Work environment and labour market participation in early adulthood.

BACKGROUND: Investigating whether a poor physical or psychosocial work environment is associated with low labour market participation in early adulthood is important to avoid negative health-related consequences and to improve job prospects. AIMS: To investigate associations between the physical or psychosocial work environment and labour market participation in early adulthood. METHODS: The study was based on data from the West Jutland Cohort, an ongoing study of individuals born in 1989 who lived in the western part of Jutland, Denmark, in 2004. Participants were employed individuals who had questionnaire data on their work environment at age 28 and register information on labour market participation at ages 28-29 (n = 1312). The outcome was categorized into low (>4 weeks) versus high (≤4 weeks) labour market participation based on the total number of weeks receiving any unemployment or health-related benefits during a 52-week period. Logistic regression analyses were performed to examine associations between work environment factors and labour market participation, taking confounders into account. RESULTS: Low influence, low quality of leadership, high job insecurity and temporary employment were associated with low labour market participation. High job insecurity (OR: 2.2; 95% CI 1.5-3.1) and temporary employment (OR: 3.1; 95% CI 2.1-4.5) were strongly associated with low labour market participation. An association was seen between hard physical work and low labour market participation. CONCLUSIONS: Several physical and psychosocial work environment factors, especially high job insecurity and temporary employment, have a negative impact on labour market participation in early adulthood.

MBL1 genotypes in wild boar populations from Sweden, Austria, the Czech Republic, and Japan.

The single nucleotide polymorphism (SNP) G949T in the mannose-binding lectin ( MBL ) 1 gene has been associated with low MBL-A concentration in serum and detected at different frequencies in various European pig populations. However, the origin of this SNP is not known. Part of the MBL1 gene was sequenced in 12 wild boar/Large White crossbred pigs from the second backcross (BC 2 ) generation in a family material originating from two wild boar x Large White intercrosses. Also, MBL-A serum concentration was measured in the entire BC 2 generation (n = 45). Furthermore, the genotypes of 68 wild boars from Sweden, Austria, the Czech Republic, and Japan were determined in regard to five previously described SNPs in MBL1 . The T allele of G949T was present among the BC 2 animals. MBL-A serum concentration in the BC 2 animals showed a bimodal distribution, with one-third of the animals at levels between 0.7 and 1.6 µg mL(-1) and the remaining pigs at levels around 13 µg mL(-1) . There was a co-variation between the presence of the T allele and low MBL-A concentration in serum. The genotyping of the wild boars revealed differences between populations. The T allele of G949T was not detected in the Austrian and Japanese samples and is thus unlikely to be an original feature of wild boars. In contrast, it was present at high frequency (0.35) among the Swedish wild boars, probably representing a founder effect. Five MBL1 haplotypes were resolved. Only two of these were present among the Japanese wild boars compared to four in each of the European populations. This difference may reflect differences in selection pressure and population history.

The lectin complement pathway serine proteases (MASPs) represent a possible crossroad between the coagulation and complement systems in thromboinflammation.

UNLABELLED: ESSENTIALS: The lectin pathway's MASP-1/2 activates coagulation factors but the trigger of the activation is unknown. MASP-1/2 activation was assessed by quantifying complexes between MASPs and antithrombin/C1-inhibitor. Activated platelets and fibrin were demonstrated to activate MASP-1 and MASP-2 both in vitro and in vivo. These findings may represent a crossroad between the complement and the coagulation systems. BACKGROUND: The activated forms of the complement lectin pathway (LP) proteases MASP-1 and MASP-2 are able to cleave the coagulation factors prothrombin, fibrinogen, factor XIII and thrombin-activatable fibrinolysis inhibitor in vitro. In vivo studies also show that MASP-1 is involved in thrombogenesis. OBJECTIVES: To clarify the not yet identified mechanisms involved in triggering activation of the LP during thrombotic reactions. METHODS: Novel sandwich-ELISAs for detection of complexes between MASP-1 or MASP-2 and the serpins C1 inhibitor (C1-INH) or antithrombin (AT), were used to specifically detect and quantify the activated forms of MASP-1 and MASP-2. RESULTS: Activated platelets were shown by flow cytometry to bind Ficolin-1, -2 and -3 but not MBL, which was associated with activation of MASP-1 and MASP-2. We also demonstrated that fibrin and the plasmin-generated fibrin fragment DD in plasma, bind and activate MASP-1 and MASP-2. As demonstrated by the ELISA and SDS-PAGE/Western blotting, the fibrin-associated activation was reflected in a specific inactivation by AT during clotting without the assistance of heparin. In all other cases the MASPs were, as previously reported, inactivated by C1-INH. In systemic lupus erythematosus patients with thrombotic disease and in polytrauma patients, the levels of activated MASP-1 and MASP-2 in complex with both AT and C1-INH were associated with markers of thrombotic disease and contact/coagulation system activation. CONCLUSIONS: MASP-1 and MASP-2 are activated during blood clotting. This activation is triggered by activated platelets and by the generation of fibrin during thrombotic reactions in vitro and in vivo, and may represent a novel activation/amplification mechanism in thromboinflammation.

Metabolism of zearalenone by sow intestinal mucosa in vitro.

Homogenized intestinal mucosa samples from sows were incubated with zearalenone in the presence of NADPH or UDPGA. In addition, UDPglucuronosyltransferase activity in the microsomal fraction of mucosa was determined using 1-naphthol as substrate. In the presence of NADPH, zearalenone was reduced to both alpha- and beta-zearalenol (0.37 +/- 0.18 and 0.29 +/- 0.11 nmol/mg protein/hr in the duodenum and jejunum, respectively). The beta-isomer was the predominant metabolite. Glucuronide conjugation of zearalenone was very high compared with the level of reduction occurring (11.3 +/- 6.1 and 9.4 +/- 5.8 nmol conjugated/mg protein/hr in the duodenum and jejunum, respectively). There was no correlation between the rates of glucuronide conjugation of zearalenone and 1-naphthol, indicating that they depend upon two different isoenzymes of UDPglucuronosyltransferase.

Metabolism of aflatoxin, ochratoxin, zearalenone, and three trichothecenes by intact rumen fluid, rumen protozoa, and rumen bacteria.

The effect of rumen microbes on six mycotoxins (aflatoxin B1, ochratoxin A, zearalenone, T-2 toxin, diacetoxyscirpenol, and deoxynivalenol ) considered to be health risks for domestic animals was investigated. The mycotoxins were incubated with intact rumen fluid or fractions of rumen protozoa and bacteria from sheep and cattle in the presence or absence of milled feed. Rumen fluid had no effect on aflatoxin B1 and deoxynivalenol . The remaining four mycotoxins were all metabolized, and protozoa were more active than bacteria. Metabolism of ochratoxin A, zearalenone, and diacetoxyscirpenol was moderately or slightly inhibited by addition of milled feed in vitro. The capacity of rumen fluid to degrade ochratoxin A decreased after feeding, but this activity was gradually restored by the next feeding time. Ochratoxin A was cleaved to ochratoxin alpha and phenylalanine; zearalenone was reduced to alpha-zearalenol and to a lesser degree to beta-zearalenol; diacetoxyscirpenol and T-2 toxin were deacetylated to monoacetoxyscirpenol and HT-2 toxin, respectively. Feeding of 5 ppm (5 mg/kg) of ochratoxin A to sheep revealed 14 ppb (14 ng/ml) of ochratoxin A and ochratoxin alpha in rumen fluid after 1 h, but neither was detected in the blood. Whether such conversions in the rumen fluid may be considered as a first line of defense against toxic compounds present in the diet is briefly discussed.

Plasma and urinary levels of zearalenone and alpha-zearalenol in a prepubertal gilt fed zearalenone.

One prepubertal gilt, fed 192 micrograms zearalenone/kg body weight/day for 4 days, showed plasma concentrations of alpha-zearalenol 3-4 times higher than of the parent compound during the treatment. Zearalenone and alpha-zearalenol could be traced in plasma until the 5th day and in urine until the 4th day of the posttreatment period. A maximum circulating amount of zearalenone plus alpha-zearalenol, 10.4 ng/ml plasma, was found on the 4th day of treatment followed by an urinary excretion of 305 ng/ml urine. All zearalenone and alpha-zearalenol in plasma and urine were bound to glucuronic acid. On the second day of treatment the animal showed oedema and reddening of the vulva which became more pronounced during the treatment. Hormone analysis, however, showed that the animal had no oestrus cycle during the 3 week experimental period.

Quantitative liquid chromatographic method using fluorescence detection for determining zearalenone and its metabolites in blood plasma and urine.

The liquid chromatographic (LC) method described, suitable for use with both blood plasma and urine, is applicable for determination of zearalenone and alpha-zearalenol at levels as low as 0.5 ng/mL plasma and 5 ng/mL urine. The sample is incubated overnight with beta-glucuronidase to analyze for both conjugated and unconjugated forms of zearalenone. The next day, the sample is acidified with H3PO4, extracted with chloroform, and evaporated to dryness. The residue is dissolved in toluene and loaded onto a silica gel cartridge which is washed with toluene and eluted with toluene-acetone (88 + 12). The eluate is evaporated, and the residue is dissolved in chloroform, extracted with 0.18M NaOH, neutralized with H3PO4, and re-extracted with chloroform. The chloroform extract is evaporated, dissolved in mobile phase for LC, and injected onto a normal phase column under the following chromatographic conditions: mobile phase of water-saturated dichloromethane containing 2% 1-propanol, and fluorescence detector, excitation wave-length 236 nm, and 418 nm cut-off emission filter. Recoveries of zearalenone and its metabolites from blood plasma and urine are 80-89% in the range 2.0-10 ng standard/mL plasma, and 81-90% in the range 10-30 ng standard/mL urine. This method was used to analyze blood and urine samples from a pig fed zearalenone-contaminated feed (5 mg/kg), corresponding to 80 micrograms/kg body weight. Zearalenone was rapidly metabolized to alpha-zearalenol, which appeared in the blood only 30 min after feeding. Almost all zearalenone and alpha-zearalenol was found conjugated with glucuronic acid in both blood plasma and urine.