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1.
Clin Rev Allergy Immunol ; 57(1): 74-82, 2019 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-30171460

RESUMEN

Over the past few years, the rates of food allergies have dramatically increased. As a result, the lives of patients and their caregivers have been dramatically altered. While most attention surrounding food allergies has focused on treatment, less consideration has been given to the mental health ramifications of living with this condition, among them depression, anxiety, post-traumatic stress, being bullied, and an overall poorer quality of life. At the same time, patients' family lives are often disrupted. Parents of food-allergic children, especially mothers, report anxiety, depression, and a decreased quality of life. Indeed, mental health issues associated with food allergies are likely underrecognized. In this review, we describe not only the psychosocial impacts of food allergies but also survey treatments that can be used to address this burgeoning problem. Interventions include educating members of the greater community about food allergies, camps for food allergic children, and support groups for parents. For physicians, treatment options consist of oral challenges, proximity challenges, oral immunotherapy, and cognitive behavioral therapy. Although the existing research is built on an already strong foundation, ultimately more studies are needed to deepen our understanding of the relationship between food allergies and mental health.


Asunto(s)
Hipersensibilidad a los Alimentos/epidemiología , Hipersensibilidad a los Alimentos/psicología , Calidad de Vida , Adolescente , Adulto , Ansiedad , Acoso Escolar , Cuidadores/psicología , Niño , Depresión , Familia/psicología , Hipersensibilidad a los Alimentos/prevención & control , Hipersensibilidad a los Alimentos/terapia , Humanos , Padres/psicología , Prevalencia
2.
Int J Parasitol ; 34(1): 27-36, 2004 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-14711587

RESUMEN

CD4(+) T cell responses and macrophage activation are essential components of schistosome egg-induced granuloma formation. Previous studies implicated tumour necrosis factor (TNF) as a potential mediator of macrophage recruitment and activation during schistosome infection. Here we demonstrate that signalling by TNF and its receptors can influence granuloma formation, but is ultimately dispensable for granuloma formation in this system. However, we identify a previously unrecognised role for TNF in limiting hepatocellular damage in response to schistosome eggs. Further, we show that this activity of TNF is independent of TNF receptors (TNFR1 and TNFR2). Taken together, these data suggest that additional, as yet unrecognised receptors exist for TNF and that these receptors are capable of mediating important pathological effects in the liver. Finally, we provide evidence that TNF plays an unexpected role in maintaining adult schistosome viability in the portal system.


Asunto(s)
Parasitosis Hepáticas/patología , Hígado/patología , Esquistosomiasis/patología , Factor de Necrosis Tumoral alfa/fisiología , Animales , Apoptosis , Huevos , Femenino , Ligandos , Hígado/parasitología , Circulación Hepática , Parasitosis Hepáticas/inmunología , Masculino , Ratones , Ratones Noqueados , Receptores del Factor de Necrosis Tumoral/metabolismo , Schistosoma/fisiología , Esquistosomiasis/inmunología
3.
Mol Biochem Parasitol ; 131(1): 65-75, 2003 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-12967713

RESUMEN

Peptidases are essential for the establishment and survival of the medically important parasite, Schistosoma mansoni. This helminth expresses a number of gut-associated peptidases that degrade host blood proteins, including hemoglobin, as a means of nutrition. Using irreversible affinity probes, we demonstrate that S. mansoni cathepsin B-like endopeptidase 1 (SmCB1) is the most abundant papain family cysteine peptidase in both the parasite gut and somatic extracts. SmCB1 zymogen (SmCB1pm) was functionally expressed in Pichia pastoris (4-11mgl(-1)). Monospecific and immunoselected antibodies raised against SmCB1pm localized the enzyme exclusively to the gut lumen and surrounding gastrodermis of adult worms. Recombinant SmCB1pm was unable to catalyze its activation, even at low pH. However, recombinant S. mansoni asparaginyl endopeptidase (SmAE), another gut-associated cysteine peptidase, processed and activated SmCB1pm in trans. Consistent with the known specificity of AEs, processing occurred on the carboxyl side of an asparagine residue, two residues upstream of the start of the mature SmCB1 sequence. The remaining pro-region dipeptide was removed by rat cathepsin C (dipeptidyl-peptidase I)-an action conceivably performed by an endogenous cathepsin C in vivo. The activated recombinant SmCB1 is biochemically identical to the native enzyme with respect to dipeptidyl substrate kinetics and pH profiles. Also, the serum proteins, hemoglobin, serum albumin, IgG, and alpha-2 macroglobulin were efficiently degraded. Further, a novel application of an assay to measure the peptidyl carboxypeptidase activity of SmCB1 and other cathepsins B was developed using the synthetic substrate benzoyl-glycinyl-histidinyl-leucine (Bz-Gly-His-Leu). This study characterizes the major digestive cysteine peptidase in schistosomes and defines novel trans-processing events required to activate the SmCB1 zymogen in vitro which may facilitate the digestive process in vivo.


Asunto(s)
Catepsina B/metabolismo , Cisteína Endopeptidasas/metabolismo , Proteínas del Helminto/metabolismo , Proteínas de Plantas/metabolismo , Schistosoma mansoni/enzimología , Activación Transcripcional , Animales , Catepsina B/química , Catepsina B/genética , Mucosa Gástrica/metabolismo , Regulación de la Expresión Génica , Proteínas del Helminto/química , Proteínas del Helminto/genética , Datos de Secuencia Molecular , Pichia/enzimología , Pichia/genética , Schistosoma mansoni/genética , Análisis de Secuencia de ADN , Especificidad por Sustrato
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