Fluoroquinolones in industrial poultry production, bacterial resistance and food residues:a review

Fluoroquinolones are antimicrobial agents frequently used in poultry production and in human medicine. The use of such substances must comply with safety criteria, including withdrawal periods, doses, and treatment duration, as their misuse and abuse may cause bacterial resistance and the presence of residues in edible tissues. Consequently, the consumption of animal products with fluoroquinolone residues may result in the transmission of resistant bacteria. In addition, if residues are beyond the acceptable levels, fluoroquinolone active metabolites are harmful to human health. This article presents a review on the use of antimicrobials of the fluoroquinolone class in poultry production, focusing on the development of bacterial resistance to these drugs and the presence of their residues in poultry products

Serotyping and Genotyping of Salmonella Strains Isolated From Broilers, Chicken Carcasses Before and After Chilling, and Frozen Chicken Breasts Produced in The States of Mato Grosso do Sul and Santa Catarina, Brazil

ABSTRACT The present study investigated the effectiveness of a single Salmonella prevention and control program applied in two different processing plants, located in the states of Mato Grosso do Sul (plant A) and Santa Catarina (Plant B), belonging to the same company, and identified Salmonella strain subtypes isolated from broilers, carcasses before and after chilling, and frozen chicken breasts. The Salmonella prevention and control program was 90% effective in plant A and 100% in plant B, considering a level of 10% positive samples per frozen chicken breast batch acceptable. A total of 128 strains were serotyped, being 10 from drag swabs, 31 from cloacal swabs, 83 from carcasses, and 4 from frozen chicken breasts. After serotyping analysis, 30 strains isolated at different processing steps and drag swabs, and three Salmonella Minnesota strains isolated in 2012 in plant A, were genotyped by PFGE. In plant A, the most frequently strain isolated was Salmonella Minnesota (90.35%), followed by Salmonella Newport (8.77%), and in Plant B, Salmonella Senftenberg (80%). Salmonella Minnesota strains were differentiated by PFGE into 19 pulsotypes distributed in three clusters. The phenotypic identification by serotyping of four strains diverged from their PFGE genotypic results. Most Salmonella Minnesota strains genotyped in plant A and the strains isolated from environmental samples in 2012 in the same broiler processing plant belong to a single cluster, confirming the dominance and persistence of this clone over time

Role of PGI(2) and effects of ACE inhibition on the bradykinin potentiation by angiotensin-(1-7) in resistance vessels of SHR

The present study determined the participation of PGI(2) in the angiotensin-(1-7) [Ang-(1-7)libradykinin (BK) interaction, in the presence and absence of Angiotensin Converting Enzyme (ACE) inhibition, trying to correlate it with tissue levels of both peptides. the isolated mesenteric arteriolar bed of Spontaneously Hypertensive Rats (SHR) was perfused with Krebs or Krebs plus enalaprilat (10 DM), and drugs were injected alone or in association. BK (10 nM)-induced relaxation was potentiated by Ang-(1-7) (2.2 mug) in the presence or absence of enalaprilat. Ang-(1-7) receptor blockade [A-779 (4.8 mug)] did not interfere with the BK effect in preparations perfused with normal Krebs, but reversed the increased BK relaxation observed after ACE inhibition. PGI(2) release by mesenteric vessels was not altered by BK or Ang-(1-7) alone, but was increased when both peptides were injected in association, in the absence or in the presence of enalaprilat. ACE inhibition caused a 2-fold increase in the BK tissue levels, and a significant decrease in the Ang-(1-7) values. We conclude that endogenous Ang-(1-7) has an important contribution to the effect of ACE inhibitors participating in the enhancement of BK response. the mechanism of Ang-(1-7) potentiating effect probably involves an increased production of PGI(2). Our results suggest that a different enzymatic pathway (non-related to ACE) is involved in the local Ang-(1-7) metabolism. (C) 2004 Elsevier B.V. All rights reserved.Univ São Paulo, Inst Biomed Sci, Dept Pharmacol, BR-05508900 São Paulo, BrazilUniversidade Federal de São Paulo, Div Nephrol, São Paulo, BrazilUniv Fed Minas Gerais, Inst Biomed Sci, Dept Physiol & Biophys, Belo Horizonte, MG, BrazilUniversidade Federal de São Paulo, Div Nephrol, São Paulo, BrazilWeb of Scienc

Role of PGI(2) and effects of ACE inhibition on the bradykinin potentiation by angiotensin-(1-7) in resistance vessels of SHR

The present study determined the participation of PGI(2) in the angiotensin-(1-7) [Ang-(1-7)libradykinin (BK) interaction, in the presence and absence of Angiotensin Converting Enzyme (ACE) inhibition, trying to correlate it with tissue levels of both peptides. the isolated mesenteric arteriolar bed of Spontaneously Hypertensive Rats (SHR) was perfused with Krebs or Krebs plus enalaprilat (10 DM), and drugs were injected alone or in association. BK (10 nM)-induced relaxation was potentiated by Ang-(1-7) (2.2 mug) in the presence or absence of enalaprilat. Ang-(1-7) receptor blockade [A-779 (4.8 mug)] did not interfere with the BK effect in preparations perfused with normal Krebs, but reversed the increased BK relaxation observed after ACE inhibition. PGI(2) release by mesenteric vessels was not altered by BK or Ang-(1-7) alone, but was increased when both peptides were injected in association, in the absence or in the presence of enalaprilat. ACE inhibition caused a 2-fold increase in the BK tissue levels, and a significant decrease in the Ang-(1-7) values. We conclude that endogenous Ang-(1-7) has an important contribution to the effect of ACE inhibitors participating in the enhancement of BK response. the mechanism of Ang-(1-7) potentiating effect probably involves an increased production of PGI(2). Our results suggest that a different enzymatic pathway (non-related to ACE) is involved in the local Ang-(1-7) metabolism. (C) 2004 Elsevier B.V. All rights reserved.Univ São Paulo, Inst Biomed Sci, Dept Pharmacol, BR-05508900 São Paulo, BrazilUniversidade Federal de São Paulo, Div Nephrol, São Paulo, BrazilUniv Fed Minas Gerais, Inst Biomed Sci, Dept Physiol & Biophys, Belo Horizonte, MG, BrazilUniversidade Federal de São Paulo, Div Nephrol, São Paulo, BrazilWeb of Scienc