Location of the major epsilon-(gamma-glutamyl)lysyl cross-linking site in transglutaminase-modified human plasminogen.
Tissue and plasma transglutaminases cross-link human plasminogen into high molecular weight complexes (Bendixen, E., Borth, W., and Harpel, P. C. (1993) J. Biol. Chem. 268, 21962-21967). A major cross-linking site in plasminogen involved in the tissue transglutaminase-mediated polymerization process has been identified. The epsilon-(gamma-glutamyl)lysyl bridges of the polymer are formed between Lys-298 and Gln-322. Both the acyl donor Gln residue and the acyl acceptor Lys residue are located in the kringle 3 domain of plasminogen, i.e. cross-linking of plasminogen by tissue transglutaminase involves neither the catalytic domain nor the lysine-dependent binding sites of plasminogen. This study documents that kringle 3 contains a novel functional site with the potential to participate in transglutaminase-mediated cross-linking interactions with plasma, cell-surface, and extracellular proteins.
Bendixen
E
E
Department of Molecular Biology, University of Aarhus, Denmark.
Harpel
P C
PC
Sottrup-Jensen
L
L
D000595:Amino Acid Sequence; D000818:Animals; D003432:Cross-Linking Reagents; D005973:Glutamine / Q000737:chemistry*; D006168:Guinea Pigs; D006801:Humans; D008239:Lysine / Q000737:chemistry*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010958:Plasminogen / Q000737:chemistry*; D011487:Protein Conformation; D011503:Transglutaminases / Q000737:chemistry*; D014357:Trypsin / Q000737:chemistry
D003432:Cross-Linking Reagents; D005973:Glutamine; D010958:Plasminogen; D011503:Transglutaminases; D014357:Trypsin; D008239:Lysine