Chromosomal and Cytoplasmic Regulation of Haemoglobin Synthesis

2015 ◽  
pp. 1056-1063
Author(s):  
C. Baglioni
BMJ ◽  
1974 ◽  
Vol 4 (5942) ◽  
pp. 451-454 ◽  
Author(s):  
D. J. Weatherall

1974 ◽  
Vol 144 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Hugh Woodland ◽  
Sarah E. Ayers

Micro-injection into the oocytes and eggs of Xenopus laevis was used to ascertain the effects of synthetic polyribonucleotides on protein synthesis in living cells. Poly(U) and poly(A) were not translated detectably, nor did they change the rate of endogenous protein synthesis. The same was true of poly(G,U), poly(A,G,U), poly(A,C,G,U), G-U-G-(U)n, A-(U)n and AUG. In contrast, A-U-G-(U)n was a potent inhibitor of protein synthesis in the cell. This might be because it is initiated normally but lacks a termination codon, or because it inhibits the translation of other molecules in some way not dependent on its normal initiation. Poly(G,U), poly(A,G,U) and poly(A,C,G,U) inhibited haemoglobin synthesis when they were injected into the oocyte with haemoglobin mRNA. The synthetic polyribonucleotides did not inhibit the translation of the natural mRNA when the two sorts of molecules were injected at different times. It is suggested that the synthetic RNA molecules compete with the natural mRNA for a pre-initiation factor in limited supply.


1973 ◽  
Vol 241 (111) ◽  
pp. 207-209 ◽  
Author(s):  
R. H. BROYLES ◽  
E. FRIEDEN

1981 ◽  
Vol 48 (2) ◽  
pp. 237-250 ◽  
Author(s):  
Philippa D. Darbre ◽  
S. M. Lauckner ◽  
J. W. Adamson ◽  
W. G. Wood ◽  
D. J. Weatherall

Development ◽  
1971 ◽  
Vol 26 (2) ◽  
pp. 313-322
Author(s):  
R. I. Freshney ◽  
J. Paul

Aminolaevulinate synthetase, aminolaevulinate dehydratase, and haem synthetase, three enzymes which may have a regulatory role in haem synthesis, have been determined in liver extracts from different foetal stages of the mouse. Haemoglobin synthesis increases rapidly from early on the 14th day, after fertilization, to reach a maximum late on the 15th day. Aminolaevulinate synthetase reaches a maximum on the 14th day, 24–36 h before the peak of haemoglobin synthesis, aminolaevulinate dehydratase on the 15th day, about 12 h before the peak of haemoglobin synthesis, and haem synthetase on the 17th day. Maximal activity of aminolaevulinate synthetase and aminolaevulinate dehydratase is of only a few hours' duration. Throughout embryonic development the activities of all three enzymes are higher than in the adult liver. The absence of a correlation of enzyme activity with foetal liver cell population changes implies that fluctuations in enzyme activity cannot be explained solely by changes in the proportions of different cell types. The high levels of activity relative to those of adult liver may be related to the high proportion of erythroid cells in the foetal liver. It is concluded that these enzymes are unlikely to form rate-limiting steps during the increase in haemoglobin synthesis between 14 and 15 days.


Development ◽  
1965 ◽  
Vol 13 (3) ◽  
pp. 275-283
Author(s):  
E. M. Deuchar ◽  
A. M. L. Dryland

In an earlier publication (Deuchar & Dryland, 1964) it was reported that α-methyl-norvaline, an amino acid described by Ross et al. (1961), whose structure resembles that of both valine and leucine (see below), caused a visible reduction in the quantity of haemoglobin formed by explants of the area vasculosa of the 48-hr, chick embryo, as compared with controls explanted without the analogue present. The structure of the haemoglobin molecule in birds has not yet been fully worked out, but according to recent work (reviewed by Gratzer & Allison, 1960) there are at least four N-terminal valine groups, two of which have leucine adjacent to them. The inhibition of haemoglobin synthesis by α-methyl-norvaline might, therefore, be due to competition with valine or leucine for uptake into these terminal sites on the peptide chains of the globin. The analogue might itself be taken up in their place, forming an abnormal haemoglobin.


1982 ◽  
pp. 37-49
Author(s):  
N. J. Russell ◽  
G. M. Powell ◽  
J. G. Jones ◽  
P. J. Winterburn ◽  
J. M. Basford

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