Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase

Lei Xiao; Paul Celano; Amy R. Mank; Anthony E. Pegg; Robert A. Casero

doi:10.1016/0006-291X(91)91385-P

Characterization of a full-length cDNA which codes for the human spermidine/spermine N¹-acetyltransferase

Lei Xiao, Paul Celano, Amy R. Mank, Anthony E. Pegg, Robert A. Casero

School of Medicine

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

Abstract

Spermidine/spermine N¹-acetyltransferase is the rate-limiting enzyme in the catabolism of cellular polyamines. Using a combination of cDNA library screening and anchored PCR methodologies, a full length cDNA designated AP3 F7 corresponding to the human SSAT was cloned using RNA from the human large cell undifferentiated lung carcinoma line NCI H157. The resulting cDNA clone is 1,060 base pairs with a 513 base open reading frame coding for a 171 amino acid protein, with a predicted subunit molecular weight of 20,023. The 5′ non-coding region of AP3 F7 is 165 bases and the 3′ untranslated region is 382 bases with a polyadenylation site 20 bases 5′ to the poly(A) tail. This full length cDNA should be an aid in the study of the regulation of spermidine/spermine N¹-acetyltransferase expression and the significance of the acetyltransferase in polyamine metabolism.

Original language	English (US)
Pages (from-to)	407-415
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	179
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(91)91385-P
State	Published - Aug 30 1991

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(91)91385-P

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title = "Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase",

abstract = "Spermidine/spermine N1-acetyltransferase is the rate-limiting enzyme in the catabolism of cellular polyamines. Using a combination of cDNA library screening and anchored PCR methodologies, a full length cDNA designated AP3 F7 corresponding to the human SSAT was cloned using RNA from the human large cell undifferentiated lung carcinoma line NCI H157. The resulting cDNA clone is 1,060 base pairs with a 513 base open reading frame coding for a 171 amino acid protein, with a predicted subunit molecular weight of 20,023. The 5′ non-coding region of AP3 F7 is 165 bases and the 3′ untranslated region is 382 bases with a polyadenylation site 20 bases 5′ to the poly(A) tail. This full length cDNA should be an aid in the study of the regulation of spermidine/spermine N1-acetyltransferase expression and the significance of the acetyltransferase in polyamine metabolism.",

author = "Lei Xiao and Paul Celano and Mank, {Amy R.} and Pegg, {Anthony E.} and Casero, {Robert A.}",

note = "Funding Information: ACKNOWLEDGMENTS: The authors wish to thank Drs. Stephen B. Baylin and Barry D. Nelkin for helpful discussions, Jeffrey Smith for expert technicial assistance and Tammy Hess and Sandra Lund for their skilled administrative assistance. This work was supported by NIH Grants CA51085, CA47492, GM26290, and The S. McDonnell Foundation.",

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doi = "10.1016/0006-291X(91)91385-P",

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AU - Celano, Paul

AU - Mank, Amy R.

AU - Pegg, Anthony E.

AU - Casero, Robert A.

N1 - Funding Information: ACKNOWLEDGMENTS: The authors wish to thank Drs. Stephen B. Baylin and Barry D. Nelkin for helpful discussions, Jeffrey Smith for expert technicial assistance and Tammy Hess and Sandra Lund for their skilled administrative assistance. This work was supported by NIH Grants CA51085, CA47492, GM26290, and The S. McDonnell Foundation.

PY - 1991/8/30

Y1 - 1991/8/30

N2 - Spermidine/spermine N1-acetyltransferase is the rate-limiting enzyme in the catabolism of cellular polyamines. Using a combination of cDNA library screening and anchored PCR methodologies, a full length cDNA designated AP3 F7 corresponding to the human SSAT was cloned using RNA from the human large cell undifferentiated lung carcinoma line NCI H157. The resulting cDNA clone is 1,060 base pairs with a 513 base open reading frame coding for a 171 amino acid protein, with a predicted subunit molecular weight of 20,023. The 5′ non-coding region of AP3 F7 is 165 bases and the 3′ untranslated region is 382 bases with a polyadenylation site 20 bases 5′ to the poly(A) tail. This full length cDNA should be an aid in the study of the regulation of spermidine/spermine N1-acetyltransferase expression and the significance of the acetyltransferase in polyamine metabolism.

AB - Spermidine/spermine N1-acetyltransferase is the rate-limiting enzyme in the catabolism of cellular polyamines. Using a combination of cDNA library screening and anchored PCR methodologies, a full length cDNA designated AP3 F7 corresponding to the human SSAT was cloned using RNA from the human large cell undifferentiated lung carcinoma line NCI H157. The resulting cDNA clone is 1,060 base pairs with a 513 base open reading frame coding for a 171 amino acid protein, with a predicted subunit molecular weight of 20,023. The 5′ non-coding region of AP3 F7 is 165 bases and the 3′ untranslated region is 382 bases with a polyadenylation site 20 bases 5′ to the poly(A) tail. This full length cDNA should be an aid in the study of the regulation of spermidine/spermine N1-acetyltransferase expression and the significance of the acetyltransferase in polyamine metabolism.

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Characterization of a full-length cDNA which codes for the human spermidine/spermine N¹-acetyltransferase

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