Efecto de ajuste del flujo dializante (Qd) sobre la eficacia en hemodialisis a pacientes de bajo peso

Introducción: Las guías KDOQI del 2006 utilizan patrón de adecuación de diálisis el Kt/V, donde V es volumen de distribución de la úrea, pacientes de bajo peso tienen menor agua corporal total, menor V, que podrían reducir el requerimiento de Qd sin afectar la eficiencia de la diálisis. Objetivo: Evaluar el efecto sobre la adecuación de hemodiálisis que produce la reducción del Qd en pacientes con peso menor o igual a 60 kg . Metodología: Se incluyeron pacientes con Enfermedad Renal crónica en hemodiálisis de forma regular con peso menor o igual a 60 Kg de la unidad renal, para evaluar dos períodos I y II, se continuaron los parámetros de la terapia, con descenso del Qd para el segundo período . Las variables fueron recolectadas de forma directa por los investigadores de la historia clínica . Los valores así obtenidos serían comparados mediante prueba t para variables relacionadas o pareadas, y significancia estadística de la prueba inferior a 0,05. Resultados: Se incluyeron 61 pacientes, el 60.7% sexo femenino, promedio de edad 57,3 años (DE 14,8). Edad promedio de los hombres 60,1 (DE 13,9) y de las mujeres fue de 55,9 (DE 15,4). No se encontraron diferencias estadísticamente significativas para las variables Kt/V y Hb, con descenso significativo del P. (p 0.015) Conclusiones: Este estudio demuestra que se logra una adecuada terapia con Qd inferiores a los estándares tradicionales, con 400ml /min en pacientes de bajo peso, siempre y cuando se mantengan los demás parámetros de suplencia renal.

"A Sequence in Subdomain 2 of DBL1a of Plasmodium falciparum Erythrocyte Membrane Protein 1 Induces Strain Transcending Antibodies"

Immunity to severe malaria is the first level of immunity acquired to Plasmodium falciparum. Antibodies to the variant antigen PfEMP1 (P. falciparum erythrocyte membrane protein 1) present at the surface of the parasitized red blood cell (pRBC) confer protection by blocking microvascular sequestration. Here we have generated antibodies to peptide sequences of subdomain 2 of PfEMP1-DBL1a previously identified to be associated with severe or mild malaria. A set of sera generated to the amino acid sequence KLQTLTLHQVREYWWALNRKEVWKA, containing the motif ALNRKE, stained the live pRBC. 50% of parasites tested (7/14) were positive both in flow cytometry and immunofluorescence assays with live pRBCs including both laboratory strains and in vitro adapted clinical isolates. Antibodies that reacted selectively with the sequence REYWWALNRKEVWKA in a 15-mer peptide array of DBL1a-domains were also found to react with the pRBC surface. By utilizing a peptide array to map the binding properties of the elicited anti-DBL1a antibodies, the amino acids WxxNRx were found essential for antibody binding. Complementary experiments using 135 degenerate RDSM peptide sequences obtained from 93 Ugandan patient-isolates showed that antibody binding occurred when the amino acids WxLNRKE/D were present in the peptide. The data suggests that the ALNRKE sequence motif, associated with severe malaria, induces strain-transcending antibodies that react with the pRBC surface

A sequence in subdomain 2 of DBL1 alpha of plasmodium falciparum erythrocyte membrane protein 1 induces strain transcending antibodies

Immunity to severe malaria is the first level of immunity acquired to Plasmodium falciparum. Antibodies to the variant antigen PfEMP1 (P. falciparum erythrocyte membrane protein 1) present at the surface of the parasitized red blood cell (pRBC) confer protection by blocking microvascular sequestration. Here we have generated antibodies to peptide sequences of subdomain 2 of PfEMP1-DBL1 alpha previously identified to be associated with severe or mild malaria. A set of sera generated to the amino acid sequence KLQTLTLHQVREYWWALNRKEVWKA, containing the motif ALNRKE, stained the live pRBC. 50% of parasites tested (7/14) were positive both in flow cytometry and immunofluorescence assays with live pRBCs including both laboratory strains and in vitro adapted clinical isolates. Antibodies that reacted selectively with the sequence REYWWALNRKEVWKA in a 15-mer peptide array of DBL1 alpha-domains were also found to react with the pRBC surface. By utilizing a peptide array to map the binding properties of the elicited anti-DBL1 alpha antibodies, the amino acids WxxNRx were found essential for antibody binding. Complementary experiments using 135 degenerate RDSM peptide sequences obtained from 93 Ugandan patient-isolates showed that antibody binding occurred when the amino acids WxLNRKE/D were present in the peptide. The data suggests that the ALNRKE sequence motif, associated with severe malaria, induces strain-transcending antibodies that react with the pRBC surface.