Sulfation of Flavonoids and Other Phenolic Dietary Compounds by the Human Cytosolic Sulfotransferases

Pai, Tongkun; Suiko, Masahito; Sakakibara, Yoichi; Liu, Ming‐Cheh

doi:10.1006/bbrc.2001.5316

Cited by 33 publications

(22 citation statements)

References 30 publications

(29 reference statements)

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“…For epicatechin, resveratrol, and chrysin, the V max /K m estimates were at least 1 order of magnitude greater with SULT1A1*1 than with SULT1E1. Specific activities for epicatechin and quercetin have been reported with purified recombinant SULTs in transformed BL21 (DE3) cells (Pai et al, 2001). At 100 M epicatechin, our mean specific activity value for sulfation by SULT1E1 (300 pmol/min/mg protein) compares very well with that published by Pai et al (351 pmol/min/mg protein).…”

Section: Discussionsupporting

confidence: 89%

“…SULT1A1*3, on the other hand, had a significantly lower K m than *1, and a comparable V max /K m estimate. Mean SULT1A1*1 activity toward 100 M epicatechin (1173 pmol/min/mg) compared well with a previously reported value (1364 pmol/min/mg) (Pai et al, 2001). Resveratrol sulfation by SULT1A1*1 and *3 allozymes showed comparable intrinsic clearance (V max /K m ) estimates despite significantly different V max estimates.…”

Section: Ung and Nagarsupporting

confidence: 81%

“…Dietary polyphenols have antioxidant properties and some inhibit angiogenesis and cancer cell proliferation in vitro (Brownson et al, 2002). Many polyphenols are conjugated in the human body to their sulfate and glucuronide conjugates, by the SULT and uridine diphosphoglucuronosyltransferase (UGT) enzyme superfamilies, respectively (Pai et al, 2001;Manach et al, 2004). Sulfation of flavonoids and nonflavonoid polyphenols by human cytosolic SULT isozymes has been described in previous reports (Pai et al, 2001;Harris et al, 2004).…”

mentioning

confidence: 93%

“…Many polyphenols are conjugated in the human body to their sulfate and glucuronide conjugates, by the SULT and uridine diphosphoglucuronosyltransferase (UGT) enzyme superfamilies, respectively (Pai et al, 2001;Manach et al, 2004). Sulfation of flavonoids and nonflavonoid polyphenols by human cytosolic SULT isozymes has been described in previous reports (Pai et al, 2001;Harris et al, 2004). It has been suggested that dietary polyphenols alter the bioavailability of endogenous estrogens by competing as substrates and/or inhibitors for human SULT1E1 and SULT1A1 isozymes, thus possibly contributing to variable breast cancer risk (Harris et al, 2004).…”

mentioning

confidence: 96%

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Variable Sulfation of Dietary Polyphenols by Recombinant Human Sulfotransferase (SULT) 1A1 Genetic Variants and SULT1E1

Ung¹,

Nagar²

2007

Drug Metab Dispos

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ABSTRACT:Human cytosolic sulfotransferases (SULTs) catalyze the sulfate conjugation of several important endo-and xenobiotics. Among the superfamily of SULT enzymes, SULT1A1 catalyzes the sulfation of small planar phenolic compounds, whereas SULT1E1 has a major role in estrogen conjugation. The human SULT1A1 gene has common single nucleotide polymorphisms that define three allozymes, SULT1A1*1, *2, and *3. The enzyme kinetics of SULT1A1 allozymes and SULT1E1 were characterized for the polyphenolic substrates apigenin, chrysin, epicatechin, quercetin, and resveratrol. Purified recombinant SULT proteins were generated in a baculoviral-insect cell system, and incubated in vitro with each substrate to determine catalytic activity. The effect of polyphenol sulfation was examined in mammalian cell lines stably expressing SULT1E1. For all polyphenols investigated, "normal-activity" SULT1A1*1 allozyme had significantly greater V max estimates than SULT1E1, and allele-specific differences in SULT1A1-mediated sulfation were observed. The polymorphic SULT1A1*2 allozyme exhibited low activity toward apigenin, epicatechin, and resveratrol. SULT1A1*1 and *3 acted as normal-activity allozymes for these substrates. Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1. These results suggest an important role for SULT isozymes and their pharmacogenetics in polyphenol disposition.

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Section: Discussionsupporting

confidence: 89%

Section: Ung and Nagarsupporting

confidence: 81%

mentioning

confidence: 93%

mentioning

confidence: 96%

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Variable Sulfation of Dietary Polyphenols by Recombinant Human Sulfotransferase (SULT) 1A1 Genetic Variants and SULT1E1

Ung¹,

Nagar²

2007

Drug Metab Dispos

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“…Because sulfates can be deconjugated in target tissues, circulating sulfate conjugates of phytochemicals may act as a source of tissue aglycones. SULT1A1 has shown high sulfating activity with a variety of flavonoids, isoflavonoids, anti-oxidants, and other phenolic dietary compounds, and SULT1A3 also has high activity with the flavonoids, but not with isoflavonoids [65,66]. Genetic variants in SULT genes with associated functional consequences on the translated protein have been identified.…”

Section: Sulfotransferasesmentioning

confidence: 99%

Interindividual differences in phytochemical metabolism and disposition

Lampe

Chang

2007

Seminars in Cancer Biology

109

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Many phytochemicals, the bioactive nonnutrient compounds found in plant foods, possess biologic effects associated with reduced risk of various diseases such as cancer. Genetic variation in pathways affecting absorption, metabolism, and distribution of phytochemicals is likely to influence exposure at the tissue level, thus modifying disease risk in individuals. Few studies have examined these genephytochemical interactions in humans. In this review, we discuss the sources of variation in metabolism and disposition of phytochemicals, and focus on two aspects of phytochemical handling that have received some attention: the impact of intestinal bacteria and genetically polymorphic phase II, conjugating enzymes.

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Extraction of Bioactive Molecules through Fermentation and Enzymatic Assisted Technologies

Larios-Cruz

Londoño-Hernández

Gómez-García

et al. 2019

High Value Fermentation Products

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Sulfation of Flavonoids and Other Phenolic Dietary Compounds by the Human Cytosolic Sulfotransferases

Cited by 33 publications

References 30 publications

Variable Sulfation of Dietary Polyphenols by Recombinant Human Sulfotransferase (SULT) 1A1 Genetic Variants and SULT1E1

Variable Sulfation of Dietary Polyphenols by Recombinant Human Sulfotransferase (SULT) 1A1 Genetic Variants and SULT1E1

Interindividual differences in phytochemical metabolism and disposition

Extraction of Bioactive Molecules through Fermentation and Enzymatic Assisted Technologies

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