Bovine hereditary
dilated cardiomyopathy (
bCMP) is endemic in Switzerland and hearts from diseased animals display important clinical and biochemical similarities to human DCM. Recent research has identified at least one
protein (
myoglobin) to be significantly reduced in bovine DCM. Using a proteomic approach, we have separated over 1125
protein species from bovine ventricular tissue. Gel analysis and
protein characterisation have identified a number of
proteins whose abundance is significantly altered in bovine DCM. Twenty-four
proteins are of decreased abundance in diseased tissue, whilst 11
proteins are of increased abundance in the diseased state. A combination of
amino acid compositional analysis,
peptide mass profiling, N-terminal microsequencing and MultiIdent (http://www.expasy.ch/sprot/multiident. html) has been employed in order to elucidate the identities of the differentially expressed
proteins. Using these techniques we have currently determined the identity of 12 of the 35 altered
proteins. We have also detected three
proteins that are differentially expressed in genotypically diseased but phenotypically normal animals, identifying a possible mechanism for the onset of the disease. The possibility that inappropriate ubiquination of
proteins plays an important role in the disease is discussed. A database of bovine
proteins is currently being established. The identity of the
proteins affected, together with a comparison of the human and bovine expression patterns, is displayed.