This study reports the presence of scinderin in fetal and adult testes, epididymides, spermatozoa, the aorta, and the vena cava. The antiserum #6 we used to generate these data has been characterized in numerous published reports. These reports show that the scinderin antiserum we used in the present study recognizes only a protein with a molecular mass of 80 kDa and that the antibody does not cross-react with gelsolin, another actin filament-severing protein of a 90-kDa molecular mass. Thus, it is highly unlikely that the weak band we observed at 90 kDa in some of the testis samples we analyzed would correspond to gel-solin. Moreover, gelsolin has been documented in chromaffin cells and in spermatozoa.
However, under our experimental conditions, there was no band at 90 kDa in chromaffin cells and spermatozoa. Therefore, on the basis of these data, we believe that the weaker band at 90 kDa is not gelsolin but probably reflects a testicular protein that may have some cross-reactivity with scinderin antiserum #6. However, we observed no immunolabeling in paraffin sections of bovine testes treated with preadsorbed scinderin antiserum #6.