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1.
GEN ; 67(3): 170-174, sep. 2013.
Article in Spanish | LILACS | ID: lil-702772

ABSTRACT

El cáncer gástrico es la principal causa de muerte por cáncer del estado Táchira - Venezuela. Con una particular elevada tasa de mortalidad en los estados andinos. Los esfuerzos realizados en la detección temprana basados en estudios radiológicos y endoscópicos no han permitido cubrir gran parte de la población. La identificación de lesiones pre malignas y cáncer asociadas a la infección por Helicobacter pylori han obligado al desarrollo de proyectos epidemiológicos de prevención primaria que tiendan a incidir sobre estilos de vida y factores dietéticos. La erradicación de H. pylori con el uso de terapia antimicrobiana convencional ha dado resultados controvertidos en diferentes latitudes, con los mismos esquemas terapéuticos. La capacidad antimicrobiana de diferentes tipos de propóleos ante el H. pylori, ya ha sido evaluada, siendo el principal responsable los flavonoides: pinocembrina, galangina y crisina. La alta prevalencia de H. pylori en la Aldea Potrero de las Casas, Táchira, Venezuela, aunado al potencial y cultura apícola de la zona promueven estudios de intervención con productos de la colmena que son accesibles y de bajo costo


Gastric Cancer is the leading cause of cancer death in Táchira State - Venezuela with a high mortality rate especially in the Andean States. Efforts at early gastric cancer detection based on radiological and endoscopic studies have failed to cover all the population. The identification of premalignant gastric lesion and gastric cancer associated with Helicobacter Pylori infection have led to the development of epidemiological primary prevention projects that led to influence on dietary and life style factors Helicobacter Pylori eradication using conventional therapy has been controversial results in differents latitudes with the same therapeutics regimens. The antimicrobial activity of different types of propolis against Helicobacter Pylori has been evaluated, the main responsibility are flavonoids,pinocembrin, galactin and chrysin. The high prevalence of Helicobacter Pylori in the village of Potrero de las Casas, Táchira Venezuela together with the potential of the area in the bee culture induce to think about to promote intervention studies with bee products that are accessible and low cost


Subject(s)
Female , Endoscopy, Gastrointestinal/methods , Helicobacter pylori/pathogenicity , Helicobacter pylori/virology , Stomach Neoplasms/diagnosis , Stomach Neoplasms/epidemiology , Stomach Neoplasms/prevention & control , Phantoms, Imaging , Gastroenterology , Medical Oncology
2.
Antimicrob Agents Chemother ; 49(10): 4240-6, 2005 Oct.
Article in English | MEDLINE | ID: mdl-16189104

ABSTRACT

The heterologous production in Escherichia coli, the purification, and the kinetic characterization of four plasmid-encoded class C beta-lactamases (ACT-1, MIR-1, CMY-2, and CMY-1) were performed. Except for their instability, these enzymes are very similar to the known chromosomally encoded AmpC beta-lactamases. Their kinetic parameters did not show major differences from those obtained for the corresponding chromosomal enzymes. However, the K(m) values of CMY-2 for cefuroxime, cefotaxime, and oxacillin were significantly decreased compared to those of the chromosomal AmpC enzymes. Finally, the susceptibility patterns of different E. coli hosts producing a plasmid- or a chromosome-encoded class C enzyme toward beta-lactam antibiotics are mainly due to the overproduction of the beta-lactamase in the periplasmic space of the bacteria rather than to a specific catalytic profile of the plasmid-encoded beta-lactamases.


Subject(s)
Bacterial Proteins/genetics , Plasmids/genetics , beta-Lactamases/genetics , Bacterial Proteins/biosynthesis , Bacterial Proteins/classification , Bacterial Proteins/isolation & purification , Bacterial Proteins/metabolism , Escherichia coli/drug effects , Escherichia coli/genetics , Kinetics , beta-Lactamases/biosynthesis , beta-Lactamases/classification , beta-Lactamases/isolation & purification , beta-Lactamases/metabolism
3.
Biochemistry ; 42(36): 10634-43, 2003 Sep 16.
Article in English | MEDLINE | ID: mdl-12962487

ABSTRACT

The crystallographic structure of the class A beta-lactamase Toho-1, an extended-spectrum beta-lactamase with potent activity against expanded-spectrum cephems, has been determined at 1.65 A resolution. The result reveals that the Lys73 side chain can adopt two alternative conformations. The predominant conformation of Lys73 is different from that observed in the E166A mutant, indicating that removal of the Glu166 side chain changes the conformation of the Lys73 side chain and thus the interaction between Lys73 and Glu166. The Lys73 side chain would play an important role in proton relay, switching its conformation from one to the other depending on the circumstances. The electron density map also implies possible rotation of Ser237. Comparison of the Toho-1 structure with the structure of other class A beta-lactamases shows that the hydroxyl group of Ser237 is likely to rotate through interaction with the carboxyl group of the substrate. Another peculiarity is the existence of three sulfate ions positioned in or near the substrate-binding cavity. One of these sulfate ions is tightly bound to the active center, while the other two are held by a region of positive charge formed by two arginine residues, Arg274 and Arg276. This positively charged region is speculated to represent a pseudo-binding site of the beta-lactam antibiotics, presumably catching the methoxyimino group of the third-generation cephems prior to proper binding in the substrate-binding cleft for hydrolysis. This high-resolution structure, together with detailed kinetic analysis of Toho-1, provides a new hypothesis for the catalytic mechanism and substrate specificity of Toho-1.


Subject(s)
beta-Lactamases/chemistry , beta-Lactamases/metabolism , Amino Acid Substitution , Anti-Bacterial Agents/antagonists & inhibitors , Anti-Bacterial Agents/chemistry , Anti-Bacterial Agents/metabolism , Binding Sites , Catalysis , Crystallography, X-Ray , Enzyme Inhibitors/pharmacology , Escherichia coli/enzymology , Escherichia coli/genetics , Hydrogen Bonding , Kinetics , Lysine/chemistry , Models, Molecular , Protein Conformation , Static Electricity , Substrate Specificity , Sulfates/chemistry , Sulfates/metabolism , beta-Lactam Resistance/genetics , beta-Lactamase Inhibitors , beta-Lactamases/genetics
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