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1.
Animals (Basel) ; 12(14)2022 Jul 21.
Artigo em Inglês | MEDLINE | ID: mdl-35883406

RESUMO

High environmental temperatures cause heat stress in ewes, resulting in thermoregulatory problems. In this study, the thermoregulatory responses of Blackbelly adult ewes (G1, n = 14) and female lambs (G2, n = 7), during the summer under tropical conditions, in southern Mexico were analyzed. Different physiological variables and skin temperatures (ST) of the ewes were recorded. Breathing frequency (BF) values were similar between groups at 116.73 ± 33.598 bpm (G1) and 113.661 ± 34.515 bpm (G2) (p > 0.05). In the case of skin elasticity (SE), there were no significant differences between the time of day and the age of the ewes (p > 0.05). Significant differences were observed between groups for BF, rectal temperature (RT), and heart rate (HR) values (p < 0.05). All ST values, for both groups, were significantly higher during the afternoon (p < 0.001). In general, all Blackbelly adult ewes and female lambs during the summer present severe heat stress conditions as a result of an increase in physiological constants and ST. It is concluded that all ewes thermoregulate body temperature by modifying different physiological variables to counteract the effect of heat stress.

2.
J Biol Chem ; 285(42): 32336-42, 2010 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-20688909

RESUMO

We present a body of ultrastructural, biochemical, and genetic evidence that demonstrates the oligomerization of virulence-associated autotransporter proteins EspC or EspP produced by deadly human pathogens enterohemorrhagic and enteropathogenic Escherichia coli into novel macroscopic rope-like structures (>1 cm long). The rope-like structures showed high aggregation and insolubility, stability to anionic detergents and high temperature, and binding to Congo Red and thioflavin T dyes. These are properties also exhibited by human amyloidogenic proteins. These macroscopic ropes were not observed in cultures of nonpathogenic Escherichia coli or isogenic espP or espC deletion mutants of enterohemorrhagic or enteropathogenic Escherichia coli but were produced by an Escherichia coli K-12 strain carrying a plasmid expressing espP. Purified recombinant EspP monomers were able to self-assemble into macroscopic ropes upon incubation, suggesting that no other protein was required for assembly. The ropes bound to and showed cytopathic effects on cultured epithelial cells, served as a substratum for bacterial adherence and biofilm formation, and protected bacteria from antimicrobial compounds. We hypothesize that these ropes play a biologically significant role in the survival and pathogenic scheme of these organisms.


Assuntos
Aderência Bacteriana , Escherichia coli Êntero-Hemorrágica , Escherichia coli Enteropatogênica , Proteínas de Escherichia coli , Serina Endopeptidases , Animais , Antibacterianos/farmacologia , Farmacorresistência Bacteriana/efeitos dos fármacos , Escherichia coli Êntero-Hemorrágica/química , Escherichia coli Êntero-Hemorrágica/genética , Escherichia coli Êntero-Hemorrágica/patogenicidade , Escherichia coli Enteropatogênica/química , Escherichia coli Enteropatogênica/genética , Escherichia coli Enteropatogênica/patogenicidade , Células Epiteliais/metabolismo , Células Epiteliais/microbiologia , Proteínas de Escherichia coli/química , Proteínas de Escherichia coli/genética , Proteínas de Escherichia coli/ultraestrutura , Células HeLa , Humanos , Serina Endopeptidases/química , Serina Endopeptidases/genética , Serina Endopeptidases/ultraestrutura
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