| pubmed-article:7826363 | pubmed:abstractText | Chemically synthesized human midkine enhanced plasminogen activator activity and decreased its inhibitor levels in bovine aortric endothelial cells. These activities were preserved in the C-terminal half, but not in the N-terminal half of the midkine molecule. Furthermore, a synthetic peptide of 43 amino acids designated as "C-domain", which formed the compact structure held by two disulfide bonds in the C-terminal half, mimicked intact midkine. Chemically synthesized C-domain of pleiotrophin (43 amino acids), which was 53% identical to midkine C-domain in amino acid sequence, expressed the similar activities. These 43 amino acid peptides are, so far, the shortest peptide able to enhance the fibrinolytic activities of the endothelial cells. | lld:pubmed |
