Changing stroke rehab and research worldwide now.Time is Brain! trillions and trillions of neurons that DIE each day because there are NO effective hyperacute therapies besides tPA(only 12% effective). I have 523 posts on hyperacute therapy, enough for researchers to spend decades proving them out. These are my personal ideas and blog on stroke rehabilitation and stroke research. Do not attempt any of these without checking with your medical provider. Unless you join me in agitating, when you need these therapies they won't be there.

What this blog is for:

My blog is not to help survivors recover, it is to have the 10 million yearly stroke survivors light fires underneath their doctors, stroke hospitals and stroke researchers to get stroke solved. 100% recovery. The stroke medical world is completely failing at that goal, they don't even have it as a goal. Shortly after getting out of the hospital and getting NO information on the process or protocols of stroke rehabilitation and recovery I started searching on the internet and found that no other survivor received useful information. This is an attempt to cover all stroke rehabilitation information that should be readily available to survivors so they can talk with informed knowledge to their medical staff. It lays out what needs to be done to get stroke survivors closer to 100% recovery. It's quite disgusting that this information is not available from every stroke association and doctors group.

Friday, May 17, 2013

SUMO wrestling cells reveal new protective mechanism target for stroke

A great name for a brain protein.
http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html
The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal search and more info website Provided by University of Bristol search and more info website

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp
 The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal search and more info website Provided by University of Bristol search and more info website

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp
The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp
The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp
The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal search and more info website Provided by University of Bristol search and more info website

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp
The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal search and more info website Provided by University of Bristol search and more info website

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp
The discovery, made by researchers from the University's School of Biochemistry and published in the EMBO journal with additional comment in Nature Reviews, could eventually lead to new therapies for stroke and other brain diseases. The research builds on earlier work by the team which identified a protein, known as SUMO, responsible for controlling the chemical processes which reduce or enhance protection mechanisms for nerve cells in the brain. The team's latest work has now identified the key role that SUMO plays in promoting cell survival. During cell stress a protein response triggers a protective mechanism that allows cell adaptation and survival. This process, known as SUMOylation, involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. This pathway is essential for survival of all plant and animal cells because it regulates how proteins interact with each other and can protect nerve cells against damage. The findings have shown that SUMOylation of a protein called dynamin-related protein 1 (Drp1) is particularly important because it controls the release of chemical signals from mitochondria that instruct the cell to die in a process called apoptosis. SUMOylation of Drp1 reduces mitochondrial release of these 'death' signals and helps nerve cells survive toxic insults associated with stroke. In the future, finding effective methods to enhance SUMOylation of Drp1 may also be beneficial for cell survival in other diseases including heart attacks and Alzheimer's disease. The European Research Council-funded study, entitled 'SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia' published in the EMBO Journal and led by Professor Jeremy Henley from the University's School of Biochemistry. More information: doi:10.1038/emboj.2013.65 Journal reference: EMBO Journal search and more info website Provided by University of Bristol search and more info website

Read more at: http://medicalxpress.com/news/2013-05-sumo-cells-reveal-mechanism.html#jCp

1 comment:

  1. I'm not sure I like that name, sumo wrestlers are morbidly obese.

    ReplyDelete