The sequence 581Ser-610Val in the fibrinogen Aα chain is responsible for the formation of complexes between plasminogen and αC-regions of fibrin(ogen).

ABSTRACT:

Objective

This study aimed to identify the binding sites for plasminogen (Pg) and its kringle-containing fragments within the αC-region of fibrin(ogen). This investigation is crucial while the conversion of fibrinogen into fibrin induces conformational changes that expose binding sites for Pg and tissue-type Pg activator (tPA), facilitating effective zymogen activation on the fibrin surface.

Methods

Two C-terminal fragments of the Aα chain ‒ 45 kDa (225Val-610Val) and 40 kDa (225Val-580Lys), were obtained through plasmin hydrolysis of human fibrinogen and subsequently characterized using MALDI TOF mass spectrometry. The interactions of Glu-Pg and Lys-Pg, as well as Pg kringle fragments (K1-3, K4, and K5), with the obtained αC truncated polypeptides were analyzed using ELISA

SUBMITTER: Kapustianenko L 

PROVIDER: S-EPMC11648866 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature