scholarly journals ANTIGEN-INDUCED CHANGES IN LYMPHOID CELL HISTONES

1965 ◽  
Vol 26 (1) ◽  
pp. 201-208 ◽  
Author(s):  
Maurice M. Black ◽  
Hudson R. Ansley

An acute effect of antigens on the nuclear histones of mouse thymocytes was investigated by means of cytophotometric measurements of thymocytes stained with ammoniacal-silver (A-S) and with fast green (FG). In addition, the DNA content was measured in terms of Feulgen staining. In terms of such staining it appeared that nuclei of control thymocytes contain a greater amount of nuclear histones and a higher histone/DNA ratio than do renal cell nuclei from the same animal. Within 1 hour after the injection of antigen the thymocyte nuclei appear to lose approximately 32 per cent and 20 per cent, respectively, of A-S and FG stainable nuclear proteins, while the Feulgen staining remains unchanged. Since the renal cell nuclei show no antigen-induced change in histone staining, the histone staining and histone/DNA ratios were found to be similar in the thymocytes and renal cells of the antigen-injected mice. The antigen-induced loss of thymocyte histones was also found to be associated with a change in the color of the A-S staining, from yellowish brown to black. This and other findings suggest that thymocyte nuclei contain an antigen-labile, lysine-rich histone. The implication of these observations in regard to the phenomenon of immunological competence is discussed and the need for continued investigation indicated.

1966 ◽  
Vol 19 (2) ◽  
pp. 233 ◽  
Author(s):  
RB Knox ◽  
IT Evans

Shoot apices of Lotium temulentum plants exposed to 1 long day were harvested at the beginning of the long day, and on each of the five following days. Longitudinal sections were stained for DNA (Feulgen), DNA and RNA (methyl greenpyronin or acridine orange fluorescence), or basic nuclear proteins (ammoniacal silver nitrate, fast green, or bromophenol blue, with or without acetylation or deamination).


1972 ◽  
Vol 25 (1) ◽  
pp. 175 ◽  
Author(s):  
AW Blackshaw ◽  
GW Salisbury

Bull spermatozoa were aged in vitro for periods of up to 9 days. Microspectro. photometric measurements were made of the nuclear DNA content of the sperm heads using ultraviolet absorption, acridine orange fluorescence, and Feulgen staining and of the nuclear histone content using fast green staining. The surface area of the sperm heads was calculated from linear measurements of head length and width.


1999 ◽  
Vol 7 (5-6) ◽  
pp. 463-469 ◽  
Author(s):  
J.T. Norman ◽  
C. Orphanides ◽  
P. Garcia ◽  
L.G. Fine

2000 ◽  
Vol 351 (3) ◽  
pp. 769-777 ◽  
Author(s):  
Georg T. WONDRAK ◽  
Daniel CERVANTES-LAUREAN ◽  
Elaine L. JACOBSON ◽  
Myron K. JACOBSON

Non-enzymic damage to nuclear proteins has potentially severe consequences for the maintenance of genomic integrity. Introduction of carbonyl groups into histones in vivo and in vitro was assessed by Western blot immunoassay and reductive incorporation of tritium from radiolabelled NaBH4 (sodium borohydride). Histone H1 extracted from bovine thymus, liver and spleen was found to contain significantly elevated amounts of protein-bound carbonyl groups as compared with core histones. The carbonyl content of nuclear proteins of rat pheochromocytoma cells (PC12 cells) was not greatly increased following oxidative stress induced by H2O2, but was significantly increased following alkylating stress induced by N-methyl-N´-nitro-N-nitrosoguanidine or by combined oxidative and alkylating stress. Free ADP-ribose, a reducing sugar generated in the nucleus in proportion to DNA strand breaks, was shown to be a potent histone H1 carbonylating agent in isolated PC12 cell nuclei. Studies of the mechanism of histone H1 modification by ADP-ribose indicate that carbonylation involves formation of a stable acyclic ketoamine. Our results demonstrate preferential histone H1 carbonylation in vivo, with potentially important consequences for chromatin structure and function.


Development ◽  
1987 ◽  
Vol 101 (4) ◽  
pp. 829-846 ◽  
Author(s):  
C. Dreyer

Oocyte nuclear proteins of Xenopus are distributed into the cytoplasm of the maturing egg after germinal vesicle breakdown. Later they are found in all cell nuclei of the embryo. At early stages of development, different nuclear proteins behave differently. A class of ‘early shifting’ antigens is accumulated by pronuclei and cleavage nuclei, whereas others appear to be excluded from the nuclei at early stages but are shifted into the nuclei at blastula or during and after gastrulation. Accumulation of ‘late-shifting’ nuclear antigens is a gradual process and occurs during a period characteristic of each protein. Multiple artificial pronuclei can be formed after injection of sperm nuclei, erythrocyte nuclei or pure lambda-DNA into unfertilized eggs. The artificial pronuclei accumulate early- but not late-shifting proteins. Early-migrating proteins rapidly accumulate into the germinal vesicle after de novo synthesis in the oocyte, indicating that the efficiency of translocation into nuclei is an intrinsic property of each protein. Artificial extension of the length of the cell cycle before midblastula transition does not lead to accumulation of the late-shifting nuclear antigens investigated.


1986 ◽  
Vol 12 (6) ◽  
pp. 426-431 ◽  
Author(s):  
G. Klöppel ◽  
W.T. Knöfel ◽  
H. Baisch ◽  
U. Otto

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