Physarum vitronectin-like protein has extensive homology to dihydrolipoamide acetyltransferase.

Abstract

Physarum vitronectin-like protein with a molecular mass of 70 kDa cross-reacts with anti-bovine vitronectin and promotes cell-spreading (Miyazaki, K. et al. 1992. Exp. Cell Res., 199: 106-110.). The amino-terminal sequence of Physarum vitronectin-like protein is, however, distinct from those of animal vitronectins but shows significant sequence homology with dihydrolipoamide acetyltransferase, a component of pyruvate dehydrogenase complex. We have investigated the structural relationships between Physarum vitronectin-like protein and dihydrolipoamide acetyltransferase by using both antibody and protein-chemical methods. The vitronectin-like protein reacted with both anti-bovine vitronectin IgG and anti-rat pyruvate dehydrogenase complex IgG, indicating that it shares common antigenic determinant(s) with rat pyruvate dehydrogenase complex. Furthermore, sequencing studies of peptides obtained by lysylendopeptidase digestion indicated that internal sequences of Physarum vitronectin-like protein show significant homology with dihydrolipoamide acetyltransferase, but do not show any homology with the primary structures of authentic vitronectins. Immunocytochemistry revealed that the protein is widely localized in cytoplasm and nuclei of Physarum polycephalum, but is not present in the central area of vacuoles. Our results indicate that Physarum vitronectin-like protein is a molecule structurally and immunologically related to dihydrolipoamide acetyltransferase but functionally similar to animal vitronectin, although its localization is unique.