@article{UngernSternbergZerneckeSeizer2018,
  author    = {Ungern-Sternberg, Saskia N. I. von and Zernecke, Alma and Seizer, Peter},
  title     = {Extracellular matrix metalloproteinase inducer EMMPRIN (CD147) in cardiovascular disease},
  series = {International Journal of Molecular Sciences},
  volume    = {19},
  journal   = {International Journal of Molecular Sciences},
  number    = {2},
  issn      = {1422-0067},
  doi       = {10.3390/ijms19020507},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-285014},
  year      = {2018},
  abstract  = {The receptor EMMPRIN is involved in the development and progression of cardiovascular diseases and in the pathogenesis of myocardial infarction. There are several binding partners of EMMPRIN mediating the effects of EMMPRIN in cardiovascular diseases. EMMPRIN interaction with most binding partners leads to disease progression by mediating cytokine or chemokine release, the activation of platelets and monocytes, as well as the formation of monocyte-platelet aggregates (MPAs). EMMPRIN is also involved in atherosclerosis by mediating the infiltration of pro-inflammatory cells. There is also evidence that EMMPRIN controls energy metabolism of cells and that EMMPRIN binding partners modulate intracellular glycosylation and trafficking of EMMPRIN towards the cell membrane. In this review, we systematically discuss these multifaceted roles of EMMPRIN and its interaction partners, such as Cyclophilins, in cardiovascular disease.},
  language  = {en}
}
@article{RosaButtHopperetal.2022,
  author    = {Rosa, Annabelle and Butt, Elke and Hopper, Christopher P. and Loroch, Stefan and Bender, Markus and Schulze, Harald and Sickmann, Albert and Vorlova, Sandra and Seizer, Peter and Heinzmann, David and Zernecke, Alma},
  title     = {Cyclophilin a is not acetylated at lysine-82 and lysine-125 in resting and stimulated platelets},
  series = {International Journal of Molecular Sciences},
  volume    = {23},
  journal   = {International Journal of Molecular Sciences},
  number    = {3},
  issn      = {1422-0067},
  doi       = {10.3390/ijms23031469},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-284011},
  year      = {2022},
  abstract  = {Cyclophilin A (CyPA) is widely expressed by all prokaryotic and eukaryotic cells. Upon activation, CyPA can be released into the extracellular space to engage in a variety of functions, such as interaction with the CD147 receptor, that contribute to the pathogenesis of cardiovascular diseases. CyPA was recently found to undergo acetylation at K82 and K125, two lysine residues conserved in most species, and these modifications are required for secretion of CyPA in response to cell activation in vascular smooth muscle cells. Herein we addressed whether acetylation at these sites is also required for the release of CyPA from platelets based on the potential for local delivery of CyPA that may exacerbate cardiovascular disease events. Western blot analyses confirmed the presence of CyPA in human and mouse platelets. Thrombin stimulation resulted in CyPA release from platelets; however, no acetylation was observed—neither in cell lysates nor in supernatants of both untreated and activated platelets, nor after immunoprecipitation of CyPA from platelets. Shotgun proteomics detected two CyPA peptide precursors in the recombinant protein, acetylated at K28, but again, no acetylation was found in CyPA derived from resting or stimulated platelets. Our findings suggest that acetylation of CyPA is not a major protein modification in platelets and that CyPA acetylation is not required for its secretion from platelets.},
  language  = {en}
}