Developmental capacities of the goldfish egg, provided with erythrocyte nucleus from adult carp

1982 ◽  
Vol 1 (1) ◽  
pp. 104-110
Author(s):  
Wu Shangqin ◽  
S. C. Wu ◽  
Cai Naner ◽  
Xu Quanhan
Keyword(s):  
1982 ◽  
Vol 55 (1) ◽  
pp. 157-187
Author(s):  
E.C. Pearson ◽  
H.G. Davies

Large granule complexes are structures found in a small percentage of chicken erythrocyte nuclei when observed in ultra-thin sections in the electron microscope. They consist of an amorphous region associated with a number of large (approximately 30 min) granules. We have shown, by a novel use of phenylhydrazine to synchronize populations of chicken erythrocytes in vivo, that large granule complexes do not occur in the nuclei until the cells have reached one-third to one-half of their normal intravascular lifespan. The mature large granule complexes are formed by aggregation of pre-existing fibrillar, granular and amorphous material, and their presence is correlated with the presence of another ultrastructural feature of the nucleus, the so-called “filled cavities' in the chromatin. Digestion of ultra-thin sections of erythrocytes embedded in the hydrophilic resin glycol methacrylate (GMA) has shown that the major component of the amorphous region is a rather acidic protein that is not haemoglobin, the most abundant protein in the erythrocyte. The large granules also contain protein and, almost certainly, RNA. The problems encountered in reaching this conclusion have emphasized the lack of unambiguous cytochemical tests for use on ultra-thin sections. We have shown that the large granule complex differs in many respects from the nucleolus in the erythrocyte series, even though the two organelles have certain superficial similarities such as their overall dimensions and the presence of granular and fibrillar regions. The most likely function of the large granule complex is as a repository for material, including RNA, the processing of which has ceased in the inactivated erythrocyte nucleus.


1969 ◽  
Vol 4 (2) ◽  
pp. 499-525
Author(s):  
H. HARRIS ◽  
E. SIDEBOTTOM ◽  
D. M. GRACE ◽  
M. E. BRAMWELL

When the nucleus of a hen erythrocyte is introduced into the cytoplasm of a human or mouse cell in culture, it resumes the synthesis of RNA. The reactivated erythrocyte nucleus undergoes great enlargement, but it does not, for at least 2 or 3 days, develop nucleoli which can be discerned under the light microscope. During this period, the heterokaryon, although it may contain several active erythrocyte nuclei, does not synthesize any hen-specific surface antigens; and the hen-specific antigens introduced into the surface of the heterokaryon by the process of cell fusion are eliminated. But when, later, the erythrocyte nuclei do develop nucleoli, hen-specific antigens reappear on the surface of the heterokaryon and progressively accumulate. Before developing nucleoli, the erythrocyte nuclei synthesize little, if any, normal 28 S or 16 S RNA; but they do synthesize large amounts of the RNA which shows polydisperse sedimentation in conventional sucrose density gradients. Autoradiographic studies involving the use of a microbeam of ultraviolet light show, however, that this ‘polydisperse’ RNA is not transferred to the cytoplasm of the cell in detectable amounts so long as the erythrocyte nucleus lacks a definitive nucleolus. The inability of the erythrocyte nucleus at this stage to determine the synthesis of hen-specific surface antigens is thus attributable to the fact that it fails to transfer the RNA made on its chromosomes to the cytoplasm of the cell. When the erythrocyte nuclei develop nucleoli, however, the RNA which they make is transferred to the cytoplasm of the cell, and the synthesis of hen-specific surface antigens then begins. These experiments suggest that the nucleolus may play a decisive role in the transfer of information from nucleus to cytoplasm. The possible nature of this role is discussed.


1970 ◽  
Vol 176 (1044) ◽  
pp. 315-317 ◽  

When, under the influence of inactivated Sendai virus, the nucleus of a mature hen erythrocyte is introduced into the cytoplasm of a human or mouse tissue culture cell, it resumes the synthesis of RNA and DNA. This reactivation of the red cell nucleus in the heterokaryon is associated with a marked increase in its volume. There is a direct relation between the volume of the nucleus and the amount of RNA that it makes. The nuclear enlargement is not the consequence of increased RNA synthesis, or of DNA synthesis: enlargement is the primary event, and the increase in RNA synthesis is determined by it. During the process of reactivation, the erythrocyte nucleus shows a five- to six-fold increase in dry mass which takes place largely before the replication of DNA begins. This increase is due to the passage of cytoplasmic proteins into the erythrocyte nucleus. The physical properties of the deoxyribonucleoprotein complex in the erythrocyte nucleus change as the nucleus enlarges. The ability of the nuclear chromatin to bind acridine orange and other intercalating dyes increases four- to fivefold; and changes in the melting profile of the deoxyribonucleoprotein indicate that its structure is loosened. It appears that, as the nucleus expands, more of the chromatin passes from a condensed to a dispersed state and more of it is transcribed. At the concentrations used to induce cell fusion, Sendai virus is haemolytic and rapidly lyses the nucleated erythrocytes. Fusion then takes place between the other cells in the combination and erythrocyte ghosts. The erythrocyte nucleus is thus introduced into the cytoplasm of the recipient cell without any appreciable contribution of erythrocyte cytoplasm. The reactivation of the hen erythrocyte nucleus is therefore achieved by signals emanating from human or mouse cytoplasm.


1979 ◽  
Vol 37 (1) ◽  
pp. 97-107
Author(s):  
E. Jost ◽  
A. d'Arcy ◽  
S. Ely

When chick erythrocyte nuclei are introduced into the cytoplasm of mouse A9 cells by cell fusion, proteins present in a fraction of the mouse nuclear envelope begin to appear in the envelope of the chick erythrocyte. The protein uptake was examined using antisera raised in chickens against the 3 major polypeptides of the nuclear pore complex-fibrous lamina fraction from rat liver nuclei. In indirect immunofluorescence studies these antisera give a strong envelope-specific staining with various mammalian but not chicken cells. Eighteen hours after cell fusion the first murine antigens can be observed in the erythrocyte nucleus. Two days after cell fusion the vast majority of the erythrocyte nuclei in cell hybrids contain some antigen and by 3 days the fluorescence of the reactivated erythrocyte nuclei reaches a level comparable to that of the mouse A9 nuclei. The rate of appearance of fluorescence in the chick nuclei depends upon the ratio of A9 cytoplasm to chick nuclei. Antigen uptake by the erythrocyte envelope is inhibited when protein synthesis is blocked suggesting that synthesis of mouse antigen, rather than a redistribution, determines the velocity or erythrocyte envelope reactivation. The early uptake of nucleospecific protein into the reactivating chick erythrocyte may not require any alteration in the nuclear envelope.


1970 ◽  
Vol 7 (1) ◽  
pp. 1-3
Author(s):  
P. R. COOK

When a chick erythrocyte nucleus is introduced into the cytoplasm of a mutant mouse cell lacking inosinic acid pyrophosphorylase, synthesis of the enzyme is induced. The enzyme induced in this way has the characteristics of chick, not mouse, inosinic acid pyrophosphorylase.


1969 ◽  
Vol 4 (1) ◽  
pp. 71-87 ◽  
Author(s):  
L. BOLUND ◽  
N. R. RINGERTZ ◽  
H. HARRIS

When the nucleus of a chick erythrocyte is introduced into the cytoplasm of a HeLa cell it resumes the synthesis of RNA and DNA. This reactivation of the red cell nucleus is associated with an increase in volume and with changes in nuclear composition. These changes have now been studied by quantitative cytochemical techniques. During the process of reactivation the dry mass of the erythrocyte nucleus shows a marked increase which takes place largely before the replication of the DNA begins. Within 24 h of cell fusion, some erythrocyte nuclei already contain an increased amount of DNA, and 48 h after fusion many of them contain twice the normal diploid amount, thus indicating that they have replicated their DNA completely. The physical properties of the nuclear deoxyribonucleoprotein complex also change. The ability of the nuclear chromatin to bind acridine orange increases 4- to 5-fold well before the synthesis of DNA begins; and changes in the melting profile of the deoxyribonucleoprotein suggest that its structure is loosened. This view is also supported by the observation that the reactivity of the erythrocyte nuclei to the Feulgen stain is altered during the early stages of reactivation.


2006 ◽  
Vol 86 (6) ◽  
pp. 1477-1480 ◽  
Author(s):  
N.J. Smit ◽  
A.J. Davies

Blood films from a marine fish, the Cape Dory (Zeus capensis), trawled at depths between 149 and 389 m off the south and west coasts of South Africa, contained a new species of haemogregarine, Desseria zei sp. nov. The apicomplexan, found in 25/97 fish from the two regions, was generally intra-erythrocytic. Parasitaemia was usually low, but attained infection levels of 1/10 erythrocytes in one fish. The parasite stages were all gamonts and monomorphic, but likely varied in maturity; they were 3.3–4.5 μm wide by 14.7–18.3 μm long, curved with bluntly pointed ends, and existed singly within erythrocytes, or in pairs in the heavy infection. Their cytoplasm was deep blue, granular, and stained deeply at the anterior and sometimes, posterior extremities. Two or three vacuoles occurred in the cytoplasm between the anterior cap and the gamont nucleus, which was positioned in the posterior third of the parasite body. Gamonts lay close to the host cell nucleus, often curved around it. Distortion of host cells and host nucleus displacement occurred when single gamonts curved away from the host nucleus, or if they were paired. A few extracellular gamonts were observed, occasionally associated with the remnants of the erythrocyte nucleus.


1973 ◽  
Vol 59 (2) ◽  
pp. 304-317 ◽  
Author(s):  
Donald E. Olins ◽  
Everline B. Wright

Isolated chicken erythrocyte nuclei have been incubated with dilute concentrations of the bifunctional cross-linking agent glutaraldehyde (0–20 mM) in order to stabilize histone-histone interactions within the native nucleus. The kinetics of the disappearance of acid-soluble histones, free amino groups, and of individual histones have been observed to be pseudo first-order. Apparent first-order rate constants for the disappearance of individual histones correlate with the lysine mole percent of that fraction and follow the ranking, kapp: F1 > F2C > F2B ≥ F2A2, F2A1, F3. Histone polymers were observed to form very rapidly during the fixation reaction. Partial fractionation and amino acid analyses of these polymers support the view that they are composed principally of cross-linked (F2C)n molecules (where n = 2 to ∼8). The rate of glutaraldehyde reaction with free amino groups in histones is drastically reduced in solvents that promote chromatin decondensation (i.e., low ionic strengths in the absence of divalent cations) whereas the formation of cross-linked F2C polymers is less severely reduced. It is proposed that some F2C histones exist in close proximity within the isolated erythrocyte nucleus.


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