0397 : Arrestin like proteins co-purified with -enolase from bovine myocardial tissues, the possible role in heart diseases as an autoantigen

Abstract

Previously, we reported that visual arrestin co-purified with glycolytic enzymes. The aim of this study was to analyze the co-purification of arrestin like proteins (ALP) in bovine cardiac tissues with enolases. The soluble extract of bovine myocardial tissues from different regions such as left and right atriums and ventricles of the bovine heart (n= 3) was analyzed by ACA-34 gel filtration, immuno-affinity column, SDS-PAGE, ELISA, western blot and a sandwich immune assay for quantification of ALP and sequence analysis. we observed that; 1) The cardiac muscle contained a 50 kDa ALP at a concentration of 751 pg/mg of soluble protein extract, 2) ALP purified, by immunoaffinity, contained alpha-enolase of 48kDa confirmed by protein sequence analysis; 3) Cardiomyocyte cells exposed to anti arrestin and antienolase monoclonal antibodies showed decreased proliferation in vitro, 4) High level of autoantibodies were detected by ELISA (3.57% for arrestin and 9.12%for α-enolase) in serum of patients with infarcted heart disease. We suggest a possible interaction between ALP and alphaenolases yielding a complex that may be involved in the induction of cardiac autoimmune diseases (figure next page). : The present data suggested that arrestin like protein can associated with α-enolase and this pair can appear on the surface of the cell membrane as auto antigen ’C’. ( Mirshahi M., BBRC, 2015 May 8; 450(3):657-62 ) The author hereby declares no conflict of interest