Recombinant Human Cyclophilin A In Vitro Inhibits the Formation of Fibrin Clot

Morozov, Yu. A.; Хромых, Л. М.; Dementieva, I. I.; Charnaia, M. A.; Куликова, Н. А.; Kazansky, Dmitry

doi:10.32607/actanaturae.10655

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“…Upon activation, CyPA can also be released from platelets [14]. Notably, higher CyPA plasma concentrations were measured in patients with acute stroke [15][16][17][18][19][20][21][22][23] (as summarized in Supplementary Table S1), and platelet surface expression of CyPA has been found to be positively correlated with hypertension, hypercholesterolemia, and increased mortality of patients with symptomatic coronary artery disease (CAD) [24].…”

Section: Introductionmentioning

confidence: 99%

Cyclophilin A Is Not Acetylated at Lysine-82 and Lysine-125 in Resting and Stimulated Platelets

Rosa

Butt

Hopper

et al. 2022

IJMS

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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.

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