Inhibition of ornithine decarboxylase and S-adenosylmethionine decarboxylase synthesis by antisense oligodeoxynucleotides

Rentala Madhubala, Anthony E. Pegg

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Oligodeoxynucleotides 18 nucleotides in length having sequences complementary to regions spanning the initiation codon regions of ornithine decarboyxlase or S-adenosylmethionine decarboxylase mRNAs were tested for their ability to inhibit translation of these mRNAs. In reticulocyte lysates, a strong and dose dependent reduction of ornithine decarboyxlase synthesis in response to mRNA from D-R L1210 cells was brought about by 5′-AAAGCT GCTCATGGTTCT-3′ which is complementary to the sequence from - 6 to + 12 of the mRNA sequence but there was no inhibition by 5′-TGCAGCTTCCATCACCGT-3′. Conversely, the latter oligodeoxynucleotide which is complementary to the sequence from - 6 to + 12 of the mRNA of S-adenosyl methionine decarboxylase was a strong inhibitor of the synthesis of this enzyme in response to rat prostate mRNA and the antisense sequence from ornithine decarboxylase had no effect. The translation of ornithine decarboxylase mRNA in a wheat germ system was inhibited by the antisense oligodeoxynucleotide at much lower concentration than those needed in the reticulocyte lysate suggesting that degradation of the hybrid by ribonuclease H may be an important factor in this inhibition. These results indicate that such oligonucleotides may be useful to regulate cellular polyamine levels and as probes to study control of mRNA translation.

Original languageEnglish (US)
Pages (from-to)191-195
Number of pages5
JournalMolecular and Cellular Biochemistry
Volume116
Issue number2
DOIs
StatePublished - Sep 1 1992

Fingerprint

Adenosylmethionine Decarboxylase
Ornithine Decarboxylase
Oligodeoxyribonucleotides
Messenger RNA
Ornithine
Reticulocytes
Protein Biosynthesis
Ribonuclease H
Initiator Codon
Polyamines
Enzyme Inhibitors
Oligonucleotides
Triticum
Prostate
Nucleotides
Rats
Degradation

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Cite this

@article{1479eb5ee7214623be5e9405cf86007a,
title = "Inhibition of ornithine decarboxylase and S-adenosylmethionine decarboxylase synthesis by antisense oligodeoxynucleotides",
abstract = "Oligodeoxynucleotides 18 nucleotides in length having sequences complementary to regions spanning the initiation codon regions of ornithine decarboyxlase or S-adenosylmethionine decarboxylase mRNAs were tested for their ability to inhibit translation of these mRNAs. In reticulocyte lysates, a strong and dose dependent reduction of ornithine decarboyxlase synthesis in response to mRNA from D-R L1210 cells was brought about by 5′-AAAGCT GCTCATGGTTCT-3′ which is complementary to the sequence from - 6 to + 12 of the mRNA sequence but there was no inhibition by 5′-TGCAGCTTCCATCACCGT-3′. Conversely, the latter oligodeoxynucleotide which is complementary to the sequence from - 6 to + 12 of the mRNA of S-adenosyl methionine decarboxylase was a strong inhibitor of the synthesis of this enzyme in response to rat prostate mRNA and the antisense sequence from ornithine decarboxylase had no effect. The translation of ornithine decarboxylase mRNA in a wheat germ system was inhibited by the antisense oligodeoxynucleotide at much lower concentration than those needed in the reticulocyte lysate suggesting that degradation of the hybrid by ribonuclease H may be an important factor in this inhibition. These results indicate that such oligonucleotides may be useful to regulate cellular polyamine levels and as probes to study control of mRNA translation.",
author = "Rentala Madhubala and Pegg, {Anthony E.}",
year = "1992",
month = "9",
day = "1",
doi = "10.1007/BF00299398",
language = "English (US)",
volume = "116",
pages = "191--195",
journal = "Molecular and Cellular Biochemistry",
issn = "0300-8177",
publisher = "Springer Netherlands",
number = "2",

}

Inhibition of ornithine decarboxylase and S-adenosylmethionine decarboxylase synthesis by antisense oligodeoxynucleotides. / Madhubala, Rentala; Pegg, Anthony E.

In: Molecular and Cellular Biochemistry, Vol. 116, No. 2, 01.09.1992, p. 191-195.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Inhibition of ornithine decarboxylase and S-adenosylmethionine decarboxylase synthesis by antisense oligodeoxynucleotides

AU - Madhubala, Rentala

AU - Pegg, Anthony E.

PY - 1992/9/1

Y1 - 1992/9/1

N2 - Oligodeoxynucleotides 18 nucleotides in length having sequences complementary to regions spanning the initiation codon regions of ornithine decarboyxlase or S-adenosylmethionine decarboxylase mRNAs were tested for their ability to inhibit translation of these mRNAs. In reticulocyte lysates, a strong and dose dependent reduction of ornithine decarboyxlase synthesis in response to mRNA from D-R L1210 cells was brought about by 5′-AAAGCT GCTCATGGTTCT-3′ which is complementary to the sequence from - 6 to + 12 of the mRNA sequence but there was no inhibition by 5′-TGCAGCTTCCATCACCGT-3′. Conversely, the latter oligodeoxynucleotide which is complementary to the sequence from - 6 to + 12 of the mRNA of S-adenosyl methionine decarboxylase was a strong inhibitor of the synthesis of this enzyme in response to rat prostate mRNA and the antisense sequence from ornithine decarboxylase had no effect. The translation of ornithine decarboxylase mRNA in a wheat germ system was inhibited by the antisense oligodeoxynucleotide at much lower concentration than those needed in the reticulocyte lysate suggesting that degradation of the hybrid by ribonuclease H may be an important factor in this inhibition. These results indicate that such oligonucleotides may be useful to regulate cellular polyamine levels and as probes to study control of mRNA translation.

AB - Oligodeoxynucleotides 18 nucleotides in length having sequences complementary to regions spanning the initiation codon regions of ornithine decarboyxlase or S-adenosylmethionine decarboxylase mRNAs were tested for their ability to inhibit translation of these mRNAs. In reticulocyte lysates, a strong and dose dependent reduction of ornithine decarboyxlase synthesis in response to mRNA from D-R L1210 cells was brought about by 5′-AAAGCT GCTCATGGTTCT-3′ which is complementary to the sequence from - 6 to + 12 of the mRNA sequence but there was no inhibition by 5′-TGCAGCTTCCATCACCGT-3′. Conversely, the latter oligodeoxynucleotide which is complementary to the sequence from - 6 to + 12 of the mRNA of S-adenosyl methionine decarboxylase was a strong inhibitor of the synthesis of this enzyme in response to rat prostate mRNA and the antisense sequence from ornithine decarboxylase had no effect. The translation of ornithine decarboxylase mRNA in a wheat germ system was inhibited by the antisense oligodeoxynucleotide at much lower concentration than those needed in the reticulocyte lysate suggesting that degradation of the hybrid by ribonuclease H may be an important factor in this inhibition. These results indicate that such oligonucleotides may be useful to regulate cellular polyamine levels and as probes to study control of mRNA translation.

UR - http://www.scopus.com/inward/record.url?scp=0027090443&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027090443&partnerID=8YFLogxK

U2 - 10.1007/BF00299398

DO - 10.1007/BF00299398

M3 - Article

C2 - 1338119

AN - SCOPUS:0027090443

VL - 116

SP - 191

EP - 195

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

SN - 0300-8177

IS - 2

ER -