Changes in serum protein profiles of chickens with tibial dyschondroplasia

by Rasaputra, K. S.; Liyanage, R.; Lay, J. O.; Erf, G. F.; Okimoto, R.; Rath, N. C.

Differences in serum protein profiles were analyzed to identify possible biomarkers assocd. with a poultry leg problem named tibial dyschondroplasia (TD) that can lead to lameness. A bead-based affinity matrix (ProteoMiner) contg. a combinatorial library of hexapeptides was used to deplete high abundant proteins and enrich the less abundant ones to compare between the sera of 6-wk-old normal and TD affected chickens. Equal amts. of proteins in ProteoMiner depleted serum from control and TD-affected birds were subject to 2-dimensional gel electrophoresis, image anal., and compared to identify the differentially expressed protein spots. The protein spots were characterized using in-gel trypsin digestion followed by mass spectrometry (MS). Of 46 matched protein spots in the gels, 33 were identified by peptide mass finger printing (PMF) and tandem mass spectrometry (MS/MS). Eight spots corresponding to Igs were up-regulated in birds with TD and 2 spots down regulated. The up-regulated Ig proteins belonged to IgM and IgY (IgG) classes indicated by the identification of µ-chain and Fc fragment assocd. peptides resp. Enzyme linked immunosorbent assay corroborated an increase in serum IgM levels but not IgG. Although the significance of the increase in IgM proteins in the serum of TD-affected chickens is not understood, it is likely that IgM plays some role in the removal of apoptotic chondrocytes which abound within TD lesions.

Open Proteomics Journal
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