Picture of Open Access badges

Discover Open Access research at Strathprints

It's International Open Access Week, 24-30 October 2016. This year's theme is "Open in Action" and is all about taking meaningful steps towards opening up research and scholarship. The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. Explore recent world leading Open Access research content by University of Strathclyde researchers and see how Strathclyde researchers are committing to putting "Open in Action".


Image: h_pampel, CC-BY

Differential effect of extracellular acidosis on the release and dispersal of soluble and membrane proteins secreted from the weibel-palade body

Babich, Victor and Knipe, Laura and Hewlett, Lindsay and Meli, Athinoula and Dempster, J. and Hannah, Matthew J. and Carter, Tom (2009) Differential effect of extracellular acidosis on the release and dispersal of soluble and membrane proteins secreted from the weibel-palade body. Journal of Biological Chemistry, 284 (18). pp. 12459-12468. ISSN 0021-9258

Full text not available in this repository. (Request a copy from the Strathclyde author)


Proteins secreted from Weibel-Palade bodies (WPBs) play important roles in regulating inflammatory and hemostatic responses. Inflammation is associated with the extracellular acidification of tissues and blood, conditions that can alter the behavior of secreted proteins. The effect of extracellular pH (pHo) on the release of von Willebrand factor (VWF), the VWF-propolypeptide (Proregion), interleukin-8, eotaxin-3, P-selectin, and CD63 from WPBs was investigated using biochemical approaches and by direct optical analysis of individual WPB fusion events in human endothelial cells expressing green or red fluorescent fusions of these different cargo proteins. Between pHo 7.4 and 7.0, ionomycin-evoked WPB exocytosis was characterized by the adhesion of VWF to the cell surface and the formation of long filamentous strands. The rapid dispersal of Proregion, interleukin-8, and eotaxin-3 into solution, and of P-selectin and CD63 into the plasma membrane, was unaltered over this pHo range. At pHo 6.8 or lower, Proregion remained associated with VWF, in many cases WPB failed to collapse fully and VWF failed to form filamentous strands. At pHo 6.5 dispersal of interleukin-8, eotaxin-3, and the membrane protein CD63 remained unaltered compared with that at pHo 7.4; however, P-selectin dispersal into the plasma membrane was significantly slowed. Thus, extracellular acidification to levels of pHo 6.8 or lower significantly alters the behavior of secreted VWF, Proregion, and P-selectin while rapid release of the small pro-inflammatory mediators IL-8 and eotaxin-3 is essentially unaltered. Together, these data suggest that WPB exocytosis during extracellular acidosis may favor the control of inflammatory processes.