Interethnic and interindividual variabilities of platelet sulfotransferases activity in Italians and Finns

Brittelli, A; Santi, Chiara De; Raunio, Hannu; Pelkonen, Olavi; Rossi, G. F.; Pacifici, Gian Maria

doi:10.1007/s002280050695

Cited by 12 publications

(4 citation statements)

References 12 publications

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“…It has been demonstrated that SULTs have substrate-dependent effects and they exhibit marked differences in tissue distribution as well as their sensitivity to thermal inactivation and inhibitor [51]. Moreover, previous studies have shown gender-specific differences for SULT activity [52–55]. Nowell et al .…”

Section: Discussionmentioning

confidence: 99%

Differential sensitivities of bladder cancer cell lines to resveratol are unrelated to its metabolic profile

Yang

et al. 2017

Oncotarget

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Resveratrol (RV) is a natural polyphenol compound with a wide range of activities, including inhibition of human bladder cancer (HBC) cell growth. Because RV is rapidly metabolized and has poor bioavailability, it is unclear whether the antitumor activity is due to RV or its metabolites. We therefore used liquid chromatography-mass spectroscopy, qRT-PCR, immunocytochemistry and western blotting to evaluate the metabolic profile and biotransformation of RV in the T24 and EJ HBC cell lines. Both T24 and EJ cells generated the same RV metabolite, RV monosulfate (RVS), and both exhibited upregulation of the RV-associated metabolic enzyme SULT1A1 (sulfotransferase). Despite these similarities, T24 cells were more sensitive to RV than EJ cells, yet T24 cells exhibited no sensitivity to an RVS mixture (84.13% RVS). Primary rat bladder epithelial cells showed no adverse effects when exposed to a therapeutic dose (100 μM) of RV. The differences in RV sensitivity between the two HBC cell lines did not reflect differences in the RV metabolic profile or SULT1A1 expression. Because RV exhibited stronger antitumor activity and better safety than RVS, we conclude that RV has significant therapeutic potential for HBC treatment, provided individual differences are considered during clinical research and application.

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Section: Discussionmentioning

confidence: 99%

Differential sensitivities of bladder cancer cell lines to resveratol are unrelated to its metabolic profile

Yang

et al. 2017

Oncotarget

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“…Similarly, thiopurine methyltransferase (TPMT) activities were lower in hepatic tissues of women compared with men (Szumlanski et al 1992), and levels of catechol-O-methyltransferase activity were also lower in women relative to men (Boudikova et al 1990). Finally, phenol sulfotransferase activity was more than 60 % lower in Finnish women than men (Brittelli et al 1999). …”

Section: Metabolismmentioning

confidence: 94%

Sex and Gender Differences in Infection and Treatments for Infectious Diseases

Klein

Roberts

2015

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This book provides an overview of the underlying sex-based and hormone-based differences in immunity, wound healing and pharmacokinetics, while also exploring how pregnancy affects immunity. The second part of the book shows, for the first time in a single volume, the growing number of infectious diseases for which sex and gender differences are noted, identifies common as well as distinct mechanisms mediating these differences and illustrates how responses to treatments might differ between the sexes. The awareness that males and females differ in their response to specific pathogens as well as to treatments for infectious diseases may yield sex-specific personalized treatments. This book will be of interest to basic scientists and clinicians in the fields of microbiology, immunology and pharmacology. Individuals working in academia, government and industry will also benefit from the information presented

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“…Ethnic variation in platelet enzymatic activity has also been reported. A study by Brittelli et al (1999) showed that SULT1A1 activity was significantly different between Spaniards and Finns, and in the case of the Finnish population, phenotype also varied by gender. Platelet SULT1A1 phenotype also tends to be higher in African Americans compared to Caucasians (Anderson et al, 1988;Nowell et al, 2000).…”

Section: Sult1a1mentioning

confidence: 99%

Pharmacogenetics of human cytosolic sulfotransferases

2006

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Cytosolic sulfotransferases (SULTs) are phase II detoxification enzymes that are involved in the biotransformation of a wide variety of structurally diverse endo-and xenobiotics, including many therapeutic agents and endogenous steroids. Single-nucleotide polymorphisms (SNPs) in SULTs have functional consequences on the translated protein. For the most part, these SNPs are fairly uncommon in the population, but some, most notably for SULT isoform 1A1, are commonly found and have been associated with cancer risk for a variety of tumor sites and also with response to therapeutic agents. SNPs in the hydroxysteroid sulfotransferase, SULT2A1, have been identified in African-American subjects and influence the ratio of plasma DHEA:DHEA-S. This modification could potentially influence cancer risk in steroidogenic tissues. SNPs in many SULTs are ethnically distributed, another factor that could influence SULT pharmacogenetics. Finally, genetic variation has also been identified in 3 0 -phosphoadenoside 5 0 -phosphosulfate synthetase (PAPPS), the enzymes responsible for producing the obligatory cosubstrate for all sulfotransferases. Taken together, this variability could substantially influence the disposition of drugs metabolized by SULTs. Elucidation of the basis and effect of variability in sulfation could greatly impact individualized therapy in the future.

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Interethnic and interindividual variabilities of platelet sulfotransferases activity in Italians and Finns

Cited by 12 publications

References 12 publications

Differential sensitivities of bladder cancer cell lines to resveratol are unrelated to its metabolic profile

Differential sensitivities of bladder cancer cell lines to resveratol are unrelated to its metabolic profile

Sex and Gender Differences in Infection and Treatments for Infectious Diseases

Pharmacogenetics of human cytosolic sulfotransferases

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