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1.
Braz. j. med. biol. res ; 47(3): 179-191, 03/2014. tab, graf
Article Dans Anglais | LILACS | ID: lil-704624

Résumé

The isolation of heat-stable enterotoxin (STa) from Escherichia coli and cholera toxin from Vibrio cholerae has increased our knowledge of specific mechanisms of action that could be used as pharmacological tools to understand the guanylyl cyclase-C and the adenylyl cyclase enzymatic systems. These discoveries have also been instrumental in increasing our understanding of the basic mechanisms that control the electrolyte and water balance in the gut, kidney, and urinary tracts under normal conditions and in disease. Herein, we review the evolution of genes of the guanylin family and STa genes from bacteria to fish and mammals. We also describe new developments and perspectives regarding these novel bacterial compounds and peptide hormones that act in electrolyte and water balance. The available data point toward new therapeutic perspectives for pathological features such as functional gastrointestinal disorders associated with constipation, colorectal cancer, cystic fibrosis, asthma, hypertension, gastrointestinal barrier function damage associated with enteropathy, enteric infection, malnutrition, satiety, food preferences, obesity, metabolic syndrome, and effects on behavior and brain disorders such as attention deficit, hyperactivity disorder, and schizophrenia.


Sujets)
Animaux , Toxines bactériennes/génétique , Entérotoxines/génétique , Protéines Escherichia coli/génétique , Hormones gastrointestinales/génétique , Guanylate cyclase/physiologie , Peptides natriurétiques/génétique , Équilibre hydroélectrolytique/physiologie , Adenylate Cyclase/physiologie , Toxines bactériennes/isolement et purification , Évolution moléculaire , Entérotoxines/isolement et purification , Protéines Escherichia coli/isolement et purification , Escherichia coli/métabolisme , Escherichia coli/pathogénicité , Prévision , Guanylate cyclase/usage thérapeutique , Mammifères/physiologie , Peptides/métabolisme , Transduction du signal/physiologie
2.
Chinese Journal of Immunology ; (12)2000.
Article Dans Chinois | WPRIM | ID: wpr-541579

Résumé

Objective:To detection antibody against heat-stable enterotoxin by fusion protein.Methods:Mutant heat-stable enterotoxin precursor gene was ligated in vector pGEX-4T-2 to inductively express as a fusion protein GST/proST_m with glutathione S-transferase(GST).To investigate the antigenic action,serum and fecal antibodies against heat-stable enterotoxin was detected with this fusion protein.Results:The fusion protein was a about 32 kD protein.All the samples contain the antibody against ST.Conclusion:Such strategy was a promising method to detect antibody against heat-stable enterotoxin.

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