|RASAPRUTRA, KOMAL - University Of Arkansas|
|LIYANAGE, R - University Of Arkansas|
|LAY, J - University Of Arkansas|
|ERF, G - University Of Arkansas|
|OKIMOTO, R - University Of Arkansas|
Submitted to: Open Proteomics Journal
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/29/2011
Publication Date: 2/1/2012
Citation: Rasaprutra, K., Liyanage, R., Lay, J., Erf, G., Okimoto, R., Rath, N.C. 2012. Changes in serum protein profiles of chickens with tibial dyschondroplasia. Open Proteomics Journal. 5:1-7. Available: http://www.benthamscience.com/open/toprotj/.
Interpretive Summary: Differences in serum protein profiles were analyzed to identify biomarkers associated with a poultry leg problem named tibial dyschondroplasia (TD) that can causes lameness. We used a type of beads called Proteominer to fractionate proteins and compare the differences in serum protein between normal and disease affected chickens with the intent to identify any disease associated protein biomarker. Although our results showed an increase in certain antibodies called IgM in the blood of chickens with TD, they could be associated with necrotizing cells in the diseased tissue which may not be useful as biomarker.
Technical Abstract: Differences in serum protein profiles were analyzed to identify biomarkers associated with a poultry leg problem named tibial dyschondroplasia (TD) that can cause lameness. We used a bead-based affinity matrix containing a combinatorial library of hexapeptides (ProteoMinerTM) to deplete high abundant proteins and enrich the less abundant ones to compare the protein differences in sera of six-week old normal and TD affected chickens. Equal amounts of ProteoMiner pretreated serum proteins from control and TD-affected birds were analyzed by 2D gel electrophoresis and image analysis to identify the differentially expressed protein spots. Each protein spot was characterized using standard in-gel trypsin digestion followed by mass spectrometry. Of 46 observed protein spots in the gels, 33 were identified, of which 8 spots corresponding to immunoglobulins (Ig) were up-regulated in birds with TD and 2 spots that were down-regulated could not be identified. The up-regulated Ig belonged to IgM and IgY classes indicated by the identification of ‘mu’ chain and Fc fragment associated proteins respectively. Enzyme linked immunosorbent assay corroborated an increase in serum IgM but not IgG. Though the significance of the increase in IgM proteins in the serum of TD-affected chickens is not understood, it is likely that it plays some role in the removal of apoptotic chondrocytes which abound within TD lesions.