in the erythroid cell

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