Immediate responses in serum tnfα and acute phase protein concentrations to infection with Pasteurella haemolytica A1 in calves

Horadagoda, A.; Eckersall, P.D.; Hodgson, John; Gibbs, H. A.; Moon, G.M.

doi:10.1016/0034-5288(94)90094-9

Cited by 85 publications

(64 citation statements)

References 17 publications

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“…The bacterial infection and immediate inflammatory reaction are presumed to be largely responsible for their concentration changes. The serum apoSAA concentration has been evaluated by enzyme-linked immunosorbent assay using polyclonal rabbit antiserum to bovine or human apoSAA [3,7,8]. It became evident in the present study that serum concentrations of the immunologically related 7.5-9.0 kDa and <6.5 kDa proteins were decreased during pneumonia.…”

Section: Discussionmentioning

confidence: 76%

“…Immunoblot analysis of apoSAA in lipoprotein fractions from sera of calves before and after inoculation of Pasteurella haemolitica. Combined sera from six calves obtained at 0 hr and at 1 day after were used as control (1-6) and pneumonic sera (7)(8)(9)(10)(11)(12), respectively. Lanes are: 1 and 7, CM; 2 and 8, VLDL; 3 and 9, LDL; 4 and 10, HDL; 5 and 11, lipoprotein-deficient fraction; and 6 and 12, serum.…”

Section: Discussionmentioning

confidence: 99%

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The Presence of Two Low Molecular Mass Proteins Immunologically Related to 14 Kilodalton Serum Amyloid A in the Lipoprotein Fraction and Their Decreased Serum Concentrations in Calves with Experimentally Induced Pneumonia

Yamamoto

Katoh

Adachi

1998

The Journal of Veterinary Medical Science

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ABSTRACT. A 14 kilodalton (kDa) serum amyloid A (apoSAA) protein was purified from cow serum. Rabbit antiserum to the 14 kDa apoSAA recognized, in addition to the 14 kDa protein, a 7.5-9.0 kDa protein and a protein having a molecular mass of less than 6.5 kDa (<6.5 kDa protein). The possibility that the two proteins were contaminants was excluded by results showing that the two proteins detected in early stages of purification procedures were not found in the purified 14 kDa apoSAA fraction, as revealed by immunoblot analysis. As in the 14 kDa apoSAA, the 7.5-9.0 kDa protein was localized in the high-density lipoprotein fraction, while the <6.5 kDa protein was in the low-density lipoprotein fraction. In calves with pneumonia induced by inoculation to the lungs of Pasteurella haemolitica, the serum concentration of the 14 kDa apoSAA was increased, whereas those of the 7.5-9.0 kDa and the <6.5 kDa proteins were conversely decreased. The time-course study indicated that the increase in concentration of the 14 kDa apoSAA and decrease in that of the <6.5 kDa protein occurred almost simultaneously. These results suggest that the 14 kDa apoSAA and the immunologically related 7.5-9.0 kDa and <6.5 kDa proteins act as positive and negative acute phase reactants, respectively, and also that concentrations of the three proteins are regulated in concert in acute phase plasma. fraction and, moreover, the serum concentration of the 14 kDa apoSAA was increased whereas those of the two low molecular mass proteins were conversely decreased in sera from calves with pneumonia induced by inoculation of Pasteurella haemolitica. MATERIALS AND METHODS Purification of apoSAA:ApoSAA was purified from cow serum during the course of purification of apoC-III [26]. Briefly, the total lipoprotein fraction [d<1.21, containing chylomicrons (CM) to HDL] prepared from sera of Holstein cows during midlactation was treated with an equal volume of acetone to extract low molecular mass apolipoproteins such as apoC-III and apoSAA. The supernatant obtained by centrifugation at 140 × g for 10 min was lyophilized and thereafter delipidated by mixing with 20 volumes of 2-propanol. Apolipoproteins pelleted by centrifugation at 1,300 × g for 10 min, were dissolved in 6 M urea and 50 mM Tris-HCl (pH 8.6), and applied to a column (2.5 × 90 cm) of Sephadex G-75 (Pharmacia Biotech, Uppsala, Sweden). Fractions rich in low molecular mass apolipoproteins were next applied to a DEAE-Sephacel (Pharmacia Biotech, Uppsala, Sweden) column (2 × 25 cm), and bound proteins were eluted by use of a linear gradient of NaCl (0-0.125 M, total 1 liter). Fractions containing apoSAA were dialyzed against 10 mM ammonium hydrogen carbonate, using cellulose dialyzer tubing with a 3,500 molecular weight cutoff, after which the dialysate was

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Section: Discussionmentioning

confidence: 76%

Section: Discussionmentioning

confidence: 99%

The Presence of Two Low Molecular Mass Proteins Immunologically Related to 14 Kilodalton Serum Amyloid A in the Lipoprotein Fraction and Their Decreased Serum Concentrations in Calves with Experimentally Induced Pneumonia

Yamamoto

Katoh

Adachi

1998

The Journal of Veterinary Medical Science

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“…The assay was quantified by comparison with dilutions of a bovine serum sample with a known concentration of haptoglobin, originally being calibrated with purified bovine haptoglobin (Horadagoda et al, 1994).…”

Section: Methodsmentioning

confidence: 99%

Susceptibility of calves to challenge with Salmonella typhimurium 4/74 and derivatives harbouring mutations in htrA or purE

et al. 2000

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Salmonella typhimurium 4/74 is highly virulent for cattle after oral challenge, causing severe diarrhoea, which is sometimes associated with systemic spread of the micro-organism. Although susceptible to oral challenge, groups of cattle were found to be relatively resistant to subcutaneous challenge with this strain. The virulence of S. typhimurium 4/74 harbouring mutations in htrA and purE was also assessed in cattle. Although S. typhimurium 4/74 htrA and purE are attenuated following oral challenge in mice, cattle were highly susceptible to oral challenge with these mutants. As with the parent S. typhimurium 4/74 strain, cattle exhibited greater susceptibility to oral compared to subcutaneous challenge with S. typhimurium htrA and purE mutants. Following subcutaneous challenge with sublethal levels of S. typhimurium 4/74, calves produced significant levels of antibodies to S. typhimurium soluble extract. No correlation was detected between interferon gamma levels in sera and susceptibility to infection by any route. The concentrations of the acute-phaseassociated protein haptoglobin were increased in the sera of five of six cattle inoculated subcutaneously, although increases in concentration were smaller in cattle inoculated orally.

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“…They act together through multiple, overlapping pathways and have local effects on the cells surrounding the site of injury in addition to systemic effects by transport via the blood stream to various target organs [14,170,181]. The serum concentration increases within a few hours after the initiating stimulus [73,83,184,185] and they are usually cleared from the circulation within a few hours [17,53,73,184].…”

Section: The Acute Phase Proteinmentioning

confidence: 99%

Application of acute phase protein measurements in veterinary clinical chemistry

2004

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-The body's early defence in response to trauma, inflammation or infection, the acute phase response, is a complex set of systemic reactions seen shortly after exposure to a triggering event. One of the many components is an acute phase protein response in which increased hepatic synthesis leads to increased serum concentration of positive acute phase proteins. The serum concentration of these acute phase proteins returns to base levels when the triggering factor is no longer present. This paper provides a review of the acute phase proteins haptoglobin, C-reactive protein and serum amyloid A and their possible use as non-specific indicators of health in large animal veterinary medicine such as in the health status surveillance of pigs at the herd level, for the detection of mastitis in dairy cattle and for the prognosis of respiratory diseases in horses.

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Immediate responses in serum tnfα and acute phase protein concentrations to infection with Pasteurella haemolytica A1 in calves

Cited by 85 publications

References 17 publications

The Presence of Two Low Molecular Mass Proteins Immunologically Related to 14 Kilodalton Serum Amyloid A in the Lipoprotein Fraction and Their Decreased Serum Concentrations in Calves with Experimentally Induced Pneumonia

The Presence of Two Low Molecular Mass Proteins Immunologically Related to 14 Kilodalton Serum Amyloid A in the Lipoprotein Fraction and Their Decreased Serum Concentrations in Calves with Experimentally Induced Pneumonia

Susceptibility of calves to challenge with Salmonella typhimurium 4/74 and derivatives harbouring mutations in htrA or purE

Application of acute phase protein measurements in veterinary clinical chemistry

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