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，Higashi，，BBB。RIKENNaoshi DohmaeTakehiro Suzuki，Toidahiko Toidahiko，Amine PharmaIzuashi Kazuei，Rensselaer Polytechnic InstituteRobert J.
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：com/news/2021-02-scientists-therapy-blood-brain-barrier.
html">Scientists discover target for stroke therapy in blood-brain barrier
html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
(Image source:style="text-align: justify;">A group of researchers from Japan and the United States hope to explore how glycocalyx degradation occurs during ischemic stroke.
One of the researchers, Associate Professor Heihei Tokyo University of Science, explained the motivation of this study: "When brain tissue is necrotic due to ischemia, the function of the blood-brain barrier is destroyed, and immune cells penetrate into the brain, exacerbating inflammation.
But the details of this process are still unclear.
” The results were published in the Journal of Biological Chemistry.
One of the researchers, Associate Professor Heihei Tokyo University of Science, explained the motivation of this study: "When brain tissue is necrotic due to ischemia, the function of the blood-brain barrier is destroyed, and immune cells penetrate into the brain, exacerbating inflammation.
But the details of this process are still unclear.
” The results were published in the Journal of Biological Chemistry.
For the first time in the published research, a group of scientists led by Dr.
Higashi has identified a possible mechanism that links the accumulation of acrolein with glycocalyx modification, leading to damage to the BBB.
The team also includes Naoshi Dohmae and Takehiro Suzuki of RIKEN Sustainable Resources Science Center, Toidahiko Toidahiko of Chiba University, Izuashi Kazuei of Amine Pharma Research Institute, Robert J.
Linhardt of Rensselaer Polytechnic Institute, and Tomomi Furihata of Tokyo University of Pharmacology.
Higashi has identified a possible mechanism that links the accumulation of acrolein with glycocalyx modification, leading to damage to the BBB.
The team also includes Naoshi Dohmae and Takehiro Suzuki of RIKEN Sustainable Resources Science Center, Toidahiko Toidahiko of Chiba University, Izuashi Kazuei of Amine Pharma Research Institute, Robert J.
Linhardt of Rensselaer Polytechnic Institute, and Tomomi Furihata of Tokyo University of Pharmacology.
Researchers initially found that the main sugars in the glycocalyx, heparan sulfate and chondroitin sulfate, showed reduced levels in the "hyperacute phase" after stroke.
They also found that the activity of glycocalyx degrading enzymes such as hyaluronidase 1 and heparanase was enhanced.
After further in vitro studies using cell lines, they found that exposure to acrolein led to the activation of heparanase (proHPSE) precursors.
Specifically, they found that acrolein modifies specific amino acids on the structure of proHPSE, thereby activating it.
They concluded that this mechanism may lead to glycocalyx degradation and subsequent destruction of the blood-brain barrier.
They also found that the activity of glycocalyx degrading enzymes such as hyaluronidase 1 and heparanase was enhanced.
After further in vitro studies using cell lines, they found that exposure to acrolein led to the activation of heparanase (proHPSE) precursors.
Specifically, they found that acrolein modifies specific amino acids on the structure of proHPSE, thereby activating it.
They concluded that this mechanism may lead to glycocalyx degradation and subsequent destruction of the blood-brain barrier.
The team’s findings are critical, because acrolein-modified proHPSE may be a new and potentially effective drug target for post-stroke inflammation.
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
Information source: com/news/2021-02-scientists-therapy-blood-brain-barrier.
html">Scientists discover target for stroke therapy in blood-brain barrier
html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
For the first time in the published research, a group of scientists led by Dr.
Higashi has identified a possible mechanism that links the accumulation of acrolein with glycocalyx modification, leading to damage to the BBB.
The team also includes Naoshi Dohmae and Takehiro Suzuki of RIKEN Sustainable Resources Science Center, Toidahiko Toidahiko of Chiba University, Izuashi Kazuei of Amine Pharma Research Institute, Robert J.
Linhardt of Rensselaer Polytechnic Institute, and Tomomi Furihata of Tokyo University of Pharmacology.
Higashi has identified a possible mechanism that links the accumulation of acrolein with glycocalyx modification, leading to damage to the BBB.
The team also includes Naoshi Dohmae and Takehiro Suzuki of RIKEN Sustainable Resources Science Center, Toidahiko Toidahiko of Chiba University, Izuashi Kazuei of Amine Pharma Research Institute, Robert J.
Linhardt of Rensselaer Polytechnic Institute, and Tomomi Furihata of Tokyo University of Pharmacology.
Researchers initially found that the main sugars in the glycocalyx, heparan sulfate and chondroitin sulfate, showed reduced levels in the "hyperacute phase" after stroke.
They also found that the activity of glycocalyx degrading enzymes such as hyaluronidase 1 and heparanase was enhanced.
After further in vitro studies using cell lines, they found that exposure to acrolein led to the activation of heparanase (proHPSE) precursors.
Specifically, they found that acrolein modifies specific amino acids on the structure of proHPSE, thereby activating it.
They concluded that this mechanism may lead to glycocalyx degradation and subsequent destruction of the blood-brain barrier.
They also found that the activity of glycocalyx degrading enzymes such as hyaluronidase 1 and heparanase was enhanced.
After further in vitro studies using cell lines, they found that exposure to acrolein led to the activation of heparanase (proHPSE) precursors.
Specifically, they found that acrolein modifies specific amino acids on the structure of proHPSE, thereby activating it.
They concluded that this mechanism may lead to glycocalyx degradation and subsequent destruction of the blood-brain barrier.
The team’s findings are critical, because acrolein-modified proHPSE may be a new and potentially effective drug target for post-stroke inflammation.
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
Information source: com/news/2021-02-scientists-therapy-blood-brain-barrier.
html">Scientists discover target for stroke therapy in blood-brain barrier
html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
Researchers initially found that the main sugars in the glycocalyx, heparan sulfate and chondroitin sulfate, showed reduced levels in the "hyperacute phase" after stroke.
They also found that the activity of glycocalyx degrading enzymes such as hyaluronidase 1 and heparanase was enhanced.
After further in vitro studies using cell lines, they found that exposure to acrolein led to the activation of heparanase (proHPSE) precursors.
Specifically, they found that acrolein modifies specific amino acids on the structure of proHPSE, thereby activating it.
They concluded that this mechanism may lead to glycocalyx degradation and subsequent destruction of the blood-brain barrier.
They also found that the activity of glycocalyx degrading enzymes such as hyaluronidase 1 and heparanase was enhanced.
After further in vitro studies using cell lines, they found that exposure to acrolein led to the activation of heparanase (proHPSE) precursors.
Specifically, they found that acrolein modifies specific amino acids on the structure of proHPSE, thereby activating it.
They concluded that this mechanism may lead to glycocalyx degradation and subsequent destruction of the blood-brain barrier.
The team’s findings are critical, because acrolein-modified proHPSE may be a new and potentially effective drug target for post-stroke inflammation.
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
Information source: com/news/2021-02-scientists-therapy-blood-brain-barrier.
html">Scientists discover target for stroke therapy in blood-brain barrier
html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
The team’s findings are critical, because acrolein-modified proHPSE may be a new and potentially effective drug target for post-stroke inflammation.
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
As the study’s corresponding author, Dr.
Higashi, speculated, “Because proHPSE, not HPSE, is localized to external cells by binding to heparan sulfate proteoglycan, acrolein-modified proHPSE represents a promising target for protecting the endothelial glycocalyx.
” (Bioon.
com)
Information source: com/news/2021-02-scientists-therapy-blood-brain-barrier.
html">Scientists discover target for stroke therapy in blood-brain barrier
html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
Information source: com/news/2021-02-scientists-therapy-blood-brain-barrier.
html">Scientists discover target for stroke therapy in blood-brain barrier
Information source: com/news/2021-02-scientists-therapy-blood-brain-barrier. html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
html">Scientists discover target for stroke therapy in blood-brain barrier
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
DOI: 10.
1074/jbc.
RA120.
015105
Original source: Kenta Ko et al, Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure , Journal of Biological Chemistry (2020).
DOI: 10.
1074/jbc.
RA120.
015105
Original source: Ischemic stroke disrupts the endothelial glycocalyx through activation of proHPSE via acrolein exposure Journal of Biological ChemistryDOI: 10.
1074/jbc.
RA120.
015105
