Deans' stroke musings: Key protein responsible for controlling communication between brain cells identified

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.

Thursday, November 28, 2013

Key protein responsible for controlling communication between brain cells identified

You will have to ask someone else to tell how to put this into a stroke protocol. A great stroke association would do it if we had one.
A writeup on it here:
http://phys.org/news/2013-11-key-protein-responsible-brain-cells.html
The abstract here:
http://www.nature.com/emboj/journal/v32/n11/full/emboj201365a.html

Chun Guo¹, Keri L Hildick¹, Jia Luo¹, Laura Dearden¹, Kevin A Wilkinson¹ and Jeremy M Henley¹

School of Biochemistry, University of Bristol, University Walk, Bristol, UK

Correspondence to:

Jeremy M Henley, School of Biochemistry, University of Bristol, University Walk, Medical Sciences Building, Bristol BS8 1TD, UK. Tel.:+44 (0)117 331 1945; Fax:+44 (0)117 331 2168; E-mail: j.m.henley@bristol.ac.uk

Received 9 January 2013; Accepted 27 February 2013

Global increases in small ubiquitin-like modifier (SUMO)-2/3 conjugation are a neuroprotective response to severe stress but the mechanisms and specific target proteins that determine cell survival have not been identified. Here, we demonstrate that the SUMO-2/3-specific protease SENP3 is degraded during oxygen/glucose deprivation (OGD), an in vitro model of ischaemia, via a pathway involving the unfolded protein response (UPR) kinase PERK and the lysosomal enzyme cathepsin B. A key target for SENP3-mediated deSUMOylation is the GTPase Drp1, which plays a major role in regulating mitochondrial fission. We show that depletion of SENP3 prolongs Drp1 SUMOylation, which suppresses Drp1-mediated cytochrome c release and caspase-mediated cell death. SENP3 levels recover following reoxygenation after OGD allowing deSUMOylation of Drp1, which facilitates Drp1 localization at mitochondria and promotes fragmentation and cytochrome c release. RNAi knockdown of SENP3 protects cells from reoxygenation-induced cell death via a mechanism that requires Drp1 SUMOylation. Thus, we identify a novel adaptive pathway to extreme cell stress in which dynamic changes in SENP3 stability and regulation of Drp1 SUMOylation are crucial determinants of cell fate.