Purification and properties of a neutral protease from rat liver chromatin

Chong, Ming Ta; Garrard, William T.; Bonner, James

doi:10.1021/bi00722a012

Cited by 97 publications

(27 citation statements)

References 27 publications

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“…Chong et al isolated a 200000-M, proteinase from a rat liver chromatin fraction prepared from the total homogenate [29]. Carter et al have reported a 25000-M, ptoteinase which is active in 2 M NaCl and 5 M urea [30].…”

Section: Discussionmentioning

confidence: 99%

Degradation of Newly Synthesized Ribosomal Proteins and Histones in Regenerating Rat Liver with and without Treatment with a Low Dose of Actinomycin D

Tsurugi

Ogata

1979

European Journal of Biochemistry

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The metabolism of newly synthesized ribosomal proteins in regenerating livers of rats pretreated with a low dose of actinomycin D which selectively inhibits rRNA synthesis, has been. investigated. After 15 min of labeling most newly synthesized proteins were found in the cell sap of regenerating livers of rats pretreated for 1 h with actinomycin D and disappeared from this fraction during a subsequent chase in the presence of cycloheximide. However, no proteinase activity for ribosomal proteins was detected in cell sap. After treatment in vivo with E-64, a thiol-proteinase inhibitor which inhibits the ribosomal protein-hydrolysing activities of nuclear and mitochondria1 plus lysosomal fractions of rat liver, a fraction of newly synthesized ribosomal proteins was found to accumulate in nuclei ofactinomycin-D-pretreated regenerating rat liver. These results may indicate that ribosomal proteins synthesized in the absence of rRNA synthesis accumulated in cell sap, and were then transported into nuclei where they were degraded by a proteinase sensitive to E-64. In the absence of actinomycin D pretreatment smaller amounts of ribosomal proteins accumulated in nuclei of regenerating livers of E-64-treated rats. Furthermore, histones (except histone H1) also accumulated in nuclei of regenerating livers of E-64-treated rats with and without actinomycin D pretreatment. Thus, these two kinds of proteins, especially histones, are synthesized in excess of nascent rRNA or DNA, and are degraded preferentially in nuclei in regenerating rat liver.

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Section: Discussionmentioning

confidence: 99%

Degradation of Newly Synthesized Ribosomal Proteins and Histones in Regenerating Rat Liver with and without Treatment with a Low Dose of Actinomycin D

Tsurugi

Ogata

1979

European Journal of Biochemistry

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“…Several investigators reported the protease which causes degradation of histone in isolated chromation34, 35,36) . But, Heinrich et al 37,38) have critically shown that this protease presents actually in the mitochondrial membrane and contaminates chromatin prepared from a total homogenate.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of 7, 12-Dimethylbenz(a)anthracene induced Mammary Tumorigenesis in Rats by a Synthetic Protease Inhibitor, N, N-Dimethylamino {p- (p -guanidinobenzoyloxy)} -benzilcarbonyloxy glycolate

Nakamura

1980

The Journal of Kansai Medical University

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“…However, this is unlikely because pepstatin, which specifically inhibits triiodothyronine-induced tadpole tail-fin regression (22) Present knowledge does not permit identification of the cellular processes that involve proteolytic steps specifically related to thyroid hormone action, but the following possibilities are worthy of consideration: (i) intracellular transport of T4 and its binding to nuclear receptors (25,26); and (ii) gene derepression. With respect to the latter, it is noteworthy that a chromatin-or nucleohistone-associated protease has been reported in many tissues and its possible role in gene derepression has been suggested (27)(28)(29)(30).…”

Section: Discussionmentioning

confidence: 99%

Antipain inhibits thyroxine-induced synthesis of carbamyl phosphate synthetase I in tadpole liver.

Mori¹,

Cohen²

1978

Proc. Natl. Acad. Sci. U.S.A.

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The increased activity of carbamyl phosphate synthetase I Icarbamoyl-phosphate synthase (ammonia); ATP: carbamate phosphotransferase (diphosphorylating), EC 2.7.2.5] in tadpole liver observed during thyroxine-induced metamorphosis was markedly inhibited by intraperitoneal injection of the microbial protease inhibitor antipain (0.1 ;&mol/g of body weight, twice daily). A somewhat less than maximal inhibition was seen when antipain was given only during the first 2 days of thyroxine treatment. On the other hand, little inhibition was observed when the inhibitor was given after the third or fourth day of thyroxine treatment. Antipain also inhibited thyroxineinduced increases of ornithine transcarbamylase (EC 2.1.3.3), arginase (EC 3.5.3.1), and succinate-cytochrome c reductase (EC 1.3.99.1) activities. Among other microbial protease inhibitors tested, chymostatin was nearly as effective as antipain, leupeptin was less effective, and pepstatin was ineffective. Analysis of the total liver protein and of the immunoprecipitate by sodium dodecyl sulfate/polyacrylamide gel electrophoresis showed that the inhibition was due to decreased amounts of the enzyme protein. Antipain had no significant effect on leucine incorporation into total protein of tadpole liver. These results indicate the involvement of a proteolytic step in the pretranscriptional events in thyroxine-stimulated enzyme induction.

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Purification and properties of a neutral protease from rat liver chromatin

Cited by 97 publications

References 27 publications

Degradation of Newly Synthesized Ribosomal Proteins and Histones in Regenerating Rat Liver with and without Treatment with a Low Dose of Actinomycin D

Degradation of Newly Synthesized Ribosomal Proteins and Histones in Regenerating Rat Liver with and without Treatment with a Low Dose of Actinomycin D

Inhibition of 7, 12-Dimethylbenz(a)anthracene induced Mammary Tumorigenesis in Rats by a Synthetic Protease Inhibitor, N, N-Dimethylamino {p- (p -guanidinobenzoyloxy)} -benzilcarbonyloxy glycolate

Antipain inhibits thyroxine-induced synthesis of carbamyl phosphate synthetase I in tadpole liver.

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