Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome

Abstract Snyder–Robinson syndrome (SRS) results from mutations in spermine synthase (SMS), which converts the polyamine spermidine into spermine. Affecting primarily males, common manifestations of SRS include intellectual disability, osteoporosis, hypotonia, and seizures. Symptom management is the...

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Main Authors: Tracy Murray Stewart, Jackson R Foley, Cassandra E Holbert, Maxim Khomutov, Noushin Rastkari, Xianzun Tao, Alex R Khomutov, R Grace Zhai, Robert A Casero
Format: Article
Language:English
Published: Springer Nature 2023-09-01
Series:EMBO Molecular Medicine
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Online Access:https://doi.org/10.15252/emmm.202317833
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author Tracy Murray Stewart
Jackson R Foley
Cassandra E Holbert
Maxim Khomutov
Noushin Rastkari
Xianzun Tao
Alex R Khomutov
R Grace Zhai
Robert A Casero
author_facet Tracy Murray Stewart
Jackson R Foley
Cassandra E Holbert
Maxim Khomutov
Noushin Rastkari
Xianzun Tao
Alex R Khomutov
R Grace Zhai
Robert A Casero
author_sort Tracy Murray Stewart
collection DOAJ
description Abstract Snyder–Robinson syndrome (SRS) results from mutations in spermine synthase (SMS), which converts the polyamine spermidine into spermine. Affecting primarily males, common manifestations of SRS include intellectual disability, osteoporosis, hypotonia, and seizures. Symptom management is the only treatment. Reduced SMS activity causes spermidine accumulation while spermine levels are reduced. The resulting exaggerated spermidine:spermine ratio is a biochemical hallmark of SRS that tends to correlate with symptom severity. Our studies aim to pharmacologically manipulate polyamine metabolism to correct this imbalance as a therapeutic strategy for SRS. Here we report the repurposing of 2‐difluoromethylornithine (DFMO), an FDA‐approved inhibitor of polyamine biosynthesis, in rebalancing spermidine:spermine ratios in SRS patient cells. Mechanistic in vitro studies demonstrate that, while reducing spermidine biosynthesis, DFMO also stimulates the conversion of spermidine into spermine in hypomorphic SMS cells and induces uptake of exogenous spermine, altogether reducing the aberrant ratios. In a Drosophila SRS model characterized by reduced lifespan, DFMO improves longevity. As nearly all SRS patient mutations are hypomorphic, these studies form a strong foundation for translational studies with significant therapeutic potential.
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spelling doaj-art-5cc8bb3c21394af3a39b11fa46178f842025-08-20T04:02:55ZengSpringer NatureEMBO Molecular Medicine1757-46761757-46842023-09-01151111110.15252/emmm.202317833Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndromeTracy Murray Stewart0Jackson R Foley1Cassandra E Holbert2Maxim Khomutov3Noushin Rastkari4Xianzun Tao5Alex R Khomutov6R Grace Zhai7Robert A Casero8Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of MedicineSidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of MedicineSidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of MedicineEngelhardt Institute of Molecular Biology, Russian Academy of SciencesSidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of MedicineDepartment of Molecular and Cellular Pharmacology, University of Miami Miller School of MedicineEngelhardt Institute of Molecular Biology, Russian Academy of SciencesDepartment of Molecular and Cellular Pharmacology, University of Miami Miller School of MedicineSidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of MedicineAbstract Snyder–Robinson syndrome (SRS) results from mutations in spermine synthase (SMS), which converts the polyamine spermidine into spermine. Affecting primarily males, common manifestations of SRS include intellectual disability, osteoporosis, hypotonia, and seizures. Symptom management is the only treatment. Reduced SMS activity causes spermidine accumulation while spermine levels are reduced. The resulting exaggerated spermidine:spermine ratio is a biochemical hallmark of SRS that tends to correlate with symptom severity. Our studies aim to pharmacologically manipulate polyamine metabolism to correct this imbalance as a therapeutic strategy for SRS. Here we report the repurposing of 2‐difluoromethylornithine (DFMO), an FDA‐approved inhibitor of polyamine biosynthesis, in rebalancing spermidine:spermine ratios in SRS patient cells. Mechanistic in vitro studies demonstrate that, while reducing spermidine biosynthesis, DFMO also stimulates the conversion of spermidine into spermine in hypomorphic SMS cells and induces uptake of exogenous spermine, altogether reducing the aberrant ratios. In a Drosophila SRS model characterized by reduced lifespan, DFMO improves longevity. As nearly all SRS patient mutations are hypomorphic, these studies form a strong foundation for translational studies with significant therapeutic potential.https://doi.org/10.15252/emmm.202317833alpha‐methylated polyamine analogueeflornithineS‐adenosylmethionine decarboxylasespermidinespermine synthase
spellingShingle Tracy Murray Stewart
Jackson R Foley
Cassandra E Holbert
Maxim Khomutov
Noushin Rastkari
Xianzun Tao
Alex R Khomutov
R Grace Zhai
Robert A Casero
Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome
EMBO Molecular Medicine
alpha‐methylated polyamine analogue
eflornithine
S‐adenosylmethionine decarboxylase
spermidine
spermine synthase
title Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome
title_full Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome
title_fullStr Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome
title_full_unstemmed Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome
title_short Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder–Robinson syndrome
title_sort difluoromethylornithine rebalances aberrant polyamine ratios in snyder robinson syndrome
topic alpha‐methylated polyamine analogue
eflornithine
S‐adenosylmethionine decarboxylase
spermidine
spermine synthase
url https://doi.org/10.15252/emmm.202317833
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