Evidence map›Paper›PMID 19589128›Full record

ReviewThe Biochemical journal2009

Polyamine catabolism and disease.

Robert A Casero, Anthony E Pegg

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers.

0numbers the graph read from it
0cells of the map it votes in
195citing papers in PubMed
9.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

195 citing papers in PubMed, 367 citations in OpenAlex.

  1. Trial
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  3. Functional Characterization of the P-Type ATPases ATP13A3 and ATP13A4 as Plasma Membrane Polyamine Transporters.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
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  8. The Role of Selected Bacteria in Breast Cancer Initiation and Development.International journal of molecular sciences · 2026
    Review
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135 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Robert A CaseroDepartment of Oncology, Johns Hopkins University School of Medicine and the Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD 21231, USA. rcasero@jhmi.edu
Anthony E Pegg
Johns Hopkins University · USPennsylvania State University · US

Funding

Spermine N1-Acetylase Induction in Lung CancersR01CA051085 · NCI · JOHNS HOPKINS UNIVERSITY · PI CASERO, ROBERT A. · 1990 to 2013
$4.7M
The Role of Polyamine Oxidase in Antitumor Drug ResponseR01CA098454 · NCI · JOHNS HOPKINS UNIVERSITY · PI CASERO, ROBERT A. · 2003 to 2013
$2.9M
MAMMALIAN POLYAMINE METABOLISMR01CA018138 · NCI · UNIVERSITY OF VIRGINIA · PI FEITH, DAVID J. · 1985 to 2015
$2.8M
MAMMALIAN AMINOPROPYLTRANSFERASESR01GM026290 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI PEGG, ANTHONY E · 1985 to 2009
$2.3M
MAMMALIAN POLYAMINE METABOLISMR37CA018138 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI PEGG, ANTHONY E · 1988 to 2004
$1.7M
NCI NIH HHS CA018138NCI NIH HHS CA51085NCI NIH HHS CA98454NCI NIH HHS R01 CA018138NCI NIH HHS R01 CA051085NCI NIH HHS R01 CA098454NCI NIH HHS R37 CA018138NIGMS NIH HHS GM26290NIGMS NIH HHS R01 GM026290
6 · The paper itself

Abstract

In addition to polyamine homoeostasis, it has become increasingly clear that polyamine catabolism can play a dominant role in drug response, apoptosis and the response to stressful stimuli, and contribute to the aetiology of several pathological states, including cancer. The highly inducible enzymes SSAT (spermidine/spermine N1-acetyltransferase) and SMO (spermine oxidase) and the generally constitutively expressed APAO (N1-acetylpolyamine oxidase) appear to play critical roles in many normal and disease processes. The dysregulation of polyamine catabolism frequently accompanies several disease states and suggests that such dysregulation may both provide useful insight into disease mechanism and provide unique druggable targets that can be exploited for therapeutic benefit. Each of these enzymes has the potential to alter polyamine homoeostasis in response to multiple cell signals and the two oxidases produce the reactive oxygen species H2O2 and aldehydes, each with the potential to produce pathological states. The activity of SSAT provides substrates for APAO or substrates for the polyamine exporter, thus reducing the intracellular polyamine concentration, the net effect of which depends on the magnitude and rate of any increase in SSAT. SSAT may also influence cellular metabolism via interaction with other proteins and by perturbing the content of acetyl-CoA and ATP. The goal of the present review is to cover those aspects of polyamine catabolism that have an impact on disease aetiology or treatment and to provide a solid background in this ever more exciting aspect of polyamine biology.

Indexed as

AcetyltransferasesAnimalsDiamine N-AcetyltransferaseDiseaseHumansOxidoreductases Acting on CH-NH Group DonorsPolyamine OxidasePolyaminesTherapeuticsAcetyltransferasesDiamine N-AcetyltransferaseOxidoreductases Acting on CH-NH Group DonorsPolyamine OxidasePolyamines

Identifiers

PMID19589128
PMCPMC2756025
OpenAlexW2147621980

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.