RESUMEN
A design for a radio frequency (RF) neutron spin flipper obtained from magneto-static and neutron spin transport simulations is presented. The RF flipper constructed from this design provides a flipping probability of 0.999 or better for a beam size 6 cm wide and 15 cm high and a wavelength band between 0.4 and 0.6 nm. Three permanent magnet guide field sections with air gaps provide a linear field gradient along the beam propagation direction over a large cross-sectional area. An RF oscillator based on coupling the resonant coil of a Hartley oscillator to the excitation coil was developed, which provides a higher current and, thereby, a larger RF amplitude, as compared to a conventional RF power amplifier. Two opaque He3 neutron spin filters were employed to measure the flipping probability of the flipper with very high precision. A spatially uniform flipping probability of 0.9995(2) or higher was measured over the large cross-sectional area neutron guide. This RF neutron spin flipper will be employed in a polychromatic beam reflectometer at the National Institute of Standards and Technology Center for Neutron Research. This design can be applied to other polarized neutron instruments or applications requiring a very high continuous flipping probability of the neutron spin for a large cross-sectional area beam.
RESUMEN
We used Gaussian separation and receiver operating characteristic (ROC) curves to optimize the neutron sensitivity and gamma rejection of an ultra-thin 6LiF:ZnS(Ag)-scintillator-based neutron detector paired with a silicon photomultiplier (SiPM). We recorded the waveforms while operating the detector in a monochromatic cold neutron beam and in the presence of isotopic 137Cs and 60Co gamma sources. We used a two-window charge comparison (CC) pulse-shape discrimination (PSD) technique to distinguish the neutron capture events from other types of signals. By feeding the recorded waveforms through variants of this algorithm, it was possible to optimize the duration of the integration windows [(0-100 ns) for the prompt window and (100-2300 ns)] for the delayed window. We then computed the detector's ROC curve from waveform recordings and compared that with the experimental performance. We also used this procedure to compare a series of detector configurations to select the optimal bias voltage for the SiPM photosensor.
RESUMEN
The present study aimed to determine different peripheral blood neutrophil functions in 18 morbidly obese subjects with body mass index (BMI) ranging between 35 and 69 kg/m(2) in parallel with age- and gender-matched lean controls. Peripheral blood neutrophil functions of obese subjects and matched lean controls were determined. Neutrophils of obese subjects showed significant elevation of the release of basal superoxides (P < 0.0001), formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated superoxides (P < 0.0001) and opsonized zymosan (OZ)-stimulated superoxides (P < 0.045) compared with lean controls. Interestingly, there were no differences in phorbol myristate acetate (PMA)-stimulated superoxide production by neutrophils of the obese subjects and controls. There was also a significant elevation of chemotactic (P < 0.0003) and random (P < 0.0001) migration of neutrophils from obese subjects compared with lean controls. Phagocytosis, CD11b surface expression and adherence of neutrophils from obese subjects were not significantly different from those of the lean controls. The elevated superoxide production and chemotactic activity, together with the normal phagocytosis and adherence, suggest that neutrophils from obese subjects are primed and have the capability to combat infections. However, neutrophils in the priming state may participate in the pathogenesis of obesity-related diseases.
Asunto(s)
Movimiento Celular/inmunología , Neutrófilos/inmunología , Obesidad Mórbida/inmunología , Fagocitosis/inmunología , Superóxidos/metabolismo , Adulto , Índice de Masa Corporal , Antígeno CD11b/biosíntesis , Adhesión Celular/inmunología , Femenino , Humanos , Masculino , N-Formilmetionina Leucil-Fenilalanina/farmacología , Neutrófilos/efectos de los fármacos , Acetato de Tetradecanoilforbol/farmacología , Zimosan/farmacologíaRESUMEN
In Alzheimer's disease, extracellular deposits of amyloid beta(1-42) (Abeta(1-42)) may induce activation of microglial cells by releasing proinflammatory factors that contribute to the neurodegeneration process. Since the activation of cytosolic phospholipase A(2)alpha (cPLA(2)alpha) has been reported in inflammatory conditions, its role in primary rat microglial cell activated by aggregated Abeta(1-42) was elucidated. The results of the present study show that activation of microglia by 5 microM aggregated Abeta(1-42) (as evident by the amoeboid morphology and increased CD68 immunofluorescence reactivity) caused an immediate activation of cPLA(2)alpha, measured by its phosphorylated form and its specific activity, followed by a gradual elevation of its expression and activity during 24 h. Inhibition of cPLA(2)alpha expression and activity by the presence of 1 microM specific antisense resulted in a significant decrease in NADPH oxidase activity that releases superoxides, PGE(2) formation, iNOS expression, and NO production, indicating a major role for cPLA(2)alpha in the regulation of these inflammatory processes. NADPH oxidase activity, which is under cPLA(2)alpha regulation, was found to upregulate cPLA(2)alpha and COX-2 protein expression through the redox-sensitive NFkappaB activation as evident by its phosphorylation on Ser-536, resulting in increased PGE(2) formation. The secreted PGE(2) induced the synthesis of iNOS and the production of NO through the PKA-CREB pathway. Taken together, our results suggest that the response of cPLA(2)alpha to aggregated Abeta(1-42) is probably a key player in the oxidative stress present in AD, regulating potent oxidative agents: the production of superoxides by NADPH oxidase and NO formation by iNOS.
Asunto(s)
Péptidos beta-Amiloides/metabolismo , Fosfolipasas A2 Grupo IV/metabolismo , Microglía/metabolismo , NADPH Oxidasas/metabolismo , Óxido Nítrico Sintasa de Tipo II/metabolismo , Fragmentos de Péptidos/metabolismo , Animales , Antígenos CD/metabolismo , Antígenos de Diferenciación Mielomonocítica/metabolismo , Western Blotting , Células Cultivadas , Citosol/metabolismo , Dinoprostona/metabolismo , Técnica del Anticuerpo Fluorescente , Inmunoprecipitación , Inflamación/metabolismo , Microscopía Confocal , Óxido Nítrico/metabolismo , Oligodesoxirribonucleótidos Antisentido , Estrés Oxidativo/fisiología , Fosforilación , Radioinmunoensayo , Ratas , Ratas Sprague-Dawley , Factores de TiempoRESUMEN
Mentally retarded people usually receive care in special social, vocational, behavioral or educational facilities. Only recently, we gained some experience in the rehabilitation after trauma of those with mental retardation. We presume that with the increasing awareness of the benefits of comprehensive and early rehabilitation after trauma, orthopedic surgeons, neurosurgeons, and physicians who work in intensive care units, refer more patients who had never before gained from this specialty. We would like to share our experience of the unique rehabilitation process of this population.
Asunto(s)
Discapacidad Intelectual/complicaciones , Rehabilitación/métodos , Heridas y Lesiones/complicaciones , Heridas y Lesiones/rehabilitación , Adulto , Femenino , Humanos , Masculino , Persona de Mediana EdadRESUMEN
Neutrophils and differentiated PLB-985 cells contain various types of PLA(2)s including the 85 kDa cytosolic PLA(2) (cPLA(2)), Ca(2+)-independent PLA(2) (iPLA(2)) and secreted PLA(2)s (sPLA(2)s). The present study focuses on the behavior of sPLA(2)s in neutrophils and PLB cells and their relationship to cPLA(2)alpha. The results of the present research show that the two types of sPLA(2) present in neutrophils, sPLA(2)-V and sPLA(2)-X, which are located in the azurophil granules, are differentially affected by physiological stimuli. While sPLA(2)-V is secreted to the extacellular milieu, sPLA(2)-X is detected on the plasma membranes after stimulation. Stimulation of neutrophils with formyl-Met-Leu-Phe (fMLP), opsonized zymosan (OZ) or A23187 resulted in a different kinetics of sPLA(2) secretion as detected by its activity in the neutrophil supernatants. Neutrophil priming by inflammatory cytokines or LPS enhanced sPLA(2) activity detected in the supernatant after stimulation by fMLP. This increased activity was due to increased secretion of sPLA(2)-V to the supernatant and not to release of sPLA(2)-X. sPLA(2) in granulocyte-like PLB cells exhibit identical characteristics to neutrophil sPLA(2), with similar activity and optimal pH of 7.5. Granulocyte-like cPLA(2)alpha-deficient PLB cells serve as a good model to study whether sPLA(2) activity is regulated by cPLA(2)alpha. Secretion and activity of sPLA(2) were found to be similar in granulocyte-like PLB cells expressing or lacking cPLA(2)alpha, indicating that they are not under cPLA(2)alpha regulation.
Asunto(s)
Neutrófilos/enzimología , Fosfolipasas A/fisiología , Línea Celular , Células Cultivadas , Activación Enzimática , Fosfolipasas A2 Grupo IV , Fosfolipasas A2 Grupo V , Fosfolipasas A2 Grupo X , Humanos , Activación Neutrófila , Fosfolipasas A/metabolismoRESUMEN
Our previously established model of cytosolic phospholipase A(2) (cPLA(2))-deficient, differentiated PLB-985 cells (PLB-D cells) was used to determine the physiological role of cPLA(2) in eicosanoid production. Parent PLB-985 (PLB) cells and PLB-D cells were differentiated toward the monocyte or granulocyte lineages using 5 x 10(-)(8) M 1,25 dihydroxyvitamin D(3) or 1.25% dimethyl sulfoxide, respectively. Parent monocyte- or granulocyte-like PLB cells released prostaglandin E(2) (PGE(2)) when stimulated by ionomycin, A23187, opsonized zymosan, phorbol 12-myristate 13-acetate, or formyl-Met-Leu-Phe (fMLP), and monocyte- or granulocyte-like PLB-D cells did not release PGE(2) with any of the agonists. The kinetics of cPLA(2) translocation to nuclear fractions in monocyte-like PLB cells stimulated with fMLP or ionomycin was in correlation with the kinetics of PGE(2) production. Granulocyte-like PLB cells, but not granulocyte-like PLB-D cells, secreted leukotriene B(4) (LTB(4)) after stimulation with ionomycin or A23187. Preincubation of monocyte-like parent PLB cells with 100 ng/ml lipopolysaccharide (LPS) for 16 h enhanced stimulated PGE(2) production, which is in correlation with the increased levels of cPLA(2) detected in these cells. LPS preincubation was less potent in increasing PGE(2) and LTB(4) secretion and did not affect cPLA(2) expression in granulocyte-like PLB cells, which may be a result of their lower levels of surface LPS receptor expression. LPS had no effect on monocyte- or granulocyte-like PLB-D cells. The lack of eicosanoid formation in stimulated, differentiated cPLA(2)-deficient PLB cells indicates that cPLA(2) contributes to stimulated eicosanoid formation in monocyte- and granulocyte-like PLB cells.
Asunto(s)
Dinoprostona/biosíntesis , Leucotrieno B4/biosíntesis , Células Mieloides/citología , Células Mieloides/metabolismo , Fagocitos/metabolismo , Fosfolipasas A/metabolismo , Diferenciación Celular/fisiología , Linaje de la Célula , Células Cultivadas , Citosol/química , Técnica del Anticuerpo Fluorescente , Humanos , Immunoblotting , Isoenzimas/metabolismo , Fagocitos/citología , Fosfolipasas A2 , Transporte de Proteínas/fisiología , Reacción en Cadena de la Polimerasa de Transcriptasa InversaRESUMEN
Modification of the ryanodine receptor (RyR)/Ca(2+) release channel with 2,4-dinitrofluorobenzene (DNFB) indicated that two classes of amino group interact with the reagent, as can be distinguished on the basis of their reactivity/accessibility and the effects on ryanodine binding and single channel activities. One group interacted very rapidly (t(1/2)<30 s) at 25 degrees C with low concentrations of DNFB [C(50) (concentration of DNFB required for 50% inhibition or stimulation of ryanodine binding)=5 microM], and at pH values of 6.2 and higher. This interaction resulted in the marked stimulation of ryanodine binding and the complete inhibition of a single Ca(2+) release channel incorporated into planar lipid bilayer. The second group is accessible at higher temperatures (37 degrees C); at pH values higher than 7.4 it reacted slowly (t(1/2)=20 min) with high concentrations of DNFB (C(50)=70 microM). This interaction led to the inhibition of ryanodine binding and single channel activity. Modification of RyR with DNFB under the stimulatory conditions resulted in 3.6-fold and 6-fold increases in ryanodine-binding and Ca(2+)-binding affinities respectively. Modification with DNFB under the inhibitory conditions resulted in a decrease in the total ryanodine-binding sites. The exposure of the RyR single channel to DNFB under both inhibitory and stimulatory conditions led to the complete closure of the channel. However, when modified under the stimulatory conditions, but not under the inhibitory ones, the DNFB-modified closed channel could be re-activated by sub-micromolar concentrations of ryanodine, in the presence of nanomolar concentrations of Ca(2+). The DNFB-modified ryanodine-activated RyR channel showed fast transitions between open, closed and several sub-conductance states, and was completely closed by Ruthenium Red. ATP re-activated the DNFB-modified closed channel or, if present during modification, prevented the inhibition of RyR channel activity by DNFB. Neither the stimulation nor the inhibition of ryanodine binding by modification with DNFB was affected by the presence of ATP. By using the photoreactive ATP analogue 3'-O-(4-benzoyl)benzoyl-[alpha-(32)P]ATP we found that DNFB modification had no effect on the ATP-binding site of RyR. The results are discussed with regard to the involvement of amino group residues in channel gating, ryanodine association/dissociation and occlusion, and the relationship between the open/closed state of the RyR and its capacity to bind ryanodine.
Asunto(s)
Dinitrofluorobenceno/metabolismo , Activación del Canal Iónico , Canal Liberador de Calcio Receptor de Rianodina/química , Canal Liberador de Calcio Receptor de Rianodina/metabolismo , Adenosina Trifosfato/análogos & derivados , Adenosina Trifosfato/metabolismo , Adenosina Trifosfato/farmacología , Aminas/química , Aminas/metabolismo , Calcio/metabolismo , Calcio/farmacología , Dinitrofluorobenceno/farmacología , Relación Dosis-Respuesta a Droga , Concentración de Iones de Hidrógeno , Activación del Canal Iónico/efectos de los fármacos , Cinética , Membrana Dobles de Lípidos/química , Membrana Dobles de Lípidos/metabolismo , Peso Molecular , Conformación Proteica/efectos de los fármacos , Rojo de Rutenio/farmacología , Rianodina/agonistas , Rianodina/antagonistas & inhibidores , Rianodina/metabolismo , Rianodina/farmacología , Retículo Sarcoplasmático/química , Retículo Sarcoplasmático/efectos de los fármacos , Retículo Sarcoplasmático/metabolismo , Relación Estructura-ActividadRESUMEN
Two high Mr protein bands (440 and 420 kDa) in sheep brain microsomal membranes were labeled with the photoaffinity ATP analog, O-(4-benzoyl)benzoyl adenosine 5'-triphosphate (Bz2ATP). The 420 kDa band is labeled by [alpha-32P]-Bz2ATP with about 1000-fold higher affinity than the 440 kDa band. The heavily labeled 420 kDa band is identified as dynein heavy chain based on its partial amino acid sequence, and cross-reactivity with anti-dynein antibodies. The 440 kDa protein is immunologically identified as the type-2 RyR. Bz2ATP binding is obtained in the absence of divalent cations. Bz2ATP and ATP increased the binding of ryanodine to its receptor up to 3-fold, and increased the binding affinity up to 6-fold. Other nucleotides stimulate ryanodine binding with decreasing effectiveness: Bz2ATP > ATP > ADP > AMP > AMP-PNP > GTP > cAMP. With respect to nucleotide specificity, this binding site is similar to the skeletal muscle RyR (type 1). However, the brain RyR may have additional one or more sites with lower affinity with inhibitory effect on ryanodine binding. These results suggest that the major RyR isoform in sheep brain corresponds to the type-2 isoform, and that modulation of ryanodine binding by ATP involves its binding to the RyR protein. The association of dynein with brain microsomal membranes may reflect a linkage of RyR to the cytoskeleton.
Asunto(s)
Adenosina Trifosfato/metabolismo , Encéfalo/metabolismo , Canal Liberador de Calcio Receptor de Rianodina/metabolismo , Adenosina Trifosfato/análogos & derivados , Marcadores de Afinidad , Secuencia de Aminoácidos , Animales , Sitios de Unión , Citoesqueleto/metabolismo , Dineínas/genética , Dineínas/metabolismo , Retículo Endoplásmico/metabolismo , Técnicas In Vitro , Membranas Intracelulares/metabolismo , Microsomas/metabolismo , Datos de Secuencia Molecular , Nucleótidos/farmacología , Isoformas de Proteínas/metabolismo , OvinosRESUMEN
Cardiac sarcoplasmic reticulum (SR) contains an endogenous phosphorylation system that under specific conditions phosphorylates two proteins with apparent molecular masses of 150 and 130 kDa. The conditions for their phosphorylation are as for the skeletal muscle sarcalumenin and the histidine-rich Ca2+ binding protein (HCP) with respect to: (i) Ca2+ and high concentrations of NaF are required; (ii) phosphorylation is obtained with no added Mg2+ and shows a similar time course and ATP concentration dependence; (iii) inhibition by similar concentrations of La3+; (iv) phosphorylation is obtained with [gamma-32P]GTP; (v) ryanodine binding is inhibited parallel to the phosphorylation of the two proteins. The endogenous kinase is identified as casein kinase II (CK II) based on its ability to use GTP as effectively as ATP, and its inhibition by La3+. The association of CK II with the cardiac SR, even after EGTA extraction at alkaline pH, is demonstrated using antibodies against CK II. The cardiac 130 kDa protein is identified as sarcalumenin based on its partial amino acid sequence and its blue staining with Stains-All. Cardiac sarcalumenin is different from the skeletal muscle protein based on electrophoretic mobilities, immunological analysis, peptide and phosphopeptide maps, as well as amino acid sequencing. Preincubation of SR with NaF and ATP, but not with NaF and AMP-PNP caused strong inhibition of ryanodine binding. This is due to decrease in Ca2+- and ryanodine-binding affinities of the ryanodine receptor (RyR) by about 6.6 and 18-fold, respectively. These results suggest that cardiac sarcalumenin is an isoform of the skeletal muscle protein. An endogenous CK II can phosphorylate sarcalumenin, and in parallel to its phosphorylation the properties of the ryanodine receptor are modified.
Asunto(s)
Proteínas de la Membrana/metabolismo , Miocardio/química , Péptidos/química , Adenosina Trifosfato/farmacología , Secuencia de Aminoácidos , Animales , Autorradiografía , Calcio/farmacología , Proteínas de Unión al Calcio/química , Proteínas de Unión al Calcio/metabolismo , Carbocianinas , Quinasa de la Caseína II , Perros , Lantano/farmacología , Músculo Esquelético/química , Músculo Esquelético/metabolismo , Miocardio/metabolismo , Péptidos/aislamiento & purificación , Péptidos/metabolismo , Fosforilación , Proteínas Serina-Treonina Quinasas/metabolismo , Conejos , Canal Liberador de Calcio Receptor de Rianodina/metabolismo , Retículo Sarcoplasmático/química , Retículo Sarcoplasmático/metabolismo , Alineación de SecuenciaRESUMEN
In this study we demonstrate the existence of a protein with properties of the voltage-dependent anion channel (VDAC) in the sarcoplasmic reticulum (SR) using multiple approaches as summarized in the following: (a) 35 and 30 kDa proteins in different SR preparations, purified from other membranal systems by Ca2+/oxalate loading and sedimentation through 55% sucrose, cross-react with four different VDAC monoclonal antibodies. (b) Amino acid sequences of three peptides derived from the SR 35 kDa protein are identical to the sequences present in VDAC1 isoform. (c) Similar to the mitochondrial VDAC, the SR protein is specifically labeled by [14C]DCCD. (d) Using a new method, a 35 kDa protein has been purified from SR and mitochondria with a higher yield for the SR. (e) Upon reconstitution into a planar lipid bilayer, the purified SR protein shows voltage-dependent channel activity with properties similar to those of the purified mitochondrial VDAC or VDAC1/porin 31HL from human B lymphocytes, and its channel activity is completely inhibited by the anion transport inhibitor DIDS and about 80% by DCCD. We also demonstrate the translocation of ATP into the SR lumen and the phosphorylation of the luminal protein sarcalumenin by this ATP. Both ATP translocation and sarcalumenin phosphorylation are inhibited by DIDS, but not by atractyloside, a blocker of the ATP/ADP exchanger. These results indicate the existence of VDAC, thought to be located exclusively in mitochondria, in the SR of skeletal muscle, and its possible involvement in ATP transport. Together with recent studies on VDAC multicompartment location and its dynamic association with enzymes and channels, our findings suggest that VDAC deserves attention and consideration as a protein contributing to various cellular functions.
Asunto(s)
Proteínas de la Membrana/análisis , Músculo Esquelético/química , Porinas , Retículo Sarcoplasmático/química , Ácido 4,4'-Diisotiocianostilbeno-2,2'-Disulfónico/farmacología , Adenosina Trifosfato/metabolismo , Animales , Aniones , Atractilósido/farmacología , Transporte Biológico , Diciclohexilcarbodiimida/farmacología , Humanos , Proteínas de la Membrana/antagonistas & inhibidores , Proteínas de la Membrana/metabolismo , Mitocondrias/metabolismo , Músculo Esquelético/metabolismo , Fosforilación , Conejos , Retículo Sarcoplasmático/metabolismo , Canal Aniónico 1 Dependiente del Voltaje , Canales Aniónicos Dependientes del VoltajeRESUMEN
Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum. Tb3+ replaces Ca2+ in both the high- and the low-affinity sites. Occupation of the low-affinity site (inhibitory), but not of the high-affinity Ca2+ binding site (activating), by Tb3+ results in a strong enhanced green fluorescence (at 543 nm) and in an inhibition of ryanodine binding. The Tb3+ concentrations required for half-maximal enhanced fluorescence and inhibition of ryanodine binding were: 22.5 +/- 2.5 microM (n = 4) and 22.3 +/- 3.1 microM (n = 2), respectively. Tb3+ appears to bind to the protein at two or more cooperative sites (nH = 2.4) and to dissociate from these sites with three different rate constants (K-1,1 = 361 +/- 250 min-1 (n = 6); K-1,2 = 0.45 +/- 0.22 min-1 (n = 11); K-1,3 = 0.011 +/- 0.013 min-1 (n = 7). The enhancement in Tb3+ fluorescence is very fast (K1 >> 5 x 10(5) M-1.min-1), and it is quenched by EGTA, La3+, or Ca2+ addition. About 20% of the bound Tb3+ was not displaced by EGTA or Ca2+; suggesting its "occlusion" in the RyR. This is also reflected in the partially irreversible inhibition of ryanodine binding by Tb3+. Reconstitution of sarcoplasmic reticulum vesicles into a planar bilayer lipid membrane showed that the Ca2+ release channel was activated by submicromolar and inhibited by micromolar concentrations of Tb3+ and La3+. The Tb(3+)-activated channel showed an enhancement of the open dwell time of the channel. The results suggest that RyR/Ca2+ release channel undergoes conformational changes due to Tb3+ binding to the low-affinity Ca2+ binding site, and this binding results in the closing of the Ca2+ release channel.
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Canales de Calcio/metabolismo , Calcio/metabolismo , Proteínas Musculares/metabolismo , Retículo Sarcoplasmático/metabolismo , Terbio/metabolismo , Animales , Sitios de Unión , Fluorescencia , Conejos , Canal Liberador de Calcio Receptor de RianodinaRESUMEN
The prevalence of antibodies against Toxoplasma gondii was measured in two rural populations in northern Israel--Jewish kibbutz members and Arab villagers. The respective prevalences in these two populations were 22.2% and 55.8% (P < 0.001). No correlation was found between the presence of antibodies and sex, occupation, contact with cats, a history of fever and/or lymphadenopathy, eye disease, abortions or delivery of children with congenital malformations. In contrast to Jewish children who were not found to have antibodies in the first decade of life, 20.5% of Arab children tested positive. A gradual increase in the prevalence of antibodies with age was seen in both groups, with the Jews reaching a prevalence of 42.6% at age 60+ and the Arabs reaching 74% at age 40. The difference between the two groups probably stems from different eating habits, namely ingestion of raw meat and unpasteurized milk and milk products.
Asunto(s)
Anticuerpos Antiprotozoarios/aislamiento & purificación , Salud Rural , Toxoplasmosis/epidemiología , Adolescente , Adulto , Envejecimiento/inmunología , Niño , Preescolar , Dieta , Femenino , Humanos , Lactante , Recién Nacido , Israel/epidemiología , Masculino , Persona de Mediana Edad , Toxoplasmosis/etnología , Toxoplasmosis/inmunologíaRESUMEN
Positive titers of antibodies against double-stranded (ds) and single-stranded (ss) DNA were found in the sera of 4 and 6 patients, respectively, of 18 who had familial Mediterranean fever (FMF). While anti-dsDNA antibodies were found only in patients with active disease, there was no correlation between the presence of anti-ssDNA antibodies and disease activity. The antibody titers were lower than those found in patients with active systemic lupus erythematosus. This may be due in part to the fact that all the FMF patients were treated with colchicine.