Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Más filtros

Banco de datos
Tipo del documento
Asunto de la revista
Intervalo de año de publicación
1.
Biochim Biophys Acta Mol Cell Res ; 1868(9): 119073, 2021 08.
Artículo en Inglés | MEDLINE | ID: mdl-34062155

RESUMEN

The Endoplasmic Reticulum (ER) is responsible for the folding and post-translational modification of secretory proteins, as well as for triaging misfolded proteins. During folding, there is a complex yet only partially understood interplay between disulfide bond formation, which is an enzyme catalyzed event in the oxidizing environment of the ER, along with other post-translational modifications (PTMs) and chaperone-supported protein folding. Here, we used the glycoprotein torsinA as a model substrate to explore the impact of ER redox homeostasis on PTMs and protein biogenesis. TorsinA is a AAA+ ATPase with unusual oligomeric properties and controversial functions. The deletion of a C-terminal glutamic acid residue (∆E) is associated with the development of Early-Onset Torsion Dystonia, a severe movement disorder. TorsinA differs from other AAA+ ATPases since it is an ER resident, and as a result of its entry into the ER torsinA contains two N-linked glycans and at least one disulfide bond. The role of these PTMs on torsinA biogenesis and function and the identity of the enzymes that catalyze them are poorly defined. Using a yeast torsinA expression system, we demonstrate that a specific protein disulfide isomerase, Pdi1, affects the folding and N-linked glycosylation of torsinA and torsinA∆E in a redox-dependent manner, suggesting that the acquisition of early torsinA folding intermediates is sensitive to perturbed interactions between Cys residues and the quality control machinery. We also highlight the role of specific Cys residues during torsinA biogenesis and demonstrate that torsinA∆E is more sensitive than torsinA when these Cys residues are mutated.


Asunto(s)
Adenosina Trifosfatasas/metabolismo , Homeostasis , Proteínas de Saccharomyces cerevisiae/metabolismo , Adenosina Trifosfatasas/química , Retículo Endoplásmico/metabolismo , Glicosilación , Modelos Moleculares , Oxidación-Reducción , Procesamiento Proteico-Postraduccional , Proteínas de Saccharomyces cerevisiae/química
2.
J Dermatol Sci ; 98(1): 2-12, 2020 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-32192826

RESUMEN

Stevens-Johnson syndrome and toxic epidermal necrolysis (SJS/TEN) are potentially life-threatening, immune-mediated adverse reactions characterized by widespread erythema, epidermal necrosis, and detachment of skin and mucosa. Efforts to grow and develop functional international collaborations and a multidisciplinary interactive network focusing on SJS/TEN as an uncommon but high burden disease will be necessary to improve efforts in prevention, early diagnosis and improved acute and long-term management. SJS/TEN 2019: From Science to Translation was a 1.5-day scientific program held April 26-27, 2019, in Vancouver, Canada. The meeting successfully engaged clinicians, researchers, and patients and conducted many productive discussions on research and patient care needs.


Asunto(s)
Necesidades y Demandas de Servicios de Salud/organización & administración , Grupo de Atención al Paciente/organización & administración , Síndrome de Stevens-Johnson/terapia , Congresos como Asunto , Carga Global de Enfermedades , Salud Global , Humanos , Cooperación Internacional , Farmacogenética/organización & administración , Sistema de Registros/estadística & datos numéricos , Síndrome de Stevens-Johnson/epidemiología , Síndrome de Stevens-Johnson/etiología , Investigación Biomédica Traslacional/organización & administración
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA