Interaction of Human Tissue Plasminogen Activator (t-PA) with Pregnancy Zone Protein. A Comparative Study to t-PA-á2-Macroglobulin Interaction".

SÁNCHEZ MC; CHIABRANDO GA; GUGLIELMONE H; BONACCI G; RABINOVICH G; VIDES MA

JOURNAL OF BIOCHEMISTRY

OXFORD UNIV PRESS

Año: 1998 vol. 124 p. 274 - 274

0021-924X

h3 class="abstract_label">Abstract Human pregnancy zone protein (PZP) is a major pregnancy-associated plasma protein strongly related to alpha2-macroglobulin (alpha2-M). Interactions of tissue plasminogen activator (t-PA) with PZP and alpha2-M were both investigated in vitro and the complexes were analyzed by polyacrylamide gel electrophoresis (PAGE). The results demonstrated that PZP-t-PA complex formation was evident within 1 h of incubation, whereas alpha2-M-t-PA complexes were formed after 18 h. Conclusions were supported by the following evidence: (i) PZP and alpha2-M complexes revealed changes of the mobility rate in non-denaturing PAGE, similar to those observed with alpha-Ms-chymotrypsin; (ii) both PZP and alpha2-M formed complexes of molecular size >360 kDa by SDS-PAGE, in accordance with the covalent binding of t-PA, which was previously reported for other proteinases; and (iii) PZP underwent a specific cleavage of the bait region with appearence of fragments of 85-