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Nitric oxide-dependent ribosomal RNA cleavage is associated with inhibition of ribosomal peptidyl transferase activity in ANA-1 murine macrophages.

Publication ,  Journal Article
Cai, CQ; Guo, H; Schroeder, RA; Punzalan, C; Kuo, PC
Published in: J Immunol
October 1, 2000

NO can regulate specific cellular functions by altering transcriptional programs and protein reactivity. With respect to global cellular processes, NO has also been demonstrated to inhibit total protein synthesis and cell proliferation. The underlying mechanisms are unknown. In a system of ANA-1 murine macrophages, iNOS expression and NO production were induced by exposure to endotoxin (LPS). In selected instances, cells were exposed to an exogenous NO donor, S-nitroso-N-acetylpenicillamine or a substrate inhibitor of NO synthesis. Cellular exposure to NO, from both endogenous and exogenous sources, was associated with a significant time-dependent decrease in total protein synthesis and cell proliferation. Gene transcription was unaltered. In parallel with decreased protein synthesis, cells exhibited a distinctive cleavage pattern of 28S and 18S rRNA that were the result of two distinct cuts in both 28S and 18S rRNA. Total levels of intact 28S rRNA, 18S rRNA, and the composite 60S ribosome were significantly decreased in the setting of cell exposure to NO. Finally, 60S ribosome-associated peptidyl transferase activity, a key enzyme for peptide chain elongation, was also significantly decreased. Our data suggest that NO-mediated cleavage of 28S and 18S rRNA results in decreased 60S ribosome associated peptidyl transferase activity and inhibition of total protein synthesis.

Duke Scholars

Published In

J Immunol

DOI

ISSN

0022-1767

Publication Date

October 1, 2000

Volume

165

Issue

7

Start / End Page

3978 / 3984

Location

United States

Related Subject Headings

  • Transcription, Genetic
  • Ribosomes
  • Ribosomal Proteins
  • RNA, Ribosomal
  • Proteins
  • Protein Synthesis Inhibitors
  • Protein Biosynthesis
  • Peptidyl Transferases
  • Nitric Oxide
  • Mice
 

Citation

APA
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Cai, C. Q., Guo, H., Schroeder, R. A., Punzalan, C., & Kuo, P. C. (2000). Nitric oxide-dependent ribosomal RNA cleavage is associated with inhibition of ribosomal peptidyl transferase activity in ANA-1 murine macrophages. J Immunol, 165(7), 3978–3984. https://doi.org/10.4049/jimmunol.165.7.3978
Cai, C. Q., H. Guo, R. A. Schroeder, C. Punzalan, and P. C. Kuo. “Nitric oxide-dependent ribosomal RNA cleavage is associated with inhibition of ribosomal peptidyl transferase activity in ANA-1 murine macrophages.J Immunol 165, no. 7 (October 1, 2000): 3978–84. https://doi.org/10.4049/jimmunol.165.7.3978.
Cai, C. Q., et al. “Nitric oxide-dependent ribosomal RNA cleavage is associated with inhibition of ribosomal peptidyl transferase activity in ANA-1 murine macrophages.J Immunol, vol. 165, no. 7, Oct. 2000, pp. 3978–84. Pubmed, doi:10.4049/jimmunol.165.7.3978.

Published In

J Immunol

DOI

ISSN

0022-1767

Publication Date

October 1, 2000

Volume

165

Issue

7

Start / End Page

3978 / 3984

Location

United States

Related Subject Headings

  • Transcription, Genetic
  • Ribosomes
  • Ribosomal Proteins
  • RNA, Ribosomal
  • Proteins
  • Protein Synthesis Inhibitors
  • Protein Biosynthesis
  • Peptidyl Transferases
  • Nitric Oxide
  • Mice