RESUMEN
We aimed to assess whether speech recognition scores (SRS) are predictive of outcomes in patients with small vestibular schwannoma (VS) undergoing observation. Ninety-five patients with VS whose initial management was observation with serial imaging were retrospectively analysed. Patients were divided into groups according to their average hearing level and SRS at diagnosis. About 60% of patients had good initial SRS (GIS) and 40% had poor initial SRS (PIS). Mean follow-up was 44 months, during which time data were collected regarding hearing level, tumour growth and the eventual management option (continued or failed observation). Observation was discontinued by 24% (23/95) of patients. GIS-patients were more likely to maintain stable hearing than those with PIS (p<0.05). Hearing was stable in 73% (64/87) of patients. These findings indicate that patients with PIS are more vulnerable to progressive hearing loss than those with GIS. Observation may be a suitable management option for all patients with small VS, particularly those with GIS.
Asunto(s)
Trastornos de la Memoria/etiología , Neuroma Acústico/complicaciones , Neuroma Acústico/diagnóstico , Patrones de Reconocimiento Fisiológico/fisiología , Percepción del Habla/fisiología , Estimulación Acústica/métodos , Adulto , Anciano , Anciano de 80 o más Años , Audiometría de Tonos Puros/métodos , Distribución de Chi-Cuadrado , Femenino , Estudios de Seguimiento , Humanos , Imagen por Resonancia Magnética , Masculino , Trastornos de la Memoria/diagnóstico , Persona de Mediana Edad , Valor Predictivo de las Pruebas , Pronóstico , PsicoacústicaRESUMEN
In a new group of polypeptides, the branches were composed of DL-Ala oligopeptide, L-serine and L-leucine or L-glutamic acid residues. The synthesis of eight different side-chain combinations is described. In the first group, Ser was attached directly to the epsilon-amino groups of polylysine, and Leu or Glu was situated at the side chain end (poly[Lys(X(i)-DL-Ala(m)-Ser(j))]). Alternatively, Leu or Glu was positioned next to the polylysine backbone (poly[Lys(Ser(j)-DL-Ala(m)-X(i))], where X=L-Leu or L-Glu and m approximately 3-6, i=1 and j=1). The second group of polymers was synthesised by grafting oligo(DL-alanine) chains to the epsilon-amino groups of polylysine, followed by coupling of Ser and Leu or Glu consecutively to the chain ends, however, in a different order, resulting in the polymers (poly[Lys(X(i)-Ser(j)-DL-Ala(m))] and poly[Lys(Ser(j)-X(i)-DL-Ala(m))], where X=L-Leu or L-Glu and m approximately 3-6, i=1 and j=1). The effect of amino-acid composition and sequence of side chains in branched polypeptides on solution conformation was studied by CD spectroscopy. CD spectra recorded in aqueous solutions of various pH (2-11) and ionic strengths (0.02-2.0 M NaCl) suggest that leucine- and serine-containing polypeptides have more ordered (alpha-helical) structure than the polymers with glutamic acid and serine residues in the same position. The influence of serine residues on ordered structure (helical or beta-sheet) formation depends on its position in the side chain as well as on the nature of amino acid X (Leu or Glu). The incorporation of Ser into the branches resulted in polypeptides possessing prolonged shelf stability and high water-solubility. No toxic effect of this new class of polymers was observed on mouse spleen cells, even after 4 h of incubation.