Processing of type 1 plasminogen activator inhibitor (PAI-1) into the regulated secretory pathway.

摘要: To understand the processing of type 1 plasminogen activator inhibitor (PAI-1) into storage granules platelets, we utilized a eukaryotic expression vector (pRC/CMV) to transfer human cDNA for PAI-1 AtT-20 cells, mouse pituitary cell line known sort proteins in regulated fashion. Immunofluorescence staining PAI-1-transfected clones revealed co-localization with an endogenously produced and stored hormone (i.e. adrenocorticotropic hormone, ACTH). Stimulation cells secretagogue resulted release both active latent form. In comparison, Chinese hamster ovary nonpackaging line) did not response exhibited immunoreactivity primarily confined Golgi region. Percoll density gradient fractionation codistribution ACTH cellular compartments same density. The half-life activity at 37 degrees C was prolonged intact (t1/2, 5 h) comparison its lysed 2 h). These studies demonstrate presence new functional property associated molecule that directs this secretory pathway.