Cross Reactivities Among Some Mammalian Haptoglobins Studied by a Monoclonal Antibody

Kaţnik, I; Pupek, Małgorzata; Stefaniak, Tadeusz

doi:10.1016/s0305-0491(97)00358-1

Cited by 9 publications

(8 citation statements)

References 19 publications

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“…Contrary to reports in other species, data regarding APP levels in cats are scarce and mostly focused on general aspects of feline APP biology, such as the demonstration of the lack of age-related changes in APP concentration in feline serum (Campbell et al, 2004), basic and comparative information about APP gene and protein structures (Mominoki et al, 1995;Yoshida et al, 1997;Ohno et al, 1999;van Rossum et al, 2004) or methodological aspects of measurement of feline APPs (Katnik et al, 1998;Kajikawa et al, 1996;Sasaki et al, 2001). Most feline APP studies have been focused on AGP, SAA and, to a lesser extent, Hp -the three proteins which have been shown to work as major APPs in the cat.…”

Section: Feline Appsmentioning

confidence: 99%

The feline acute phase reaction

Paltrinieri¹

2008

The Veterinary Journal

131

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The acute phase reaction (APR) is a response to potentially pathogenic stimuli. It begins with the release of interleukin (IL)-1, IL-6 and tumour necrosis factor (TNF)-alpha from inflammatory cells. These cytokines induce fever, leucocytosis and release of serum acute phase proteins (APPs). In this review, the characteristics of the feline APR are described. In cats with inflammatory conditions, fever is a common finding, with leucocytosis due to the release of cells from the marginal pool, followed by activation of myelopoiesis. Because excitement frequently causes leucocytosis in cats, a diagnosis of inflammation should therefore be supported by additional findings such as the presence of toxic neutrophils. The major APPs are serum amyloid A and alpha(1)-acid glycoprotein (AGP), which both increase a few hours after the inflammatory stimulus and remain elevated for as long as the inflammation persists. AGP plays an important role in the diagnosis of feline infectious peritonitis (FIP) and may also be useful also in studies of FIP pathogenesis.

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Section: Feline Appsmentioning

confidence: 99%

The feline acute phase reaction

Paltrinieri¹

2008

The Veterinary Journal

131

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“…After Hp-Hb complex formation, Hp concentration can be measured by two different ways: (a) Hp-Hb complex formation produces changes in absorbance characteristics of Hb in proportion to the concentration of Hp (Harvey, 1986); (b) use of the innate peroxidase activity of Hp-Hb, which can be quantified at a mildly acidic pH by addition to hydrogen peroxide in the presence of a chromogen at 600 nm wavelength (Makimura and Suzuki, 1982;Eckersall et al, 1999). Immunological methods use specific antibodies against Hp, and the formation of antigen-antibody complexes can be detected and quantified by: (a) addition of a secondary enzyme-labelled antibody against the primary specific anti-Hp antibody (ELISA methods) (Katnik et al, 1998;Yee and Brown, 1999); (b) appearance of spectrophotometrically detectable turbidity in the reaction cuvette due to a precipitate that appear when antigen and antibody are mixed in the correct proportions (immunoturbidimetric methods) (Moseley, 1980). Commercial immunological kits developed for human Hp determination use anti-human Hp anti-serum; although in the case of Hp these kits can be used in veterinary practice, cross-reactivity between anti-human Hp antibodies and Hp from other species must be previously verified (Solter et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Validation of a Commercially Available Human Immunoturbidimetric Assay for Haptoglobin Determination in Canine Serum Samples

et al. 2006

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Haptoglobin is a positive acute-phase protein with a valuable role as a marker of inflammation in both human and veterinary medicine. The aim of this study was to validate a commercially available immunoturbidimetric method designed for human haptoglobin determination (Izasa SA, Barcelona, Spain) for its use in canine samples. Cross-reactivity between anti-human haptoglobin antiserum and canine haptoglobin was found when agarose gel immunodiffusion and ELISA tests were performed. The use of canine pooled serum with haptoglobin concentration of 6.3 g/L as standard provided higher analytical range than commercially available standards. Intra-assay and inter-assay coefficients of variation were 2.49% and 4.60%, respectively. A linear regression model between immunoturbidimetric results and a previously validated spectrophotometric method (Tridelta Development Limited, Ireland) yielded a slope at 95% confidence interval of 0.94 (0.86, 1.02) and y-intercept at 95% confidence interval of 0.11 (-0.59, 0.82). No significant differences were produced by anticoagulants, lipaemia and bilirubinaemia, although haemolysis significantly decreased haptoglobin. A significant increase of haptoglobin concentration was detected in inflammatory conditions such as pyometra and leishmaniasis, in neoplastic conditions, and after glucocorticoid administration. Canine serum haptoglobin concentration can be reliably measured using the commercially available Izasa immunoturbidimetric method developed for human haptoglobin determination. This method is precise and accurate, provides a wider analytical range than previous reported methods, and can be easily automated and used for routine haptoglobin determination in canine samples.

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“…A mouse monoclonal antibody to human haptoglobin recognized goat, sheep and bovine haptoglobins and to a lesser extent horse and rabbit haptoglobins. This antibody did not react with haptoglobins from dog, fox, cat and pig (Katnik et al, 1998). Another study found that an antibody preparation reacted with goat, sheep and bovine haptoglobins but not with pig haptoglobin (Busby and Travis, 1978).…”

Section: Introductionmentioning

confidence: 89%

Conservation of Binding of Llama and Other Animals’ Hemoglobins to Haptoglobins Across Species

Woldemeskel¹,

Vanderpuye²

2018

American Journal of Biochemistry and Biotechnology

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The plasma protein haptoglobin binds hemoglobin released from lysed erythrocytes. It causes removal of the free hemoglobin, thus preventing pathological oxidation of cells. Hemoglobin higher level structures are well conserved across animal species but primary structures can be as little as 50% homologous. Because of these differences, the question arose as to what extent hemoglobins can bind to haptoglobins from different species. The charge properties and binding to three genetic variants of human haptoglobin were compared by non-denaturing agarose gel electrophoresis, with llama, human, dog, pig, horse and goat hemoglobins. In this study, it was reported for the first time that llama and alpaca hemoglobins differed in electrophoretic mobility from hemoglobins from several animal species and humans. Llama hemoglobin was more positively charged than the other mammalian hemoglobins. Electrophoretic mobility changes of the animal hemoglobins in the presence of human plasma and two different purified human haptoglobin genetic variants suggested that hemoglobins from all animals in this study could bind all three genetic variants of human haptoglobin. In all cases, the llama hemoglobin-haptoglobin samples had lesser mobility than those of the other mammals. This study showed that the binding sites on hemoglobin and haptoglobin for each other have been evolutionarily conserved despite differences in primary structure and marked difference in the charge of llama hemoglobin from the other animal species and humans.

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Cross Reactivities Among Some Mammalian Haptoglobins Studied by a Monoclonal Antibody

Cited by 9 publications

References 19 publications

The feline acute phase reaction

The feline acute phase reaction

Validation of a Commercially Available Human Immunoturbidimetric Assay for Haptoglobin Determination in Canine Serum Samples

Conservation of Binding of Llama and Other Animals’ Hemoglobins to Haptoglobins Across Species

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