Protein electrophoresis of non‐traditional species: A review

Abstract

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,

Supplementation of Boswellia serrata and Salix alba Extracts during the Early Laying Phase: Effects on Serum and Albumen Proteins, Trace Elements, and Yolk Cholesterol

“…It is well-recognized that the AGE applied to serum and plasma samples suffers from differences due to commercial platforms and reagents [ 22 ]. However, despite subtle differences in electrophoretic profiles, Cray (2021) [ 18 ], using a different platform (Helena SPIFE 3000 system), reported the same fractions (prealbumin, albumin, α1, α2, β, and γ globulins) in the electropherograms of chicken sera that were found in this study. Therefore, taken together, these data can be considered a first attempt to define a standard profile for serum proteins in healthy chickens.…”

“…Gel electrophoresis is widely used to analyze protein-rich samples, from agarose gel electrophoresis used in clinical settings to separate serum proteins (SPE–AGE) to the more sensitive mono- or bidimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) used to separate complex protein mixtures in different biological samples [ 15 , 16 , 17 ]. Despite its routine use in domestic and farm mammals and its increasing popularity in non-conventional avian species [ 18 ], SPE–AGE has rarely been applied to poultry. The lack of standardization of fraction separation and information regarding the protein composition makes the use of this diagnostic technique in poultry limited.…”

Increasing the data on elasmobranch plasma protein electrophoresis: electrophoretogram reference values determination in the undulate skate (Raja Undulata) and the nursehound shark (Scyliorhinus stellaris) maintained under human care

“…Caution was taken to delete the injection peak and the end delimiter produced by the urine buffer before electrophoretogram interpretation and division into fractions for its analysis. As done in previous PPE studies with elasmobranchs, and in the absence of studies defining which proteins correspond to each electrophoretogram fraction, the classification of the different fractions as pre-albumin, alpha-, beta-, and gamma-globulins, was made based on their similarity in migration properties with respect to other taxa [ 11 ]. The further division of protein fractions migrating in the alpha- and beta-globulin regions into several subfractions was possible as the different peaks in the curve were consistent and reproducible among all the individuals sampled.…”

“…If possible, PPE analysis should be included in the routine health evaluation of elasmobranchs, as disease diagnosis in this group of animals can be challenging and the clinical application of PPE for health evaluation and disease diagnosis is useful, not only in mammal and avian species, but also in elasmobranchs [ 3 , 9 – 11 ]. Variations in plasma protein values can indicate a subclinical disease before the animal shows clinical symptoms [ 4 ].…”

“…Variations in plasma protein values can indicate a subclinical disease before the animal shows clinical symptoms [ 4 ]. Moreover, together with the serum protein changes that can be seen in plasma chemistry analysis, PPE has been shown to be a beneficial testing method as it can be used to evaluate variations in plasma protein trends without the need for species-specific reagents and can more accurately quantitate lipoproteins, providing valuable information for assessing ongoing inflammatory processes [ 11 , 12 ].…”