Abstract
Simple Summary The most common cardiomyopathy in feline is hypertrophic cardiomyopathy (HCM) that is recognized as an inheritance of autosomal dominant transmission in some cats. Feline HCM has been associated with the mutation of the myosin-binding protein C3 (MYBPC3) gene in several locations with a specific breed. Recently, the proteomic analyzed by mass spectrometry is a promising novel approach to characterize the specific pattern of peptide and protein for relatively clinical biomarkers. However, there has been only limited knowledge of differential peptides and proteins related to the MYBPC3 gene mutation. Therefore, this study aimed to investigate the MYBPC3 gene mutation in Bengal cats with HCM. In combined with mass spectrometry, we purposed to identify the potential peptide candidates and expected proteins. The obtained findings of specific peptides and proteins from mass spectrometry may contribute to the development of novel diagnostic tools for feline HCM related to the MYBPC3 gene mutation. Further, this observation appears to be useful information such as a database of peptidomics library in veterinary medicine for the future diagnosis of feline cardiomyopathy associated with gene mutation. This study aimed to identify the potential peptide candidates and expected proteins associated with MYBPC3-A74T gene mutations in Bengal cats and determine if peptidome profiles differ between healthy controls and cats with MYBPC3-A74T gene mutations. All animals were evaluated using echocardiography. DNA was isolated and followed by the screening test of MYBPC3 gene mutation. The MALDI-TOF mass spectrometry was conducted for analyzing the targeted peptide and protein patterns. The expected protein candidates were searched for within the NCBI database. Our results demonstrated that the MYBPC3-A74T gene mutation was dominant in Bengal cats but not in domestic shorthair cats. Correlations between baseline characteristics and echocardiographic parameters were discovered in Bengal cats. Mass spectrometry profiles of the candidate proteins were suspected to accompany the cat with the MYBPC3-A74T gene mutation, involving integral protein-membrane, organization of nucleus, DNA replication, and ATP-binding protein. Therefore, MYBPC3-A74T gene mutations occur frequently in Bengal cat populations. The high incidence of homozygotes for the mutation supports the causal nature of the MYBPC3-A74T mutation. In addition, peptidomics analysis was established for the first time under this condition to promise a complementary technique for the future clinical diagnosis of the MYBPC3-A74T mutation associated with physiological variables and cardiac morphology in cats.
