RESUMEN
The use of a removable partial denture to restore the posterior edentulous space continues to be a viable treatment option for patients who are not candidates for cantilevered fixed prostheses or dental implants because of the nature of the remaining teeth and bony support, the anatomy of the residual ridges, or financial constraints. The purpose of this paper is to introduce an alternative technique for the fabrication of a well-fitting distal extension RPD that will take maximum advantage of the dual nature of the support provided by the teeth and the resilient tissues of the residual ridge.
Asunto(s)
Técnica de Colado Dental , Diseño de Dentadura/métodos , Dentadura Parcial Removible , Resinas Acrílicas , Técnica de Impresión Dental , Bases para Dentadura , Alineadores Dentales , Humanos , Arcada Parcialmente Edéntula/rehabilitación , MandíbulaRESUMEN
This study investigated the incidences of undercarboxylated (protein induced by vitamin K absence: PIVKA) prothrombin and protein C in 496 neonates across a wide range of gestational ages. These findings are related to vitamin K1 levels (an indicator of cofactor availability) and vitamin K1 epoxide levels (a measure of the efficiency of the hepatic vitamin K cycle). PIVKA protein C was present in at least trace amounts in 27% of infants; whereas, PIVKA prothrombin was present in 7% of infants. PIVKA prothrombin and protein C were present at high plasma concentrations in 2% to 3% of term and preterm neonates and both PIVKA protein C and prothrombin increased with gestational age. Despite elevated plasma concentrations of PIVKA protein C and diminished levels of normally carboxylated protein C, clinical thrombosis was not observed. The mean (+/- SD) vitamin K1 level in the study population was 0.009 +/- 0.02 nmol/L (adult reference interval: 0.3 to 2.6 nmol/L) with no clear relationship between vitamin K1 levels and production of PIVKA protein C or prothrombin. By comparison with adults, the epoxide form of the vitamin comprised an abnormally high proportion of total vitamin K1; this suggests possible inefficiencies in hepatic reductase cycling.
Asunto(s)
Biomarcadores , Recien Nacido Prematuro/sangre , Proteína C/metabolismo , Precursores de Proteínas , Protrombina/análogos & derivados , Vitamina K 1/sangre , Sangre Fetal/metabolismo , Edad Gestacional , Humanos , Recién Nacido , Protrombina/metabolismo , Vitamina K 1/análogos & derivadosRESUMEN
The anticoagulant factor Protein S circulates in two major forms, free and bound to C4b binding protein (C4BP). We report a monoclonal antibody-based enzyme-linked immunosorbent assay of human Protein S that is sensitive (detection limit 30 ng) and free of notable competition from other vitamin K-dependent proteins. We demonstrate assay sensitivity to Protein S-C4BP complex, as well as to free Protein S by (a) results of immunoaffinity chromatography involving the assay antibody; (b) parallelism between the standard curve and a plasma dilution curve, including dilutions greater than 100-fold; (c) lack of effect of added C4BP on Protein S values; and (d) reactivity in the assay by high-molecular-mass plasma Protein S in gel permeation studies. These latter studies also indicate that uncomplexed Protein S has an apparent molecular mass of approximately 150,000 Da, attributable to either polymerization or conformational considerations. Inter- and intra-assay CVs were 9.8% and 5.1%, respectively, and 90% of Protein S added to plasma was recovered. Reference ranges (mean and SD) for total Protein S in middle-aged normal subjects were 16.6 (1.9) mg/L for men (n = 54) and 16.0 (3.0) mg/L for women (n = 38). In the polyethylene glycol precipitation method, the reference values for free Protein S were 5.4 (1.6) mg/L for men and 4.4 (1.1) mg/L for women.