ABSTRACT
BACKGROUND: As the average age of the population continues to rise in the 21st century, chronic illnesses have become the most prominent threats to human health. Research has shown that early screenings for chronic diseases are an effective way of lowering incidence and mortality rates. However, low participation rates for health screening is one of the main challenges for preventive medicine. The objective of this study was to determine the primary drivers which: (1) first motivate people to participate in community-based health screening for chronic diseases; and (2) increase their willingness to continue to participate. METHODS: A total of 440 individuals between 30 and 75 years of age were invited to undergo a health screening and then complete an interview questionnaire. Screenings and interviews were conducted in four regions in northern Taiwan. The questionnaire was separated into three sections, which explored sociodemographic differences, drivers of willingness to participate, and willingness to continue to participate respectively. Raw data was analyzed using the statistical software package SPSS (SPSS Inc., Chicago, IL, USA). MAIN OUTCOME MEASURES: Effects of sociodemographic factors on health screening participation rate, drivers of willingness to participate, and willingness to continue to participate. RESULTS: Seventy-three percent of participants responded that they would be willing to continue to join in future health screenings. Notably, elderly people and married people were respectively more likely to participate in preventive health screening than were younger people and people who were single, divorced, separated, or widowed. Level of education was another key driver of willingness to participate in health screening for chronic diseases, as were the concern of relatives/friends and the provision of participation incentives. DISCUSSION: Some of our findings, such as the key drivers of willingness to continue to participate in health screening that we identified, were different from findings of many previous studies conducted in other countries. The current study also found that a higher percentage of participants would be willing to join a similar health screening in the future if the service design is considered in advance and is well-implemented.
Subject(s)
Chronic Disease/psychology , Community Health Centers/statistics & numerical data , Mass Screening/psychology , Mass Screening/statistics & numerical data , Motivation , Preventive Health Services/statistics & numerical data , Adult , Aged , Female , Humans , Male , Middle Aged , Surveys and Questionnaires , TaiwanABSTRACT
Both endogenous and exogenous methylamine have been found to be involved in many human disorders. The quantitative assessment of methylamine has drawn considerable interest in recent years. Although there have been many papers about the determination of methylamine, only a few of them involved cigarette smoke or mammalian tissue analysis. The major hurdles of the determination of methylamine are the collection of methylamine from samples and the differentiation of methylamine from the background compounds, e.g., biogenic amines. We have solved this problem using a micro trapping system coupled with an HPLC procedure. The interference from other biogenic amines has been avoided. The high selectivity of this method was achieved using four techniques: distillation, trapping, HPLC separation and selective detection. The chromatograms of both mouse tissues and cigarette smoke are simple, with only a few peaks. The method is easy and efficient and it has been validated and applied to the determination of methylamine in tissues of normal CD 1 mice and cigarette smoke. The methylamine contents were determined to be approximately 268.3 ng g(-1) in the liver, 429.5 ng g(-1) in the kidney and 547.4 ng g(-1) in the brain respectively. The methylamine in the cigarette smoke was approximately 213 ng to 413 ng per cigarette. These results in tissues and in cigarette smoke were found to be consistent with the data in the previous literature. To the best of our knowledge, this is the first report on a method suitable for methylamine analysis in both mammalian tissue and cigarette smoke.
Subject(s)
Methylamines/analysis , Smoking , Animals , Chromatography, High Pressure Liquid , MiceABSTRACT
Methylamine and aminoacetone are endogenous aliphatic amines found in human blood and urine. They can be oxidized by semicarbazide-sensitive amine oxidase (SSAO), leading to the production of toxic aldehydes such as formaldehyde and methylglyoxal as well as hydrogen peroxide and ammonia. SSAO is localized on the surface of vascular endothelial and smooth muscle cells and of adipocytes. Increases in SSAO activity are linked to vascular disorders associated with pathological conditions such as diabetic complications, heart failure, and vascular dementia. Quantitative assessment of methylamine and acetonitrile in tissues has been hampered due to the volatility and hydrolipophilicity of these amines as well as interference by complex biological constituents. We have overcome this problem and developed an FMOC/HPLC (9-fluorenylmethyl chloroformate-Cl/high-performance liquid chromatography) method for simultaneous assessment of methylamine and aminoacetone. This method has been validated using rodent tissues with a detection limit at the picogram level. Methylamine and aminoacetone distributed unevenly among different tissues ranged from 0.1 to 27 nmol/g. To our knowledge, this is the first report on simultaneous determination of methylamine and aminoacetone in mammal tissues.
Subject(s)
Acetone/analogs & derivatives , Chromatography, High Pressure Liquid/methods , Methylamines/analysis , Acetone/analysis , Acetone/blood , Amine Oxidase (Copper-Containing)/metabolism , Animals , Chromatography, High Pressure Liquid/instrumentation , Fluorenes/chemistry , Male , Methylamines/blood , Mice , Mice, Inbred Strains , Reproducibility of Results , Spectrometry, FluorescenceABSTRACT
PURPOSE: To determine whether low-dose creatine and protein supplementation during resistance training (RT; 3 d x wk(-1); 10 wk) in older men (59-77 yr) is effective for improving strength and muscle mass without producing potentially cytotoxic metabolites (formaldehyde). METHODS: Older men were randomized (double-blind) to receive 0.1 g x kg(-1) creatine + 0.3 g x kg(-1) protein (CP; n = 10), creatine (C; n = 13), or placebo (PLA; n = 12) on training days. Measurements before and after RT included lean tissue mass (air-displacement plethysmography), muscle thickness (ultrasound) of elbow, knee, and ankle flexors and extensors, leg and bench press strength, and urinary indicators of cytotoxicity (formaldehyde), myofibrillar protein degradation [3-methylhistidine (3-MH)],and bone resorption [cross-linked N-telopeptides of type I collagen (NTx)]. RESULTS: Subjects in C and CP groups combined experienced greater increases in body mass and total muscle thickness than PLA (P < 0.05). Subjects who received CP increased lean tissue mass (+5.6%) more than C (+2.2%) or PLA (+1.0%; P < 0.05) and increased bench press strength (+25%) to a greater extent than C and PLA combined (+12.5%; P < 0.05). CP and C did not differ from PLA for changes in formaldehyde production (+24% each). Subjects receiving creatine (C and CP) experienced a decrease in 3-MH by 40% compared with an increase of 29% for PLA (P < 0.05) and a reduction in NTx (-27%) versus PLA (+13%; P = 0.05). CONCLUSIONS: Low-dose creatine combined with protein supplementation increases lean tissue mass and results in a greater relative increase in bench press but not leg press strength. Low-dose creatine reduces muscle protein degradation and bone resorption without increasing formaldehyde production.
Subject(s)
Creatine/administration & dosage , Dietary Proteins/administration & dosage , Resistance Training , Aged , Bone Resorption/metabolism , Dietary Supplements , Dose-Response Relationship, Drug , Double-Blind Method , Formaldehyde/analysis , Formaldehyde/urine , Humans , Male , Middle Aged , Muscle Strength , Myofibrils/metabolism , PlacebosABSTRACT
Nanoparticles based on amorphous poly(3-hydroxybutyrate)-poly(ethylene glycol)-poly(3-hydroxybutyrate) (PHB-PEG-PHB) are potential drug delivery vehicles, and so their cytotoxicity and hemolysis assay were investigated in vitro using two kinds of animal cells. The PHB-PEG-PHB nanoparticles showed excellent biocompatibility and had no cytotoxicity on animal cells, even when the concentrations of the PHB-PEG-PHB nanoparticle dispersions were increased to 120 microg/mL. Moreover, no hemolysis was detected with the PHB-PEG-PHB nanoparticles, suggesting that the PHB-PEG-PHB nanoparticles were obviously much hemocompatible for drug delivery applications. In the presence of intracellular enzyme esterase, the biocompatible PHB-PEG-PHB nanoparticles might be hydrolyzed, and their biodegradable behavior was monitored by the fluorescence spectrum and the pH meter. The initial biodegradation rate of the PHB-PEG-PHB nanoparticles was closely related to the enzymatic amount and the PHB block length. Compared with that obtained from the fluorescence determination, the initial biodegradation rate from pH measurement was faster. The biodegraded products mainly consisted of 3HB monomer and dimer, which were the metabolites present in the body.
Subject(s)
Cytotoxins , Drug Carriers , Hemolysis , Nanoparticles , Polyesters , Polyethylene Glycols , Animals , Biocompatible Materials/chemistry , Biocompatible Materials/metabolism , Cell Adhesion , Cell Line , Cell Proliferation , Cytotoxins/chemistry , Cytotoxins/metabolism , Drug Carriers/chemistry , Drug Carriers/metabolism , Hydrogen-Ion Concentration , Materials Testing , Nanoparticles/chemistry , Nanoparticles/ultrastructure , Polyesters/chemistry , Polyesters/metabolism , Polyethylene Glycols/chemistry , Polyethylene Glycols/metabolismABSTRACT
Aminoguanidine (AG) is capable of preventing advanced protein glycation and inhibiting the activity of enzymes with carbonyl groups as cofactors, such as nitric-oxide synthase (NOS) and semicarbazide-sensitive amine oxidase (SSAO). The hydrazide moiety of AG can also interact with different endogenous carbonyl metabolites and potentially harmful endogenous aldehydes. Aldehydes can be generated via different pathways, such as lipid peroxidation (malondialdehyde and 4-hydroxynonenal), oxidative deamination (aldehydes), and carbohydrate metabolism (methylglyoxal). Formaldehyde and methylglyoxal are produced via SSAO-catalyzed deamination of methylamine and aminoacetone, respectively. An increase in SSAO-mediated deamination is known to be associated with various vascular disorders, such as diabetic complications. The present study demonstrates that AG is not only capable of rapidly interacting with aldehydes in vitro but also scavenging aldehydes in vivo. The AG-formaldehyde adducts were traced, and their structures were elucidated by high-performance liquid chromatography-mass spectrometry. AG has also been shown to block formaldehyde-induced beta-amyloid aggregation. Thus, AG can be an aldehyde scavenger in addition to blocking advanced glycation and inhibition of SSAO and NOS activity. Such reactions may contribute to its pharmacological effects in the treatment of vascular disorders associated with diabetic complications and other disorders.
Subject(s)
Amine Oxidase (Copper-Containing)/metabolism , Formaldehyde/metabolism , Guanidines/metabolism , Aldehydes/metabolism , Amination , Amine Oxidase (Copper-Containing)/antagonists & inhibitors , Animals , Diabetic Angiopathies , Free Radical Scavengers , Glycation End Products, Advanced/antagonists & inhibitors , Mice , Nitric Oxide Synthase/antagonists & inhibitorsABSTRACT
Aldehydes are capable of inducing protein cross-linkage. An increase in aldehydes has been found in Alzheimer's disease. Formaldehyde and methylglyoxal are produced via deamination of, respectively, methylamine and aminoacetone catalyzed by semicarbazide-sensitive amine oxidase (SSAO, EC 1.4.3.6. The enzyme is located on the outer surface of the vasculature, where amyloidosis is often initiated. A high SSAO level has been identified as a risk factor for vascular disorders. Serum SSAO activity has been found to be increased in Alzheimer's patients. Malondialdehyde and 4-hydroxynonenal are derived from lipid peroxidation under oxidative stress, which is also associated with Alzheimer's disease. Aldehydes may potentially play roles in beta-amyloid aggregation related to the pathology of Alzheimer's disease. In the present study, thioflavin-T fluorometry, dynamic light scattering, circular dichroism spectroscopy and atomic force microscopy were employed to reveal the effect of endogenous aldehydes on beta-amyloid at different stages, i.e. beta-sheet formation, oligomerization and fibrillogenesis. Formaldehyde, methylglyoxal and malondialdehyde and, to a lesser extent, 4-hydroxynonenal are not only capable of enhancing the rate of formation of beta-amyloid beta-sheets, oligomers and protofibrils but also of increasing the size of the aggregates. The possible relevance to Alzheimer's disease of the effects of these aldehydes on beta-amyloid deposition is discussed.
Subject(s)
Aldehydes/metabolism , Alzheimer Disease/metabolism , Amyloid beta-Peptides/chemistry , Amyloid beta-Peptides/metabolism , Brain/metabolism , Neurofibrillary Tangles/metabolism , Aldehydes/pharmacology , Alzheimer Disease/physiopathology , Amine Oxidase (Copper-Containing)/metabolism , Amyloid beta-Peptides/drug effects , Benzothiazoles , Brain/physiopathology , Cell Adhesion Molecules/metabolism , Fluorometry , Formaldehyde/metabolism , Humans , Lipid Peroxidation/physiology , Malondialdehyde/metabolism , Microscopy, Atomic Force , Oxidative Stress/physiology , Polymers/metabolism , Protein Folding , Proteomics/methods , Pyruvaldehyde/metabolism , Spectrum Analysis , ThiazolesABSTRACT
New amorphous amphiphilic triblock copolymers of poly(3-hydroxybutyrate)-poly(ethylene glycol)-poly(3-hydroxybutyrate) (PHB-PEG-PHB) were synthesized using the ring-opening copolymerization of beta-butyrolactone monomer. They were characterized by fluorescence, SEM and (1)H NMR. These triblock copolymers can form biodegradable nanoparticles with core-shell structure in aqueous solution. Comparing to the poly(ethylene oxide)-PHB-poly(ethylene oxide) (PEO-PHB-PEO) copolymers, these nanoparticles exhibited much smaller critical micelle concentrations and better drug loading properties, which indicated that the nanoparticles were very suitable for delivery carriers of hydrophobic drugs. The drug release profile monitored by fluorescence showed that the release of pyrene from the PHB-PEG-PHB nanoparticles exhibited the second-order exponential decay behavior. The initial biodegradation rate of the PHB-PEG-PHB nanoparticles was related to the enzyme amount, the initial concentrations of nanoparticle dispersions and the PHB block length. The biodegraded products detected by (1)H NMR contained 3HB monomer, dimer and minor trimer, which were safe to the body.
Subject(s)
Absorbable Implants , Drug Carriers/chemistry , Nanostructures/chemistry , Pharmaceutical Preparations/administration & dosage , Pharmaceutical Preparations/chemistry , Polyesters/chemistry , Polyethylene Glycols/chemistry , Absorption , Diffusion , Hydrophobic and Hydrophilic Interactions , Materials Testing , Nanostructures/ultrastructure , Particle SizeABSTRACT
Semicarbazide-sensitive amine oxidase (SSAO) resides on the vascular endothelium and smooth muscle cell surface and is capable of deaminating short chain aliphatic amines and producing toxic aldehydes and hydrogen peroxide. The enzyme, also known as a vascular adhesion protein-1, is involved in the inflammation process. This intriguing protein with dual functions is increased in the serum of diabetic and heart failure patients. In the present study we assessed the involvement of SSAO in a lipopolysaccharide-induced pulmonary inflammation model using transgenic mice that overexpress human vascular adhesion protein-1. Overexpression of SSAO activity increased the formation of protein-formaldehyde deposits in tissues. Lysine residues of proteins were the primary targets for cross-linkage with formaldehyde derived from deamination of methylamine. Lipo-polysaccharide-induced increases in inflammatory cells in the bronchoalveolar lavage (BAL) fluid were significantly higher in the transgenic than in the nontransgenic mice. BAL cell counts were also higher in the untreated transgenic than in nontransgenic mice. Blocking SSAO activity with a selective inhibitor significantly reduced the number of neutrophils as well as levels of macrophage inflammatory protein-1alpha, granulocyte colony-stimulating factor, tumor necrosis factor-alpha, and interleukin-6 in the BAL fluid. Inhalation of methylamine also increased BAL neutrophil counts. Together, these results suggest a role for SSAO-mediated deamination in pulmonary inflammation.
Subject(s)
Amine Oxidase (Copper-Containing)/physiology , Cell Adhesion Molecules/physiology , Pneumonia, Bacterial/enzymology , Amine Oxidase (Copper-Containing)/antagonists & inhibitors , Amine Oxidase (Copper-Containing)/genetics , Animals , Bronchoalveolar Lavage Fluid/cytology , Cell Adhesion Molecules/antagonists & inhibitors , Cell Adhesion Molecules/genetics , Chemokine CCL4 , Deamination , Granulocyte Colony-Stimulating Factor/metabolism , Humans , Interleukin-6/metabolism , Leukocyte Count , Lipopolysaccharides/toxicity , Macrophage Inflammatory Proteins/metabolism , Methylamines/metabolism , Methylamines/pharmacology , Mice , Mice, Transgenic , Neutrophils/drug effects , Neutrophils/metabolism , Pneumonia, Bacterial/chemically induced , Pneumonia, Bacterial/genetics , Proteins/metabolism , Tumor Necrosis Factor-alpha/metabolismABSTRACT
Increase in methylglyoxal is thought to be involved in different pathological conditions. Deamination of aminoacetone by semicarbazide-sensitive amine oxidase (SSAO) leads to production of methylglyoxal. We have synthesized aminoacetone and developed a novel HPLC procedure for its quantitative determination. The urinary excretion of aminoacetone is approximately 20-30 microg/mouse/day, and the concentration is about 0.5 microg/g in mouse liver and small intestine. SSAO inhibitor increases aminoacetone levels in both tissues and urines. Results confirm that aminoacetone is an endogenous substrate for SSAO. However, data also indicate that deamination is not the only catabolic pathway for aminoacetone.
Subject(s)
Acetone/analogs & derivatives , Chromatography, High Pressure Liquid/methods , Pyruvaldehyde/metabolism , Acetone/chemistry , Acetone/metabolism , Acetone/urine , Allyl Compounds/pharmacology , Amine Oxidase (Copper-Containing)/antagonists & inhibitors , Amine Oxidase (Copper-Containing)/metabolism , Amino Acids/chemistry , Animals , Anion Exchange Resins , Butylamines/pharmacology , Chromatography, Ion Exchange/methods , Enzyme Inhibitors/pharmacology , Fluorenes/chemistry , Intestinal Mucosa/metabolism , Intestines/drug effects , Liver/drug effects , Liver/metabolism , Male , Mice , Rats , Rats, Wistar , Reproducibility of ResultsABSTRACT
The effects of saturated and unsaturated fatty acids (lauric acid, palmitic acid, steric acid, oleic acid, linoleic acid, soybean oil) on Sphaerotilus natans, 0B17 (Pseudomonas sp.), and recombinant Escherichia coli DH5(/pUC19/CAB were studied. Oleic acid enhances Poly-3-hydroxybutyrate (PHB) production in these three bacterial strains, suggesting that the single double bond of the acid activates the polyhydroxylkanoate accumulation enzymatic reaction. Under the effect of lauric acid and linoleic acid, the growth of S. natans and 0B17 were totally inhibited. However, the enhanced PHB accumulation in recombinant E. coli was observed.
Subject(s)
Cell Culture Techniques/methods , Escherichia coli/physiology , Fatty Acids/metabolism , Hydroxybutyrates/metabolism , Polyesters/metabolism , Pseudomonas/physiology , Sphaerotilus/physiology , Bioreactors/microbiology , Cell Proliferation/drug effects , Escherichia coli/classification , Escherichia coli/drug effects , Fatty Acids/pharmacology , Pseudomonas/classification , Pseudomonas/drug effects , Species Specificity , Sphaerotilus/classification , Sphaerotilus/drug effectsABSTRACT
Films made of poly (3-hydroxybutyrate) (PHB), poly(3-hydroxybutyrate- co-3-hydroxyhexanoate) (PHBHHx) consisting of 5%, 12% and 20% hydroxyhexanoate (HHx), respectively, were evaluated for biomedical application in comparison with poly (L-Lactide) (PLA). With the increase of HHx content in PHBHHx, the polymer surface properties changed accordingly. P(HB-co-20%-HHx) had the smoothest surface while PHB surface was most hydrophilic among the evaluated PHB and all the PHBHHx. All PHBHHx also showed strong protein affinity and biocompatibility. It was found that fibroblast and osteoblast had different responses to these polymers: fibroblast cells favored P(HB-co-20%-HHx), yet osteoblast cells preferred P(HB-co-12%-HHx). PHB and all PHBHHx appeared to have better biocompatibility for fibroblast and osteoblast compared with PLA. Polymers possessing different surface properties may help meet different cellular requirements. Combined with their good mechanical properties for elongation and adjustable biocompatibility, PHBHHx may meet the needs of growth requirements of different tissues and cells.
Subject(s)
3-Hydroxybutyric Acid/chemistry , Biocompatible Materials/chemistry , Caproates/chemistry , Fibroblasts/cytology , Fibroblasts/physiology , Osteoblasts/cytology , Osteoblasts/physiology , Tissue Engineering/methods , Animals , Cell Proliferation , Cells, Cultured , Materials Testing , Membranes, Artificial , Mice , Rabbits , Surface PropertiesABSTRACT
Semicarbazide-sensitive amine oxidase (SSAO) catalyzes the conversion of methylamine to formaldehyde. This enzyme is located on the surface of the cytoplasmic membrane and in the cytosol of vascular endothelial cells, smooth muscle cells, and adipocytes. Increased SSAO activity has been found in patients with diabetes mellitus, chronic heart failure, and multiple types of cerebral infarcts and is associated with obesity. Increased SSAO-mediated deamination may contribute to protein deposition, the formation of plaques, and inflammation, and thus may be involved in the pathophysiology of chronic vascular and neurological disorders, such as diabetic complications, atherosclerosis, and Alzheimer's disease. In the present study, we demonstrate the induction of cross-linkage of formaldehyde with the lysine moiety of peptides and proteins. Formaldehyde-protein adducts were reduced with sodium cyanoborohydride, hydrolyzed in hydrochloric acid, and the amino acids in the hydrolysates were derivatized with fluorenylmethyl chloroformate and then identified with high-performance liquid chromatography. We further demonstrate that incubation of methylamine in the presence of SSAO-rich tissues, e.g., human brain meninges, results in formaldehyde-protein cross-linkage of particulate bound proteins as well as of soluble proteins. This cross-linkage can be completely blocked by a selective inhibitor of SSAO. Our data support the hypothesis that the SSAO-induced production of formaldehyde may be involved in the alteration of protein structure, which may subsequently cause protein deposition associated with chronic pathological disorders.
Subject(s)
Amine Oxidase (Copper-Containing)/metabolism , Cross-Linking Reagents/metabolism , Formaldehyde/metabolism , Methylamines/metabolism , Proteins/metabolism , Animals , Brain/cytology , Brain/metabolism , Deamination , Humans , Lysine/metabolism , Male , Mice , Rats , Serum Albumin, Bovine/metabolismABSTRACT
Semicarbazide-sensitive amine oxidase (SSAO) is located on outer surfaces of adipocytes and endothelial and vascular smooth muscle cells. This enzyme catalyzes deamination of methylamine and aminoacetone, leading to production of toxic formaldehyde and methylglyoxal, respectively, as well as hydrogen peroxide and ammonium. Several lines of evidence suggest that increased SSAO activity is related to chronic inflammation and vascular disorders related to diabetic complications. We found that a highly potent and selective SSAO inhibitor, (E)-2-(4-fluorophenethyl)-3-fluoroallylamine (FPFA), was capable of reducing numbers of atherosclerotic lesions as well as weight gain in obese KKAy mice fed an atherogenic diet. SSAO inhibitors cause a moderate and long-lasting hyperglycemia. Such an increase in serum glucose is a result of reduction of glucose uptake by adipocytes. SSAO-mediated deamination of endogenous methylamine substrates induces adipocyte glucose uptake and lipogenesis. Highly selective SSAO inhibitors can effectively block induced glucose uptake. The results suggest that increased SSAO-mediated deamination may be concomitantly related to obesity and vascular disorders associated with type 2 diabetes.
Subject(s)
Adipose Tissue/metabolism , Amine Oxidase (Copper-Containing)/physiology , Diabetes Mellitus/genetics , Diabetes Mellitus/metabolism , Glucose/metabolism , Muscle Proteins , Obesity/metabolism , Weight Gain/physiology , Adipocytes/physiology , Amine Oxidase (Copper-Containing)/antagonists & inhibitors , Animals , Benzylamines/pharmacology , Biological Transport, Active , Blood Glucose/metabolism , Cell Differentiation/physiology , Deamination , Deoxyglucose/metabolism , Enzyme Inhibitors/pharmacology , Glucose Transporter Type 4 , Hypoglycemic Agents/pharmacology , Insulin/pharmacology , Mice , Mice, Obese , Monosaccharide Transport Proteins/metabolism , Obesity/enzymology , Weight Gain/drug effects , Weight Gain/geneticsABSTRACT
Formaldehyde is a well-known environmental toxic hazard. It is also a product of oxidative deamination of methylamine catalyzed by semicarbazide-sensitive amine oxidase (SSAO). Increased SSAO-mediated deamination has been implicated in some pathophysiological conditions, such as diabetic complications. The measurement of formaldehyde in the enzymatic reactions and in vivo production using conventional methods was not straightforward due to limitations of selectivity and sensitivity. A novel high-performance liquid chromatography (HPLC)/electrochemical procedure for the measurement of formaldehyde has been developed. The measurement is based on the formation of adducts between formaldehyde and dopamine. These adducts can be selectively purified and concentrated using a batch method of alumina absorption, separated by HPLC, and electrochemically quantified. The method is highly selective and substantially more sensitive, i.e., detection of picomole levels of formaldehyde, than the conventional methods. The procedure not only facilitates the assessment of SSAO activity in vitro but also is useful for assessing formaldehyde in tissues and biological fluids.
Subject(s)
Chromatography, High Pressure Liquid/methods , Formaldehyde/analysis , Formaldehyde/urine , Methylamines/metabolism , Animals , Brain Chemistry , Calibration , Deamination , Dopamine/metabolism , Electrochemistry , Formaldehyde/metabolism , Kidney/chemistry , Liver/chemistry , Male , Mice , Models, Molecular , Oxidation-Reduction , Rabbits , Sensitivity and SpecificityABSTRACT
Batch biosorption experiments were conducted to investigate the removal of Cu2+ ions from aqueous solutions by a series of bacterial strains isolated from a local activated sludge process. The characteristics of 12 isolates were identified and examined for their ability to bind Cu2+ ions from aqueous solution. Among the isolates, two species exhibited biosorption capacity >40 mg of Cu/g of dry cell. Isotherms for the biosorption of copper on bacterial cells were developed and compared, and the equilibrium data fitted well to the Langmuir and Freundlich isotherm models. The biosorption of copper increased significantly with increasing pH from 2.0 to 6.0 regardless of the species. More than 90% of copper sorbed on the cells of Bacillus sp. could be recovered by washing with 0.1 M HNO3 for 5 min. The performance of two different desorption processes was also tested and compared. The results show that five biosorption and desorption cycles are a better operation process than five successive biosorptions followed by one desorption to remove and recover copper from aqueous solution. The biosorbent could be used for at least five biosorptions and desorption cycles without loss of copper removal capacity. It can be concluded that the activated sludge or sludge-isolated bacteria could be a potential biosorbent for copper removal.
Subject(s)
Bacillus/metabolism , Bacteria/metabolism , Copper/metabolism , Micrococcus/metabolism , Pseudomonas/metabolism , Sewage , Adsorption , Bacteria/classification , Bacteria/isolation & purification , Hydrogen-Ion Concentration , KineticsABSTRACT
Semicarbazide-sensitive amine oxidase (SSAO) catalyzes the deamination of primary amines. Such deamination has been shown capable of regulating glucose transport in adipose cells. It has been independently discovered that the primary structure of vascular adhesion protein-1 (VAP-1) is identical to SSAO. VAP-1 regulates leukocyte migration and is related to inflammation. Increased serum SSAO activities have been found in patients with diabetic mellitus, vascular disorders and Alzheimer's disease. The SSAO-catalyzed deamination of endogenous substrates, that is, methylamine and aminoacetone, led to production of toxic formaldehyde and methylglyoxal, hydrogen peroxide and ammonia, respectively. These highly reactive aldehydes have been shown to initiate protein cross-linkage, exacerbate advanced glycation of proteins and cause endothelial injury. Hydrogen peroxide contributes to oxidative stress. 14C-methylamine is converted to 14C-formaldehyde, which then forms labeled long-lasting protein adduct in rodents. Chronic methylamine treatment increased the excretion of malondialdehyde and microalbuminuria, and enhanced the formation of fatty streaks in C57BL/6 mice fed with an atherogenic diet. Treatment with selective SSAO inhibitor reduces atherogenesis in KKAy diabetic mice fed with high-cholesterol diet. Aminoguanidine, which blocks advanced glycation and reduces nephropathy in animals, is in fact more potent at inhibiting SSAO than its effect on glycation. It suggests that SSAO is involved in vascular disorders under certain pathological conditions. Although SSAO has been known for several decades, its physiological and pathological implications are just beginning to be recognized.
Subject(s)
Acetone/analogs & derivatives , Amine Oxidase (Copper-Containing)/physiology , Semicarbazides/pharmacology , Acetone/metabolism , Adipocytes/metabolism , Amine Oxidase (Copper-Containing)/blood , Animals , Catalysis , Cell Adhesion Molecules/physiology , Deamination , Formaldehyde/toxicity , Glucose/metabolism , Humans , Hydrogen Peroxide/toxicity , Inflammation/etiology , Methylamines/metabolism , Oxidation-ReductionABSTRACT
Polyhydroxyalkanoates, biodegradable plastics with the desired physical and chemical properties of conventional synthetic plastics, are extensively investigated. In this study, specific bacterial strains produced specific copolymers from food waste. Copolymers of HB and HV (poly[3-hydroxybutyrate-co-3-hydroxyvalerate]) were obtained using various ratios of butyric acid (C4) and valeric acid (C5) as carbon sources. The C4 to C5 ratio affected the melting points of the copolymers. Melting and glass transition temperatures and many other thermal properties are important parameters relative to in-service polymer applications. Higher ratios of butyrate to valerate gave higher melting points. When a mixed culture of activated sludge was employed to produce copolymers using food wastes as nutrients, the obtained copolymers showed various monomer compositions. Copolymers with a higher portion of HV were obtained using soy waste; copolymers with less HV were obtained using malt wastes. Pure strains, (i.e., Alcaligenes latus DSM 1122, and DSM 1124, Staphylococcus spp., Klebsiella spp.) produced specific copolymers from food waste. Only Klebsiella spp. produced different copolymers; the ratios of HB:HV were 93:7 and 79:21 from malt waste and soy waste, respectively. The other strains produced polymers of 100% HB. Selecting industrial food wastes as carbon sources can further reduce the cost of producing copolymers.