Los procesos de internacionalización y globalización en la educación superior: un análisis de los países OCDE.

Resumen del autor. Resumen en castellano e inglés. Este artículo se incluye en el monográfico 'Educación y Deporte'

Intestino médio de larvas de Anticarsia gemmatalis (Hübner) (Lepidoptera: Noctuidae): estudo das células epiteliais ao microscópio de luz e eletrônico

The morphology of the midgut epithelium cells of Anticarsia gemmatalis (Hübner) larvae is described by light and transmission electron microscopy. The midgut of A. gemmatalis is the largest portion of the digestive tract, with three distinct regions: proximal, media and distal. Its wall is formed by pseudostratified columnar epithelial tissue having four cell types: columnar, goblet, regenerative, and endocrine cells. The columnar cells are numerous and long, with the apical portion showing many lengthy microvilli and the basal portion invaginations forming a basal labyrinth. The goblet cells have a large goblet-shaped central cavity delimited by cytoplasmic projections filled with mitochondria. The regenerative cells present electron-dense cytoplasm and few organelles. The endocrine cells are characterized by electron-dense secretory granules, usually concentrated in the cytoplasm basal region.

Unstable argininosuccinate lyase in variant forms of the urea cycle disorder argininosuccinic aciduria.

Loss of function of the urea cycle enzyme argininosuccinate lyase (ASL) is caused by mutations in the ASL gene leading to ASL deficiency (ASLD). ASLD has a broad clinical spectrum ranging from life-threatening severe neonatal to asymptomatic forms. Different levels of residual ASL activity probably contribute to the phenotypic variability but reliable expression systems allowing clinically useful conclusions are not yet available. In order to define the molecular characteristics underlying the phenotypic variability, we investigated all ASL mutations that were hitherto identified in patients with late onset or mild clinical and biochemical courses by ASL expression in human embryonic kidney 293 T cells. We found residual activities >3 % of ASL wild type (WT) in nine of 11 ASL mutations. Six ASL mutations (p.Arg95Cys, p.Ile100Thr, p.Val178Met, p.Glu189Gly, p.Val335Leu, and p.Arg379Cys) with residual activities ≥16 % of ASL WT showed no significant or less than twofold reduced Km values, but displayed thermal instability. Computational structural analysis supported the biochemical findings by revealing multiple effects including protein instability, disruption of ionic interactions and hydrogen bonds between residues in the monomeric form of the protein, and disruption of contacts between adjacent monomeric units in the ASL tetramer. These findings suggest that the clinical and biochemical course in variant forms of ASLD is associated with relevant residual levels of ASL activity as well as instability of mutant ASL proteins. Since about 30 % of known ASLD genotypes are affected by mutations studied here, ASLD should be considered as a candidate for chaperone treatment to improve mutant protein stability.