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1.
Rev. gastroenterol. Perú ; 32(2): 134-140, abr.-jun. 2012. tab, graf, ilus
Artículo en Español | LILACS, LIPECS | ID: lil-661407

RESUMEN

INTRODUCCIÓN: La enfermedad celiaca (EC) es una condición en la que la ingesta de gluten desencadena una respuesta de autoinmunidad que genera aplanamiento de las vellosidades intestinales causando malabsorción. La prevalencia mundial es de aproximadamente 1%. En nuestro país no es conocida MATERIALES Y MÉTODOS: Estudio retrospectivo, descriptivo y observacional realizado en la Clínica Angloamericana entre Septiembre del 2004 y Febrero 2012. Se revisaron las historias clínicas, reportes endoscópicos y reportes de biopsias duodenales de los pacientes con anti Transglutaminasa tisular (TTG) positiva, mayores de 18 años. Resultados: Se estudiaron 39 casos, siendo 26 (66.7%) mujeres y 13 (33.3%) varones. La edad media de diagnóstico fue 61.25 años. Los síntomas fueron diarrea crónica en 32 (82.1%), dolor abdominal en 22 (56.4%), distensión abdominal en 14 (35.9%) y otros en menor frecuencia. Ocho (20.5%) pacientes presentaron anemia. Solo 5 (12.8%) pacientes presentaron hallazgos endoscópicos compatibles con EC. La clasificación Marsh de las biopsias duodenales fueron 0: 5 (12.7%), I: 1 (2.6%), II: 0 (0%), III A: 20 (51.3%), III B: 12 (30.8%) y III C: 1 (2.6%). CONCLUSIONES: La EC debe ser considerada como diagnóstico diferencial de pacientes con síntomas gastrointestinales inespecíficos de larga data, teniendo en cuenta también sus manifestaciones extraintestinales. Para el diagnóstico debe utilizarse la anti TTG como prueba inicial y posteriormente realizar una biopsia duodenal para estadiaje.


BACKGROUND: Celiac disease (CD) is a condition in which gluten intake develops an autoimmune response genetaring intestinal villous atrophy, causing malabsorption. Prevalence worlwide is approximately 1%, in our country it is not known. MATERIAL AND METHODS: Retrospective, descriptive, observational study in Anglo American Clinic between September 2004 and February 2012. We reviewed the medical charts, upper Gl endoscopy reports and duodenal biopsy reports of all patients with positive anti TTG results, who were older than 18 years of age. RESULTS: We studied 39 cases, 26 (66.7%) women and 13 (33.3%) men. Mean age was 61.25 years. The symptoms were chronic diarrhea in 32 (82.1%), abdominal pain in 22 (56.4%), abdominal distention in 14 (35.9%), and others in lower frequency. Eight (20.5%) patients had anemia. Just 5 (12.8%) had upper endoscopy findings consistent with CD, and Marsh classification was: 0: 5 (12.7%), l: 1 (2.6%), ll: 0 (0%), llll A: 20 (51.3%), lll B: 12 (30.8%) y lll C: 1 (2.6%). CONCLUSIONS: CD should be considered as a differential diagnosis of patients with non-specific-long-term gastrointestinal symptoms, extraintestinal symptoms should also be taken into account. Diagnosis should be made with anti TTG as the initial test and posteriorly with a duodenal biopsy for staging.


Asunto(s)
Humanos , Enfermedad Celíaca , Glútenes , Transglutaminasas/antagonistas & inhibidores , Epidemiología Descriptiva
2.
Artículo en Inglés | MEDLINE | ID: mdl-16153866

RESUMEN

A clotting protein (CP) was purified from the plasma of the pink shrimp Farfantepenaeus paulensis by sequential anion-exchange chromatography. The shrimp CP was able to form stable clots in vitro in the presence of hemocyte lysate and Ca2+, suggesting that the clotting reaction is catalyzed by a Ca2+-dependent transglutaminase present in shrimp hemocytes. Dansylcadaverine was incorporated into the shrimp CP in the presence of endogenous transglutaminase (hemocyte lysate), confirming that the shrimp purified CP is the substrate for the transglutaminase enzyme. The molecular mass of the CP was determined by gel filtration to be 341 kDa and 170 kDa by SDS-PAGE under reducing conditions. These results suggest that the shrimp CP consists of two identical subunits, covalently linked by disulphide bonds. The amino acid sequence at the N-terminus was 100% identical to that of the penaeids Litopenaeus vannamei and Penaeus monodon and 66% to 80% identical to the CPs of other decapods. This is the first report of a CP characterization in an Atlantic penaeid species. Further studies, including a molecular cloning approach would enable to detect which tissues express the gene of the clotting protein. It would be also useful to understand the mechanism by which the coagulation time is delayed in shrimps under stress conditions.


Asunto(s)
Coagulación Sanguínea/fisiología , Proteínas Sanguíneas , Lipoproteínas , Penaeidae/metabolismo , Secuencia de Aminoácidos , Animales , Proteínas Sanguíneas/química , Proteínas Sanguíneas/genética , Proteínas Sanguíneas/aislamiento & purificación , Proteínas Sanguíneas/metabolismo , Cadaverina/análogos & derivados , Cadaverina/metabolismo , Femenino , Colorantes Fluorescentes/metabolismo , Lipoproteínas/química , Lipoproteínas/genética , Lipoproteínas/aislamiento & purificación , Lipoproteínas/metabolismo , Masculino , Datos de Secuencia Molecular , Peso Molecular , Subunidades de Proteína/química , Subunidades de Proteína/genética , Subunidades de Proteína/aislamiento & purificación , Subunidades de Proteína/metabolismo , Alineación de Secuencia , Transglutaminasas/antagonistas & inhibidores , Transglutaminasas/metabolismo
3.
Biotechnol Appl Biochem ; 37(Pt 3): 295-9, 2003 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-12529180

RESUMEN

A new microbial transglutaminase (EC 2.3.2.13) from a Bacillus circulans strain isolated from the aquatic Amazonian environment was purified and characterized. Enzyme purification started with (NH(4))(2)SO(4) 'salting out' and proceeded with liquid chromatography on Q-Sepharose FF and octyl-Sepharose 4 FF. The purification factor was approx. 150-fold with a yield of 32%. The enzyme's molecular mass was estimated as 45000 Da on SDS/PAGE. The purified transglutaminase had an optimum temperature of 47 degrees C, the optimum pH of the reaction was 7 and it presented no calcium-dependent activity.


Asunto(s)
Bacillus/química , Reactores Biológicos , Cromatografía/métodos , Transglutaminasas/química , Transglutaminasas/aislamiento & purificación , Bacillus/enzimología , Brasil , Calcio/química , Activación Enzimática , Estabilidad de Enzimas , Concentración de Iones de Hidrógeno , Cinética , Especificidad de la Especie , Temperatura , Teprotido , Transglutaminasas/antagonistas & inhibidores , Transglutaminasas/biosíntesis
4.
Arch Microbiol ; 164(3): 186-93, 1995 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-7545385

RESUMEN

Activity of the enzyme glutaminyl-peptide--glutamylyl-transferase (EC 2.3.2.13; transglutaminase), which forms the interpeptidic cross-link N epsilon-(gamma-glutamic)-lysine, was demonstrated in cell-free extracts obtained from both the yeast like and mycelial forms of Candida albicans. Higher levels of enzymatic activity were observed in the cell wall fraction, whereas the cytosol contained only trace amounts of activity. Cystamine, a highly specific inhibitor of the enzyme, was used to analyze a possible role of transglutaminase in the organization of the cell wall structure of the fungus. Cystamine delayed protoplast regeneration and inhibited the yeast-to-mycelium transition and the incorporation of proteins into the cell wall. The incorporation of covalently bound high-molecular-weight proteins into the wall was sensitive to cystamine. Proteic epitopes recognized by two monoclonal antibodies, one of which is specific for the mycelial walls of the fungus, were also sensitive to cystamine. These data suggest that transglutaminase may be involved in the formation of covalent bonds between different cell wall proteins during the final assembly of the mature cell wall.


Asunto(s)
Candida albicans/enzimología , Proteínas Fúngicas/metabolismo , Transglutaminasas/metabolismo , Anticuerpos Antifúngicos/inmunología , Anticuerpos Monoclonales/inmunología , Antígenos Fúngicos/análisis , Candida albicans/efectos de los fármacos , Candida albicans/ultraestructura , Pared Celular/inmunología , Pared Celular/metabolismo , Cistamina/farmacología , Epítopos/análisis , Proteínas Fúngicas/biosíntesis , Proteínas Fúngicas/inmunología , Peso Molecular , Protoplastos/enzimología , Protoplastos/fisiología , Transglutaminasas/antagonistas & inhibidores
5.
Int J Immunopharmacol ; 10(5): 555-61, 1988.
Artículo en Inglés | MEDLINE | ID: mdl-2903131

RESUMEN

The effect of different amines on antibody-dependent cellular cytotoxicity (ADCC) activity of human mononuclear cells was tested. Whereas monocyte cytotoxic capacity was significantly stimulated in the presence of methylamine (MA), dansylcadaverine (DC) and glycine ethylester (GEE), lymphocyte ADCC was markedly suppressed by these agents. The pharmacological actions of these compounds in our system are not related to their ability to inhibit transglutaminase (TGase) enzymes, since tertiary amines such as sarcosine ethylester (SEE) and chloroquine (CQ) elicited identical responses to MA, DC and GEE. The calmodulin (CAM) inhibitors trifluoperazine (TFP) and the more specific N-(6-aminohexyl)-5-chloro-1-naphtalene sulfonamide (W-7) [Hidaka, Sasaki, Tanaka, Endo, Ohno, Fujii & Nagata (1981) Proc. natn. Acad. Sci. U.S.A., 78, 4353-4357] mimicked the effects of amines on ADCC, suggesting the possibility that a CAM-regulated process might be involved in the functional changes provoked by amines on ADCC. Finally, binding of 125I-immune complexes to the effector cells in the presence of amines showed lack of correlation between alterations in ADCC capacity and Fc gamma R expression.


Asunto(s)
Aminas/farmacología , Citotoxicidad Celular Dependiente de Anticuerpos/efectos de los fármacos , Linfocitos/efectos de los fármacos , Monocitos/efectos de los fármacos , Antígenos de Diferenciación , Calcio/metabolismo , Calmodulina/antagonistas & inhibidores , Humanos , Técnicas In Vitro , Linfocitos/inmunología , Linfocitos/metabolismo , Monocitos/inmunología , Monocitos/metabolismo , Receptores Fc , Receptores de IgG , Transglutaminasas/antagonistas & inhibidores
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