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Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure

Kenta Ko, Takehiro Suzuki, Ryota Ishikawa, Natsuko Hattori, Risako Ito, Kenta Umehara, Tomomi Furihata, Naoshi Dohmae, Robert J. Linhardt, Kazuei Igarashi, Toshihiko Toida, Kyohei Higashi

2020Journal of Biological Chemistry40 citationsDOIOpen Access PDF

Abstract

, located in the immediate vicinity of the 6-kDa linker, at least in part is attributed to the activation of proHPSE. Because proHPSE, but not HPSE, localizes outside cells by binding with heparan sulfate proteoglycans, ACR-modified proHPSE represents a promising target to protect the endothelial glycocalyx.

Topics & Concepts

GlycocalyxHeparanaseHeparan sulfateInflammationChemistryBlood–brain barrierGlycosaminoglycanMedicineImmunologyCell biologyBiochemistryInternal medicineBiologyCentral nervous systemTrauma, Hemostasis, Coagulopathy, ResuscitationNeuroscience of respiration and sleepNeutrophil, Myeloperoxidase and Oxidative Mechanisms
Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure | Litcius