Immunohistochemical Detection of Phenol Sulfotransferase‐Containing Neurons in Human Brain

Zou, Jianyan; Pentney, Roberta J.; Roth, Jerome A.

doi:10.1111/j.1471-4159.1990.tb03119.x

Cited by 32 publications

(19 citation statements)

References 11 publications

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“…The reaction was terminated by adding 100 l of 0.25 M Tris-HCL (pH 8.7). SULT1A1-catalyzed liberation of p-nitrophenyl from p-nitrophenyl sulfate was measured by determining absorbance at 405 nm using a SpectraMax model 250 spectrophotometric plate reader (Molecular Devices) and quantified using the extinction coefficient (18,200 cm Ϫ1 M Ϫ1 ), which directly correlates with the concentration of 2-naphthylsulfate formed (34). Assays were performed in triplicate along with controls that did not contain 2-naphthol.…”

Section: Methodsmentioning

confidence: 99%

Association of SULT1A1 Phenotype and Genotype with Prostate Cancer Risk in African-Americans and Caucasians

Nowell

Ratnasinghe

Ambrosone

et al. 2004

Cancer Epidemiology, Biomarkers &Amp; Prevention

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Exposure to heterocyclic amines may increase prostate cancer risk. Human sulfotransferase 1A1 (SULT1A1) is involved in the bioactivation of some dietary procarcinogens, including the N-hydroxy metabolite of the food-borne heterocyclic amine, 2-amino-1-methyl-6-phenylimidazo(4,5-b) pyridine. This study compares a polymorphism in the SULT1A1 gene, SULT1A1 enzyme activity, meat consumption, and the risk of prostate cancer in a population based case-control study. Prostate cancer patients (n ‫؍‬ 464) and control individuals (n ‫؍‬ 459), frequency matched on age and ethnicity, provided informed consent, answered a survey, and provided a blood sample. Platelets were isolated for phenotype analysis, and DNA was isolated from lymphocytes for genotype determination. Meat consumption was assessed using a dietary questionnaire. Caucasians homozygous for the SULT1A1*1 high activity allele were at increased risk for prostate cancer [odds ratio (OR), 1.68; 95% confidence interval (CI), 1.05-2.68] compared with individuals homozygous for the low-activity allele. The association between SULT1A1 genotype and prostate cancer risk in African-Americans did not reach significance (OR, 1.60; 95% CI, 0.46 -5.62). When SULT1A1 activity was considered, there was a strong association between increased SULT1A1 activity and prostate cancer risk in Caucasians (OR, 3.04; 95% CI, 1.8 -5.1 and OR, 4.96; 95% CI, 3.0 -8.3, for the second and third tertiles of SULT1A1 activity, respectively) compared with individuals in the low enzyme activity tertile. A similar association was also found in AfricanAmerican patients, with ORs of 6.7 and 9.6 for the second and third tertiles of SULT1A1 activity (95% CI, 2.1-21.3 and 2.9 -31.3, respectively). When consumption of well-done meat was considered, there was increased risk of prostate cancer (OR, 1.42; 95% CI, 1.01-1.99 and OR, 1.68; 95% CI, 1.20 -2.36 for the second and third tertiles, respectively). When SULT1A1 activity was stratified by tertiles of meat consumption, there was greater risk of prostate cancer in the highest tertile of meat consumption. These results indicate that variations in SULT1A1 activity contributes to prostate cancer risk and the magnitude of the association may differ by ethnicity and be modified by meat consumption.

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Section: Methodsmentioning

confidence: 99%

Association of SULT1A1 Phenotype and Genotype with Prostate Cancer Risk in African-Americans and Caucasians

Nowell

Ratnasinghe

Ambrosone

et al. 2004

Cancer Epidemiology, Biomarkers &Amp; Prevention

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“…Several SULTs have been identified in human brain [3,5,6] ; however, these SULTs are also found at high levels in other tissues. The phenol SULTs, P-PST-1 (ST1A1) and M-PST (ST1A3), which have been localized in brain [4,6], are also expressed in the liver and\or intestine at high levels. Hydroxysteroid SULTs identified in rat brain [19,20] are also expressed in liver [21,22].…”

Section: Discussionmentioning

confidence: 99%

“…Several of the SULTs have been identified in human brain tissues [3][4][5], and the phenol SULTs have been immunolocalized in neurons in several different brain regions [6].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain

Falany

Xie

Wang

et al. 2000

Biochemical Journal

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The sulphotransferase (SULT) gene family is involved with the conjugation of many small drugs, xenobiotics and endogenous compounds. In this report, we describe the cloning and expression of novel cDNAs from human and rat brain, which are structurally related to the SULTs. These cDNAs have been termed ‘brain sulphotransferase-like’ (BR-STL), because of their similarity to the SULTs and their selective expression in brain tissue. The proteins encoded by the human and rat BR-STL cDNAs (hBR-STL-1 and rBR-STL cDNA respectively), denoted as hBR-STL and rBR-STL, are 98% identical and 99% similar in sequence. The hBR-STL-1 cDNA contains an 852-nt open reading frame encoding a 284-amino-acid protein with a calculated molecular mass of 33083 Da. Northern-blot analyses of RNA isolated from eight human tissues indicate that the hBR-STL message is selectively expressed in brain. Characterization of different brain regions showed that message levels were highest in cortical brain regions. rBR-STL message levels were relatively low in brains of 1-day-old male and female rats, but increased to adult levels in RNA from 7-day-old rats, and remained at that level in adult animals. The hBR-STL and rBR-STL cDNAs were expressed in both Escherichia coli and Sf9 insect cells in the presence or absence of an N-terminal histidine-affinity tag (His-tag). Polyclonal antibodies were raised in chickens against purified His-tagged hBR-STL, and were used to detect the presence of rBR-STL in adult male and female rat brain cytosol. The high degree of sequence conservation, and the selective localization of the BR-STL message in brain, suggest an important function in the central nervous system.

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“…A third, less characterized subfamily of brain-specific SULT has also been described (Liyou et al, 2003). SULT enzymes have a widespread tissue distribution and are expressed in the liver, lung, brain, skin, platelets, breast, kidney and gastrointestinal tissue (Cappiello et al, 1989;Zou et al, 1990;Kudlacek et al, 1995;Falany and Falany, 1996;Hume et al, 1996). The biological function of SULT enzymes is to catalyse the transfer of the sulfonyl group from 3 0 -phosphoadenosine 5 0 -phosphosulfate (PAPS) to the hydroxyl, sulfhydryl, amino or N-oxide groups of various substrates.…”

Section: Introductionmentioning

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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Immunohistochemical Detection of Phenol Sulfotransferase‐Containing Neurons in Human Brain

Cited by 32 publications

References 11 publications

Association of SULT1A1 Phenotype and Genotype with Prostate Cancer Risk in African-Americans and Caucasians

Association of SULT1A1 Phenotype and Genotype with Prostate Cancer Risk in African-Americans and Caucasians

Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain

Pharmacogenetics of human cytosolic sulfotransferases

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