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EC number: 249-616-3 | CAS number: 29420-49-3
- Life Cycle description
- Uses advised against
- Endpoint summary
- Appearance / physical state / colour
- Melting point / freezing point
- Boiling point
- Density
- Particle size distribution (Granulometry)
- Vapour pressure
- Partition coefficient
- Water solubility
- Solubility in organic solvents / fat solubility
- Surface tension
- Flash point
- Auto flammability
- Flammability
- Explosiveness
- Oxidising properties
- Oxidation reduction potential
- Stability in organic solvents and identity of relevant degradation products
- Storage stability and reactivity towards container material
- Stability: thermal, sunlight, metals
- pH
- Dissociation constant
- Viscosity
- Additional physico-chemical information
- Additional physico-chemical properties of nanomaterials
- Nanomaterial agglomeration / aggregation
- Nanomaterial crystalline phase
- Nanomaterial crystallite and grain size
- Nanomaterial aspect ratio / shape
- Nanomaterial specific surface area
- Nanomaterial Zeta potential
- Nanomaterial surface chemistry
- Nanomaterial dustiness
- Nanomaterial porosity
- Nanomaterial pour density
- Nanomaterial photocatalytic activity
- Nanomaterial radical formation potential
- Nanomaterial catalytic activity
- Endpoint summary
- Stability
- Biodegradation
- Bioaccumulation
- Transport and distribution
- Environmental data
- Additional information on environmental fate and behaviour
- Ecotoxicological Summary
- Aquatic toxicity
- Endpoint summary
- Short-term toxicity to fish
- Long-term toxicity to fish
- Short-term toxicity to aquatic invertebrates
- Long-term toxicity to aquatic invertebrates
- Toxicity to aquatic algae and cyanobacteria
- Toxicity to aquatic plants other than algae
- Toxicity to microorganisms
- Endocrine disrupter testing in aquatic vertebrates – in vivo
- Toxicity to other aquatic organisms
- Sediment toxicity
- Terrestrial toxicity
- Biological effects monitoring
- Biotransformation and kinetics
- Additional ecotoxological information
- Toxicological Summary
- Toxicokinetics, metabolism and distribution
- Acute Toxicity
- Irritation / corrosion
- Sensitisation
- Repeated dose toxicity
- Genetic toxicity
- Carcinogenicity
- Toxicity to reproduction
- Specific investigations
- Exposure related observations in humans
- Toxic effects on livestock and pets
- Additional toxicological data
Specific investigations: other studies
Administrative data
- Endpoint:
- mechanistic studies
- Type of information:
- experimental study
- Adequacy of study:
- supporting study
- Study period:
- 2011
- Reliability:
- 3 (not reliable)
- Rationale for reliability incl. deficiencies:
- significant methodological deficiencies
Data source
Reference
- Reference Type:
- publication
- Title:
- The inhibition of human and rat 11B-hydroxysteroid dehydrogenase 2 by perfluoroalkylated substances
- Author:
- Zhao, B.; Lian, Q.; Chu, Y.; Hardy, D.; Xiao-Kun, L.; Ge, R.
- Year:
- 2 011
- Bibliographic source:
- Journal of Steroid Biochemistry and Molecular Biology. 125: 143-147.
Materials and methods
Test guideline
- Qualifier:
- no guideline available
- Principles of method if other than guideline:
- - Principle of test: The inhibition of human and rat 11beta-hydroxysteriod dehydrogenase by PFBS was evaluated in isolated liver and kidney microsomes.
- Short description of test conditions: Rat kidney was homogenized in 0.01mM phosphate buffered saline (PBS, pH 7.4) containing 0.25M sucrose, and nuclei and large cell debris were removed by centrifugation at 700×g at 4 ◦C for 30 min. The post-nuclear supernatants were centrifuged at 14,500×g at 4 ◦C for 30 min to remove mitochondria, and the resulting supernatants were further centrifuged twice at 105,000×g at 4 C to collect microsomes. The resultant microsomal pellets were resuspended. Protein contents were measured by Bio-Rad Dye Reagent Concentrate according to manufacturer’s instructions. The concentration of microsome protein was adjusted to 2mg/ml. Microsomes were used for measurement of 11beta-HSD2 activities.
The oxidation of CORT by 11beta-HSD2 was determined in a mixture containing 0.2–0.5 uM CORT (plus 30,000cpm [3H]-CORT), 0.2mM NAD+, 10mM DTT and 2% ethanol in 0.1mM potassium phosphate buffer (pH 7.2, 250 uL total volume) at 37 C. Because 11beta-HSD2 in kidney microsomes is present as a dimer, 10 mM DTT (a reducing agent) was added to reaction buffer to disrupt kidney microsomes and the disulfyl group of 11beta-HSD2 to convert 11beta-HSD2 to as a monomer to increase its activity. Reactions were initiated by the addition of microsomes and NAD+ and terminated by the addition of 2ml ice-cold ether. The steroids were extracted by vigorous mixing for 1min, and the organic layer was dried under nitrogen. The extraction efficiency for CORT and 11DHC were 105.8±8.8% (mean±SD) for CORT and 104.2±14.8% for 11DHC. The steroids were separated chromatographically on thin layer plates in chloroform and methanol (90:10, v/v), and the radioactivity was measured using a scanning radiometer (System AR2000, Bioscan Inc., Washington, DC). The percentage conversion of CORT to 11DHC and was calculated by dividing the radioactive counts identified as 11DHC by the total counts associated with CORT plus 11DHC as previously described [16], and the velocity of the 11beta-HSD2 was calculated according to the percentage of substrate conversion, substrate concentration, enzyme amount and reaction time. The formation of product was determined at 4 time points within the linear portion of the reaction.
Inhibition of the oxidation of CORT catalyzed by 11beta-HSD2 was measured using varying concentrations of each inhibitor with the substrate concentrations set to about 2× Km to calculate the half maximal inhibitory concentration (IC50) values. The mode of inhibition was assayed by adding different fixed CORT concentrations in the presence of various concentrations of each inhibitor. Initial velocity data were fit to competitive, noncompetitive, uncompetitive, and mixed inhibition modes. The inhibition constant Ki was determined.
- Parameters analysed / observed: 11beta-HSD2 enzyme activity and inhibition were determined. - GLP compliance:
- no
- Type of method:
- in vitro
- Endpoint addressed:
- other: Inhibition of human and rat 11beta-hydroxysteriod dehydrogenase.
Test material
- Reference substance name:
- Potassium 1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulphonate
- EC Number:
- 249-616-3
- EC Name:
- Potassium 1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulphonate
- Cas Number:
- 29420-49-3
- Molecular formula:
- C4HF9O3S.K
- IUPAC Name:
- potassium 1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulfonate
Constituent 1
- Specific details on test material used for the study:
- SOURCE OF TEST MATERIAL
- Source and lot/batch No.of test material: Sigma Aldrich
- Expiration date of the lot/batch: No data
- Purity test date: No data
Test animals
- Species:
- rat
- Strain:
- Sprague-Dawley
- Remarks:
- Rats were utilized to isolate kidney microsomes.
- Sex:
- male
- Details on test animals or test system and environmental conditions:
- TEST ANIMALS
- Source: CHarles River Laboratories
- Age at study initiation: No data
- Weight at study initiation: 250-300 g
- Fasting period before study: No data
- Housing: No data
- Diet (e.g. ad libitum): No data
- Water (e.g. ad libitum): No data
- Acclimation period: No data
ENVIRONMENTAL CONDITIONS
- Temperature (°C): No data
- Humidity (%): No data
- Air changes (per hr): No data
- Photoperiod (hrs dark / hrs light): No data
IN-LIFE DATES: No data
Administration / exposure
- Route of administration:
- other: Rat and human kidney microsomes were utlized to isolate 11beta-HSD2 enzymes.
- Vehicle:
- not specified
- Details on exposure:
- Upon incubation with PFBS, 11beta-HSD2 activity was measured by the conversion of corticosterone to 11-dehydrocorticosterone in the presence of increasing concentrations of PFBS up to 250 uM.
- Analytical verification of doses or concentrations:
- not specified
- Duration of treatment / exposure:
- Not specified.
Doses / concentrationsopen allclose all
- Dose / conc.:
- 0 other: uM
- Dose / conc.:
- 50 other: uM
- Dose / conc.:
- 250 other: uM
- Details on study design:
- See 'Principles of Method' section.
Results and discussion
- Details on results:
- PFBS generated 1.25 +/- 2.56% inhibition of 11beta-HSD2 activity at the highest dose tested (250 uM).
Applicant's summary and conclusion
- Conclusions:
- PFBS generated 1.25 +/- 2.56% inhibition of 11beta-HSD2 activity at the highest dose tested (250 uM). At concentrations up to 250 mM, K+PFBS did not statistically significantly impact 11beta-HSD2 activity.
- Executive summary:
The inhibition of human and rat 11beta-hydroxysteriod dehydrogenase 2 by PFBS was evaluated in isolated kidney microsomes. Human microsomes were purchased. Rat kidney from male Sprague Dawley rats was homogenized in 0.01mM phosphate buffered saline (PBS, pH 7.4) containing 0.25M sucrose, and nuclei and large cell debris were removed by centrifugation at 700×g at 4 ◦C for 30 min. The post-nuclear supernatants were centrifuged at 14,500×g at 4 ◦C for 30 min to remove mitochondria, and the resulting supernatants were further centrifuged twice at 105,000×g at 4 C to collect microsomes. The resultant microsomal pellets were resuspended. Protein contents were measured by Bio-Rad Dye Reagent Concentrate according to manufacturer’s instructions. The concentration of microsome protein was adjusted to 2mg/ml. Microsomes were used for measurement of 11beta-HSD2 activities. The oxidation of CORT by 11beta-HSD2 was determined in a mixture containing 0.2–0.5 uM CORT (plus 30,000cpm [3H]-CORT), 0.2mM NAD+, 10mM DTT and 2% ethanol in 0.1mM potassium phosphate buffer (pH 7.2, 250 uL total volume) at 37 C. Because 11beta-HSD2 in kidney microsomes is present as a dimer, 10 mM DTT (a reducing agent) was added to reaction buffer to disrupt kidney microsomes and the disulfyl group of 11beta-HSD2 to convert 11beta-HSD2 to as a monomer to increase its activity. Reactions were initiated by the addition of microsomes and NAD+ and terminated by the addition of 2ml ice-cold ether. The steroids were extracted by vigorous mixing for 1min, and the organic layer was dried under nitrogen. The extraction efficiency for CORT and 11DHC were 105.8±8.8% (mean±SD) for CORT and 104.2±14.8% for 11DHC. The steroids were separated chromatographically on thin layer plates in chloroform and methanol (90:10, v/v), and the radioactivity was measured using a scanning radiometer (System AR2000, Bioscan Inc., Washington, DC). The percentage conversion of CORT to 11DHC and was calculated by dividing the radioactive counts identified as 11DHC by the total counts associated with CORT plus 11DHC as previously described [16], and the velocity of the 11beta-HSD2 was calculated according to the percentage of substrate conversion, substrate concentration, enzyme amount and reaction time. The formation of product was determined at 4 time points within the linear portion of the reaction. Inhibition of the oxidation of CORT catalyzed by 11beta-HSD2 was measured using varying concentrations of each inhibitor with the substrate concentrations set to about 2× Km to calculate the half maximal inhibitory concentration (IC50) values. The mode of inhibition was assayed by adding different fixed CORT concentrations in the presence of various concentrations of each inhibitor. Initial velocity data were fit to competitive, noncompetitive, uncompetitive, and mixed inhibition modes. The inhibition constant Ki was determined. PFBS generated 1.25 +/- 2.56% inhibition of 11beta-HSD2 activity at the highest dose tested (250 uM). At concentrations up to 250 mM, K+PFBS did not statistically significantly impact 11beta-HSD2 activity.
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