ABSTRACT
Las personas con Trastorno del Espectro Autista (TEA) tienen características únicas y hay una falta de conocimiento sobre cómo estas características podrían influir en sus familias y en el ajuste conductual, emocional y social de sus hermanos. El presente estudio tiene el objetivo de centrarse en los hermanos de estas personas con TEA y realizar una revisión teórica relacionada con el ajuste conductual, emocional y social de hermanos de niños con TEA. Un total de 24 artículos han sido incluidos y analizados con el fin de encontrar resultados relevantes que puedan ayudar a entender las necesidades de estos hermanos. El estudio sugiere, en ocasiones, resultados diferentes pero identifica aquellos factores de riesgo que podrían impactar en el núcleo familiar y, principalmente, en los hermanos de niños con TEA
Many individuals with an Autism Spectrum Disorder (ASD) have unique characteristics and very little is known about how these characteristics may influence the family and the behavioural, social and emotional adjustment of their siblings. The purpose of the current study is to focus on the siblings and to review the literature related to the behavioural, social and emotional adjustment of siblings of individuals with ASD. We have identified and analysed 24 articles to find the relevant results that may help us to understand the needs of these siblings. The findings suggest mixed results or outcomes but they also bring to light a number of risk factors that could have an impact on the entire family and particularly on the siblings of children with ASD
Subject(s)
Child , Humans , Adaptation, Psychological , Autistic Disorder/psychology , Siblings/psychology , Sibling Relations , Child Development Disorders, Pervasive/psychology , Severity of Illness IndexABSTRACT
Glucosidase I is an endoplasmic reticulum (ER) type II membrane enzyme that cleaves the distal alpha1,2-glucose of the asparagine-linked GlcNAc2-Man9-Glc3 precursor. To identify sequence motifs responsible for ER localization, we prepared a protein chimera by transferring the cytosolic and transmembrane domain of glucosidase I to the luminal domain of Golgi-Man9-mannosidase. The GIM9 hybrid was overexpressed in COS 1 cells as an ER-resident protein that displayed alpha1,2-mannosidase activity, excluding the possibility that the glucosidase I-specific domains interfere with folding of the Man9-mannosidase catalytic domain. After substitution of the Args in position 7, 8, or 9 relative to the N-terminus by leucine, the GIM9 mutants were transported to the cell surface indicating that the (Arg)3 sequence functions as an ER-targeting motif. Cell surface expression was also observed after substitution of Arg-7 or Arg-8 but not Arg-9 in GIM9 by either lysine or histidine. Thus the side chain structure, including its positive charge, appears to be essential for signal function. Analysis of the N-linked glycans suggests that the (Arg)3 sequence mediates ER localization through Golgi-to-ER retrograde transport. Glucosidase I remained localized in the ER after truncation or mutation of the N-terminal (Arg)3 signal, in contrast to comparable GIM9 mutants. ER localization was also observed with an M9GI chimera consisting of the cytosolic and transmembrane domain of Man9-mannosidase and the glucosidase I catalytic domain. ER-specific targeting information must therefore be provided by sequence motifs contained within the glucosidase I luminal domain. This structural information appears to direct ER localization by retention rather than by retrieval, as concluded from N-linked Man9-GlcNAc2 being the major glycan released from the wild-type enzyme.
