What is it about?
Due to the lack of an N-terminal signal peptide, SerpinB2 (plasminogen activator inhibitor type 2) accumulates in cells and only a small percentage of it is secreted. The extracellular concentration of SerpinB2 significantly increases during inflammation.
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Why is it important?
We investigated the mechanism with which SerpinB2 can be secreted from endothelial cells activated with LPS and evaluated its intracellular distribution by double immunogold labeling followed by a high resolution electron microscopy analysis. We found that SerpinB2 gathers in the vesicular structures and in the endothelial cell periphery.These vesicles stained positive for the trans-Golgi network marker TGN46, which is consistent with their formation by the endoplasmatic reticulum (ER) and Golgi-dependent pathways. SerpinB2 was delivered to the plasma membrane, apparently together with TGN46 in the same vesicles, which after fusion with the membranes released cargo.
Perspectives
Secretion of SerpinB2 was partially inhibited by brefeldin A. The secreted SerpinB2 was predominantly in its nonglycosylated 43 kDa form. Our data suggest that increased expression of SerpinB2 by an inflammatory stimulus is sufficient to generate structures that resemble secretory vesicles. These vesicles may represent the mechanism by which high local concentrations of SerpinB2 are released at inflammation sites from endothelial cells
Professor Elzbieta Wyroba
Nencki Institute of Experimental Biology
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This page is a summary of: Secretion of SerpinB2 from endothelial cells activated with inflammatory stimuli, Experimental Cell Research, May 2013, Elsevier,
DOI: 10.1016/j.yexcr.2013.02.018.
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