Effect of Pasteurella haemolytica infection of α1-acid glycoprotein and albumin concentrations in serum and subcutaneous tissue chamber fluid of calves

Walker, Joan L.; Clarke, Cyril R.; Lessley, Bruce A.; Hague, Christinia M.

doi:10.1016/0034-5288(94)90098-1

Cited by 10 publications

(13 citation statements)

References 16 publications

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“…The concentrations of erythromycin were within the range of those expected in serum and tissues after intravascular (4) or intramuscular (5) g of albumin (Sigma Chemical Co.) per ml in buffer. Similar concentrations of these proteins have been reported in the sera of cattle inoculated with P. haemolytica (13,25). The purity of bovine AAG was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.…”

Section: Materuils and Methodssupporting

confidence: 78%

“…Furthermore, the chamber model allows study of protein binding in infected animals, which may be particularly appropriate when a drug interacts with acute-phase proteins, such as AAG. Previous studies have shown that inoculation of P. haemolytica into subcutaneous tissue chambers causes inflammatory changes that are similar to those observed in the lungs of cattle with pneumonic pasteurellosis (10,11,25). These changes include rapid sequestration of degranulating neutrophils, deposition of fibrin, and leakage of plasma proteins.…”

Section: Discussionmentioning

confidence: 71%

“…The purity of bovine AAG was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Samples of albumin in PBS were assayed by radial immunodiffusion assay (25) and were found to be contaminated with very low levels of AAG (0.034 ± 0.019 mg of AAG per ml in samples containing 300 mg of albumin per ml). These levels were considered inconsequential.…”

Section: Materuils and Methodsmentioning

confidence: 99%

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Effects of localized Pasteurella haemolytica infection on erythromycin-binding properties of bovine alpha-1-acid glycoprotein, albumin, serum, and tissue chamber fluids

Walker

Clarke

Hague

et al. 1994

Antimicrob Agents Chemother

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The in vitro erythromycin-binding properties of bovine alpha-i-acid glycoprotein (AAG) and albumin were studied by using equilibrium dialysis. In addition, the proportions of free erythromycin in bovine serum and tissue chamber fluid before and 4 days after inoculation of subcutaneous tissue chambers with Pasteurella haemolytica were measured. At a concentration of 5 jig/ml, erythromycin was moderately bound to AAG (39%o 4% free) and was only slightly bound to albumin (86%o + 2% free). Scatchard analysis of the data describing binding to pure bovine AAG indicated that erythromycin was bound to a single high-affinity (6.45 x 104 M-1) site on the protein. At lower total concentrations of erythromycin, the free concentrations of the antibiotic were lower in serum samples collected after infection (49% +± 3% at 5 ,ug of erythromycin per ml) than in those collected before inoculation (55% 3% at 5 ,ug of erythromycin per ml). Inoculation had no eflect on binding to macromolecules in chamber fluids. Inoculated tissue chambers served as a convenient model for studying the eflect of infection on drug-macromolecule interactions in interstitial fluid.

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Section: Materuils and Methodssupporting

confidence: 78%

Section: Discussionmentioning

confidence: 71%

Section: Materuils and Methodsmentioning

confidence: 99%

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Effects of localized Pasteurella haemolytica infection on erythromycin-binding properties of bovine alpha-1-acid glycoprotein, albumin, serum, and tissue chamber fluids

Walker

Clarke

Hague

et al. 1994

Antimicrob Agents Chemother

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“…Particularly hp, Saa and Cp are regarded as important aPPs as these are produced in low-levels in healthy cattle, but in extremely high concentrations during an acute phase response (BASBUG et al, 2011;GOKCE and BOZUKLUHAN, 2009;GRUYS et al, 1994;REGESSA and NOakeS, 1999;SkINNer, 2001;WaLker et al, 1994). thus, these parameters were also determined in the study.…”

Section: Discussionmentioning

confidence: 99%

“…In the studies conducted, it was revealed that Saa and hp values were extremely important markers (HORADAGODA et al, 1999) in distinctive diagnosis of bacterial (AYTEKIN et al, 2016;ECKERSALL et al, 2006;GANHEIM et al, 2003;SKINNER and rOBertS, 1991;WaLker et al, 1994) and viral (BASBUG et al, 2016;GANHEIM et al, 2003;HEEGARD et al, 2000;HOFNER et al, 1994;STENFELDT et al, 2011;ULUTAS et al, 2011) diseases, and plasma levels in these diseases increased significantly.…”

Section: Discussionmentioning

confidence: 99%

Haptoglobin, serum amyloid A and ceruloplasmin concentrations in cattle with suspicion of coryza gangrenosa bovum

et al. 2017

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the aim of this study was to determine haptoglobin (hp), serum amyloid-a (Saa) and ceruloplasmin (Cp) levels in naturally occurring cases of coryza gangrenosa bovum (CGB). the study was conducted on 14 animals, where 7 were sick cattle clinically diagnosed with CGB (patient group), and 7 healthy cattle from the same region (control group). It was determined that the general clinical examination results (rectal temperature, heart and respiratory frequency and rumen movement) detected in the patient group of animals showed significant differences (P<0.001) with respect to the animals in the control group. Serum hp, Saa and Cp concentrations in the animals in the control group were determined as 0.22 ± 0.02 mg/mL, 13.96 ± 0.79 µg/mL and 8.10 ± 2.85 mg/dL respectively, but 0.75 ± 0.20 mg/mL, 182.25 ± 22.63 µg/mL and 9.40 ± 2.54 mg/dL, respectively for the patient group. It was determined that Saa (P<0.001) and hp (P<0.05) concentrations of the cattle in the patient group were significantly enhanced, while the increase in Cp levels were observed to be insignificant (P>0.05). Consequently, serum SAA and Hp concentrations in the cattle with CGB infection increased significantly in the acute phase of the disease, and it was concluded that further in-depth studies should be conducted on more animals in order to reveal the clinical significance of these changes in CGB infections, and also for precise diagnosis of CGB.

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Acute Phase Proteins in Animals

Cray

2012

Progress in Molecular Biology and Translational Science

512

701

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Acute phase proteins (APP) were first identified in the early 1900s as early reactants to infectious disease. They are now understood to be an integral part of the acute phase response (APR) which is the cornerstone of innate immunity. APP have been shown to be valuable biomarkers as increases can occur with inflammation, infection, neoplasia, stress, and trauma. All animals--from fish to mammals--have demonstrable APP, but the type of major APP differs by species. While the primary application of these proteins in a clinical setting is prognostication, studies in animals have demonstrated relevance to diagnosis and detection and monitoring for subclinical disease. APP have been well documented in laboratory, companion, and large animals. With the advent of standardized and automated assays, these biomarkers are available for use in all fields of veterinary medicine as well as basic and clinical research.

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Effect of Pasteurella haemolytica infection of α1-acid glycoprotein and albumin concentrations in serum and subcutaneous tissue chamber fluid of calves

Cited by 10 publications

References 16 publications

Effects of localized Pasteurella haemolytica infection on erythromycin-binding properties of bovine alpha-1-acid glycoprotein, albumin, serum, and tissue chamber fluids

Effects of localized Pasteurella haemolytica infection on erythromycin-binding properties of bovine alpha-1-acid glycoprotein, albumin, serum, and tissue chamber fluids

Haptoglobin, serum amyloid A and ceruloplasmin concentrations in cattle with suspicion of coryza gangrenosa bovum

Acute Phase Proteins in Animals

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