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BackgroundChildren’s congenital hip dislocation is ranked first, accounting for 49,4% among other skeletal anomalieswhich cause to physical disability.There is a tendency that the number of newborn with the congenitalhip dislocation is going to be increased in recent years, 5000:1 were in 1976 and 1000:1,3% in 1998.Bilateral dysplasia accounts for 50-62% of the total incidences. In unilateral cases,left hip seems to beinvolved 2 times more than the right,and the sex ratio is 2,5:1. Some cultures who swaddle their infantstightly with their legs straightened have a far greater incidence of developmental dysplasia of the hip. Aresearch indicated that discouraging this traditional swaddling method has reduced the prevalence ofdevelopmental dysplasia of the hip and congenital hip dislocationby 6 times in America. It is noted thatthis methodhas also been implemented in Japan and Turkey.Aim.This research aimed to study about the prevalence of congenital hip dislocation, developmental dysplasiaof the hip and other anomalies among the children who were underwent treatment at Pediatric Traumaand Orthopedic Department of National Trauma and OrthopedicResearch Centre of Mongolia in 2013-2015 and children served by outpatient visit in the clinics in 2011-2015.The following objectives were defined in the scope of the research. Herein:1. Evaluate and determine the percentage and prevalence of congenital hip dislocation anddevelopmental dysplasia of the hip among the children who undergo treatment in Pediatric Traumaand Orthopedic Departmentof National Trauma Orthopedic Research Center of Mongolia.2. Evaluate and determine the percentage and prevalence of congenital hip dislocation, developmentaldysplasia of the hip and other anomalies among children who are being served by outpatient visit inClinics of National Trauma and Orthopedic Research Center of Mongolia.Materialis and MethodThis research were studied the prevalence of congenital hip dislocation, developmental dysplasia of thehip and other anomalies among the children who were underwent treatment at Pediatric Trauma andOrthopedic Department of National Trauma and OrthopedicResearch Centre of Mongolia in 2013-2015and children served by outpatient visit in the clinics in 2011-2015.ResultTotal of 40559 inpatients underwent treatment in National Trauma andOrthopedic Research of Mongolia;of which 12217 were inpatient in Pediatric Trauma and Orthopedic Department, aged 0-19;of which1351 has been registered with birth defects of hip; of which 248 has been diagnosed with developmentaldysplasia hip, 869 with congenital hip dislocation. Sex ratio of cases of congenital hip dislocationinmales to female is around 1:4.Total of 633 (13,8%) examinations were performed in the clinics in 2011;704 (15,3%) in 2012;962 (20,9%)in 2013;1013 (22%) in 2014;1287 (28%) in 2015 respectively. It shows an increase in the number ofexaminations year by year.Total of 4142 (90,1%) cases were diagnosed with congenital hip dislocation and developmental dysplasiain both hips; left hip has been dislocated 2 times more than the right, 162 (3,5%) with congenitaldislocation of right hip; 292 (6.4%) with congenital dislocation of left hip.ConclusionTo conclude, the analysis above shows that the prevalence of developmental dysplasia of the hip andcongenital hip dislocation is still high in Mongolia. Therefore, number of diagnosis with congenital hipdislocation has rapidly increased in the recent 2 years.
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In order to investigate the effects of temperature and ionic strength on the N-B-transition and the alkaline denaturation of the human serum albumin, the pH-dependences of fluorescence position and relative yield of Trp-24 and of protein bound dye ANS were measured. The measurements were carried out at temperatures from 10 to 45 degrees C and ionic strengths (NaCl) from 0.001 to 0.2. The pH-induced structural transitions have different realization in environments of tryptophanyl and tightly bound ANS. The alkaline denaturation does not change the Trp-214 fluorescence. The N-B-transition gives rise to the slight polarity and/or mobility lowering in the Trp-214 environment (the shorter-wave-length spectral shift). Increase in the temperature and ionic strength induces the shift of the transition midpoint from ca. 8 to 8.7 and reduces the spectral shift amplitude. At low ionic strengths, the new structural transition in the Trp-214 environment is observed at pH change from 6.7 to 5.7. This transition is not observable using ANS fluorescence. The N-B-transition is accompanied by an enhancement and longer-wavelength shift of the ANS fluorescence spectra. The transition midpoint is independent of temperature, but is shifted to lower pH values at a decrease of ionic strength value. At ionic strengths less than or equal to 0.01 the shorter-wavelength spectral shift is seen at pH from 7.5 to 9, which seems to reflect the disulfide B-A-isomerisation. The alkaline denaturation gives rise to the sharp quenching of ANS fluorescence, probably due to the ANS binding site decomposition.(ABSTRACT TRUNCATED AT 250 WORDS)
Asunto(s)
Albúmina Sérica/análisis , Naftalenosulfonatos de Anilina , Colorantes Fluorescentes , Humanos , Concentración de Iones de Hidrógeno , Conformación Proteica , Espectrometría de FluorescenciaRESUMEN
Using fluorescence parameters of tryptophanyl and bound ANS, the acid-induced structural transitions of defatted monomeric human serum albumin were measured as pH-dependences from 6 to 2.5 in the wide range of temperature (10 to 45 degrees C) and ionic strength (from 0.001 to 0.2 M NaCl or 0.067 M Na2SO4). Temperature rise and decrease in ionic strength value result in the splitting of the N-F-transition onto two stages, N-F1 and F1-F2. The N-F1-transition is accompanied by the blue shift of tryptophanyl and ANS fluorescence spectra and increase in the ANS emission yield. The F1-F2-stage is manifested in an additional blue spectral shift and a sharp drop of the ANS emission yield, which is shown to be due to the lowering of albumin affinity for the dye. In the acidic-extension stage (F2-E), the spectra undergo a red shift which means that the nanosecond dipole relaxation of protein groups and bound water becomes faster. In the F2 from, the albumin affinity for ANS is significantly lowered; the association constant of the primary binding site is lower by an order of quantity and two secondary sites are practically disappeared. The complex effect of temperature, ionic strength and pH changes on the properties of ANS-binding sites is considered as a model of possible control influences of these factors upon the albumin transport of amphiphilic anions in organism.
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Albúmina Sérica , Sitios de Unión , Colorantes Fluorescentes , Humanos , Concentración de Iones de Hidrógeno , Técnicas In Vitro , Concentración Osmolar , Conformación Proteica , TemperaturaRESUMEN
In order to investigate effects of temperature in the physiological range (from 10 to 50 degrees C) on structural, physical and functional properties of the N-form of human serum albumin (HSA), the temperature dependences of fluorescence parameters of Trp-214 residue of HSA and of the specifically bound dye ANS, as well as of association constants of ANS binding in the primary and secondary binding sites on HSA molecule were measured. The temperature-induced changes of these properties of HSA are essentially dependent on pH (7.0 or 5,6) and ionic strength (0.001-0.008 or 0.2 M NaCl). At pH 7.0 and 0.2 M NaCl the environment of Trp-214 remained invariant at temperature changes between 10 and 50 degrees C. On the other hand, the affinity to ANS of a primary binding site doubled and that of secondary ones halved. These affinity changes seem to be due, are least partly, to the heating-induced dissociation of Cl-ions, which are inhibitors of the primary dye binding. By lowering pH (to 5.6) and ionic strength the temperature-induced changes in the Trp-214 environment were observed. The changes are interpreted as indole group transition into the buried region, inaccesible to water (the "closing" of a structural slit). The affinity of secondary binding sites of ANS was halved.
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Albúmina Sérica/metabolismo , Temperatura , Naftalenosulfonatos de Anilina/metabolismo , Sitios de Unión , Cristalización , Fluorescencia , Humanos , Concentración de Iones de Hidrógeno , Técnicas In Vitro , Unión ProteicaRESUMEN
The effect of ionic strength on the 1-anilino-8- naphtalene sulfonate (ANS) binding sites of the N-form of human serum albumin (HSA) was studied by means of the protein and ligand fluorescence. The parameters of the binding of ANS to HSA (the number of sites and the binding constants) were determined by two methods: by measuring the ANS fluorescence either (i) at increasing protein concentrations and constant ANS concentration, or (ii) at increasing ANS concentration and two constant protein concentrations (9.6 and 2.53 microM). An increase in the NaCl concentration results in a monotonous decrease of the ANS fluorescence yield of HSA-ANS complex, which could be interpreted in terms of two different effects: first, the direct collisional quenching interaction of Cl-ions with bound ANS located on the surface of HSA and, second, the ca. 10 per cent decrease of the number of bound ANS molecules due to the lowering of the ANS-HSA association constant values. The fluorimetric titration showed that at low ionic strength (0.008 M NaCl) HSA molecule has one strong ( lgKaI = 6.75-7.25) and two secondary sites with lower affinity ( lgKaII = 6.35). The increase in the NaCl concentration results in a decrease of the affinity for both kinds of binding sites (in 0.2 NaCl lgKaI = 6.3-6.7; lgKaII = 5.6-5.9). In contrast with NaCl, Na2SO4 induces only a limited decrease of the ANS fluorescence occurring within a narrow concentration range (from ca. 0.02 to 0.05 M Na2SO4, e. i. at ionic strengths from 0.07 to 0.15) and which can be described as a cooperative interaction of six SO4(2)-ions with a HSA molecule.(ABSTRACT TRUNCATED AT 250 WORDS)