Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase

R. A. Casero, P. Celano, S. J. Ervin, N. B. Applegren, L. Wiest, Anthony Pegg

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

Spermidine/spermine N1 acetyltransferase (Spd/Spm acetyltransferase) is the rate-limiting enzyme in the catabolism of polyamines. This enzyme is highly inducible by several stimuli, including the natural polyamines and their structural analogues. To investigate the underlying mechanism responsible for the control of this enzyme a cDNA which codes for an active human Spd/Spm acetyltransferase has been isolated from a random primed cDNA library constructed from mRNA of a polyamine analogue treated large cell lung carcinoma line, NCI H157. The 972-base pair cDNA was identified using a 32-fold degenerate, 20-base oligomer probe to a 7-amino acid polypeptide sequence derived from the purified protein. The cDNA has a 513-base open reading frame that codes for a protein of 171 amino acids with a predicted molecular weight of 20,023. In vitro translation studies demonstrated the protein product of this cDNA to be a biologically active enzyme. The cDNA recognizes a 1.5-kilobase transcript in human cells which is highly induced in the human large cell lung carcinoma NCI H157 line following treatment with the polyamine analogue. The unusually high expression of Spd/Spm acetyltransferase mRNA by the NCI H157 cells in response to treatment does not appear to be a result of an amplification of the Spd/Spm acetyltransferase gene.

Original languageEnglish (US)
Pages (from-to)810-814
Number of pages5
JournalJournal of Biological Chemistry
Volume266
Issue number2
StatePublished - Feb 19 1991

Fingerprint

Acetyltransferases
Spermidine
Spermine
Polyamines
Complementary DNA
Clone Cells
Large Cell Carcinoma
Cells
Enzymes
Amino Acids
Lung
Messenger RNA
Proteins
Gene Library
Oligomers
Base Pairing
Open Reading Frames
Amplification
Amino Acid Sequence
Genes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Casero, R. A. ; Celano, P. ; Ervin, S. J. ; Applegren, N. B. ; Wiest, L. ; Pegg, Anthony. / Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 2. pp. 810-814.
@article{78902ce051a64fabad480bfbabe08211,
title = "Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase",
abstract = "Spermidine/spermine N1 acetyltransferase (Spd/Spm acetyltransferase) is the rate-limiting enzyme in the catabolism of polyamines. This enzyme is highly inducible by several stimuli, including the natural polyamines and their structural analogues. To investigate the underlying mechanism responsible for the control of this enzyme a cDNA which codes for an active human Spd/Spm acetyltransferase has been isolated from a random primed cDNA library constructed from mRNA of a polyamine analogue treated large cell lung carcinoma line, NCI H157. The 972-base pair cDNA was identified using a 32-fold degenerate, 20-base oligomer probe to a 7-amino acid polypeptide sequence derived from the purified protein. The cDNA has a 513-base open reading frame that codes for a protein of 171 amino acids with a predicted molecular weight of 20,023. In vitro translation studies demonstrated the protein product of this cDNA to be a biologically active enzyme. The cDNA recognizes a 1.5-kilobase transcript in human cells which is highly induced in the human large cell lung carcinoma NCI H157 line following treatment with the polyamine analogue. The unusually high expression of Spd/Spm acetyltransferase mRNA by the NCI H157 cells in response to treatment does not appear to be a result of an amplification of the Spd/Spm acetyltransferase gene.",
author = "Casero, {R. A.} and P. Celano and Ervin, {S. J.} and Applegren, {N. B.} and L. Wiest and Anthony Pegg",
year = "1991",
month = "2",
day = "19",
language = "English (US)",
volume = "266",
pages = "810--814",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "2",

}

Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. / Casero, R. A.; Celano, P.; Ervin, S. J.; Applegren, N. B.; Wiest, L.; Pegg, Anthony.

In: Journal of Biological Chemistry, Vol. 266, No. 2, 19.02.1991, p. 810-814.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase

AU - Casero, R. A.

AU - Celano, P.

AU - Ervin, S. J.

AU - Applegren, N. B.

AU - Wiest, L.

AU - Pegg, Anthony

PY - 1991/2/19

Y1 - 1991/2/19

N2 - Spermidine/spermine N1 acetyltransferase (Spd/Spm acetyltransferase) is the rate-limiting enzyme in the catabolism of polyamines. This enzyme is highly inducible by several stimuli, including the natural polyamines and their structural analogues. To investigate the underlying mechanism responsible for the control of this enzyme a cDNA which codes for an active human Spd/Spm acetyltransferase has been isolated from a random primed cDNA library constructed from mRNA of a polyamine analogue treated large cell lung carcinoma line, NCI H157. The 972-base pair cDNA was identified using a 32-fold degenerate, 20-base oligomer probe to a 7-amino acid polypeptide sequence derived from the purified protein. The cDNA has a 513-base open reading frame that codes for a protein of 171 amino acids with a predicted molecular weight of 20,023. In vitro translation studies demonstrated the protein product of this cDNA to be a biologically active enzyme. The cDNA recognizes a 1.5-kilobase transcript in human cells which is highly induced in the human large cell lung carcinoma NCI H157 line following treatment with the polyamine analogue. The unusually high expression of Spd/Spm acetyltransferase mRNA by the NCI H157 cells in response to treatment does not appear to be a result of an amplification of the Spd/Spm acetyltransferase gene.

AB - Spermidine/spermine N1 acetyltransferase (Spd/Spm acetyltransferase) is the rate-limiting enzyme in the catabolism of polyamines. This enzyme is highly inducible by several stimuli, including the natural polyamines and their structural analogues. To investigate the underlying mechanism responsible for the control of this enzyme a cDNA which codes for an active human Spd/Spm acetyltransferase has been isolated from a random primed cDNA library constructed from mRNA of a polyamine analogue treated large cell lung carcinoma line, NCI H157. The 972-base pair cDNA was identified using a 32-fold degenerate, 20-base oligomer probe to a 7-amino acid polypeptide sequence derived from the purified protein. The cDNA has a 513-base open reading frame that codes for a protein of 171 amino acids with a predicted molecular weight of 20,023. In vitro translation studies demonstrated the protein product of this cDNA to be a biologically active enzyme. The cDNA recognizes a 1.5-kilobase transcript in human cells which is highly induced in the human large cell lung carcinoma NCI H157 line following treatment with the polyamine analogue. The unusually high expression of Spd/Spm acetyltransferase mRNA by the NCI H157 cells in response to treatment does not appear to be a result of an amplification of the Spd/Spm acetyltransferase gene.

UR - http://www.scopus.com/inward/record.url?scp=0025977642&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025977642&partnerID=8YFLogxK

M3 - Article

VL - 266

SP - 810

EP - 814

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 2

ER -