Quantitation of Acute Phase Proteins and Protein Electrophoresis Fractions in Ferrets

Ravich, Michelle; Johnson-Delaney, Cathy A.; Kelleher, Susan A.; Hess, Laurie; Arheart, Kristopher L.; Cray, Carolyn

doi:10.1053/j.jepm.2015.04.010

Cited by 3 publications

(7 citation statements)

References 19 publications

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“…158,159 Reference intervals derived from the AGE method have been previously reported in the ferret. 160 Two bands have been commonly observed in the alpha 2 globulin fraction. Compared with samples from clinically abnormal ferrets with a wide variety of presentations, the alpha 2, beta, and gamma globulin fractions were found to be significantly increased.…”

Section: S Mall E Xoti C Mammal Smentioning

confidence: 99%

Protein electrophoresis of non‐traditional species: A review

Cray

2021

Veterinary Clinical Pathol

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EPH can provide information regarding serum or plasma proteins, including albumin and globulins, that can be broadly classified based on their migration. The globulin fractions can reveal inflammation as well as polyclonal and monoclonal gammopathies. Detection of the latter, also named paraproteins, is one of the most common applications of EPH in human medicine as clinicians have a large toolbox of specific assays for various acute-phase proteins (APPs) that allow them to more specifically gauge inflammation. 1,2 In veterinary medicine, given the advances in species-specific and cross-reactive reagents for major APP in traditional species, including dogs, cats, and horses, these tools can complement the use of EPH in its valid quantitation of albumin and detection of paraproteinemia. [3][4][5][6][7][8] In non-traditional species, including birds, reptiles, fish, amphibians, invertebrates, small exotic mammals, and non-domesticated mammals, EPH can also be used as an aid to the diagnosis of lymphoproliferative disease, but its primary use is in the detection of inflammation and polyclonal gammopathies. For many of these species, reagents are not yet available or widely validated to quantitate APPs. The valid quantitation of albumin, a key negative APP, by biochemistry analyzer methods, remains a major issue. Moreover, in non-mammalian species, as innate immunity is perhaps the essential, diverse, and robust immune response, EPH can provide even more value. 9,10 Challenges in the applications of EPH in these special species include a lack of standardization of fraction delimiter placements, RIs, and information regarding fraction composition. This paper reviews the applications of EPH in non-traditional species as well as the currently available methodology. Additional reviews on this subject with a varied focus are also available. [11][12][13][14][15] | APPLI C ATI ON S OF EPH IN NON -TR ADITIONAL S PECIE S | Detection of monoclonal gammopathyAs described in mammals, EPH is a key tool in the detection of paraproteins. 2,3 This application has also been demonstrated in nontraditional species. 16,17 In electrophoretograms of avian plasma,

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Section: S Mall E Xoti C Mammal Smentioning

confidence: 99%

Protein electrophoresis of non‐traditional species: A review

Cray

2021

Veterinary Clinical Pathol

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“…In other similar species such as pet ferrets, slightly higher values of 61 g/L (Ravich et al. 2015 ) and 63 g/L (Eshar et al. 2021 ) have been reported.…”

Section: Discussionmentioning

confidence: 87%

“…Using AGE methods in pet ferrets, the same protein fractions have been identified as in minks but with lower levels in the percentage of albumin and higher levels for those of β-globulins (Ravich et al. 2015 ). The interpretation of the existence of inflammation or the reaction of γ-globulins to infectious diseases in European mink is greatly limited due to this fact.…”

Section: Discussionmentioning

confidence: 99%

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Serum protein electrophoresis in European mink ( Mustela lutreola ): reference intervals and comparison of agarose gel electrophoresis and capillary zone electrophoresis

Villanueva-Saz,

Aranda,

Jiménez

et al. 2024

Veterinary Quarterly

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Background Knowledge of reference intervals for blood analytes, including serum protein fractions, is of great importance for the identification of infectious and inflammatory diseases and is often lacking in wild animal species. Material and methods Serum samples were obtained from European minks enrolled in the breeding program (n = 55). Agarose gel electrophoresis (AGE) and capillary zone electrophoresis (CZE) were used to separate and identify protein fractions. Albumin, α1, α2, β, and γ-globulins fractions were identified in all mink sera by both electrophoresis methods. Reference intervals (90% CI) were determined following the 2008 guidelines of the Clinical Laboratory Standard Institute. The methods were compared using Passing-Bablok regression, Bland–Altman analysis, and Lin’s concordance correlation. Results A significant bias was found between methods for α1, α2, and γ-globulin. Lin’s concordance correlation was considered unacceptable for α1, α2, and β-globulins. Differences for gender between methods were found for albumin and α2-globuins, which were higher for males than females. γ-globulins were higher for adults than young minks using both methods; however, α1 and α2-globulins were lower. Conclusion Both methods are adequate for identifying serum protein disorders, but the AGE and CZE methods are not equivalent. Therefore, reference intervals for each technique are required.

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“…Consequently, we may have introduced a slight bias and overestimated the abundance of ferret Igk in the serum of influenza-naive ferrets. Nevertheless, the competitive ELISA approach described in this study could still serve as an improvement to existing techniques used to evaluate serum Ig in ferrets (37). Furthermore, the affinity chromatography methods described in this study could be expanded upon, such as resolution of ferret Ig species according to size, to create more refined protein fractions.…”

Section: Discussionmentioning

confidence: 99%

Infection of Ferrets with Influenza Virus Elicits a Light Chain–Biased Antibody Response against Hemagglutinin

Kirchenbaum

Allen

Layman

et al. 2017

The Journal of Immunology

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The domestic ferret () is a commonly used animal model for the study of influenza virus infection and vaccination. Recently, our group has developed murine mAbs with specificity for the κ (Igκ) and λ (Igλ) L chains of ferret Ig. These mAbs were used to quantify the abundance of Igκ and Igλ in serum and to evaluate L chain usage of the Ab response against the hemagglutinin (HA) protein elicited by influenza infection. After influenza A infection of immunologically naive ferrets with various H1N1 or H3N2 strains, the acute Ab response against HA exhibited an inherent bias toward λ L chain usage. In contrast, secondary infection of H1N1 preimmune ferrets with an antigenically distinct H1N1 virus elicited a recall response against the original HA that was no longer biased toward Igλ and possessed differential specificity. Moreover, sequential infection of ferrets with H1N1 influenza viruses elicited an Igκ-biased Ab response directed against the HA globular head and stem regions. Furthermore, sequential infection of ferrets with viral vectors expressing chimeric HA, aimed at boosting Ab reactivity against the HA stem region, also elicited an Igκ-biased response. Collectively, these findings suggest that ferret B cells expressing an Igκ or Igλ BCR possess differential specificities, and highlight the utility of our recently developed mAbs for studying the immune response to influenza virus infection and vaccination in the ferret model.

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Quantitation of Acute Phase Proteins and Protein Electrophoresis Fractions in Ferrets

Cited by 3 publications

References 19 publications

Protein electrophoresis of non‐traditional species: A review

Protein electrophoresis of non‐traditional species: A review

Serum protein electrophoresis in European mink ( Mustela lutreola ): reference intervals and comparison of agarose gel electrophoresis and capillary zone electrophoresis

Infection of Ferrets with Influenza Virus Elicits a Light Chain–Biased Antibody Response against Hemagglutinin

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