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Thread: HBOT-HyperBaric Oxygen Therapy

  1. #1
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    Question HBOT-HyperBaric Oxygen Therapy

    Hi everyone

    Has anyone had experience of HBOT (Hyperbaric Oxygen therapy?).
    There is not much information around, but of the reviews I have managed to find the results seem mixed.
    My father has recently been diagnosed with PBP, and I wonder whether he would find this treatment helpful with regard to his comfort. At the moment he has trouble swallowing and has an affected voice; some of the reviews I have read claim HBOT can slow the progression of these symptoms, but I wonder if I am getting my hopes up for a pipe dream.

    Any experiences / thoughts/ advice would be greatly appreciated

  2. #2
    Forum Member Newbie17's Avatar
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    Hi Totigal
    I've tried this therapy, had about 6 sessions a year ago. I had problems getting a mask to fit airtight and found them heavy and uncomfortable. I thought it was worth a try, other people using it seemed to have either MS or cancer.
    I couldn't find evidence to prove it was beneficial or not. Placebo effect maybe? It made me feel proactive and empowered that I was fighting my illness as best I could.
    Best of luck
    Helen

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    Thank you Helen, I appreciate your response

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    Forum Member Terry's Avatar
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    Hi Totigal;

    I looked into it and reckon it could do noting but good. How much good it would do is questionable.

    I was going to try it but the amount of time needed for a few weeks was quite hard to arrange because I could only get in one chamber that was not used so often. Also I do have some claustrophobia.

    I think our chamber was set up with help from the MS society and those got a reduced rate which is probably why it's not so popular for Mnd people.

    Love Terry

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    Hi Terry.

    The clinic I have found is an MS clinic but they seem to have a flat rate. I think I will bring it to my father's attention and see how he feels about giving it a go.

    Thank you for your help :-)

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    I did the 'dives' at an MS Therapy centre. Think I paid £20 to join and around £10 for each dive. You build up to a deeper level.
    You're in the chamber for about an hour, with up to 6 people.
    You can read and have wifi! It's a bit weird the first time!

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    Quote Originally Posted by Newbie17 View Post
    I did the 'dives' at an MS Therapy centre. Think I paid £20 to join and around £10 for each dive. You build up to a deeper level.
    You're in the chamber for about an hour, with up to 6 people.
    You can read and have wifi! It's a bit weird the first time!
    Thanks! Did you feel it had any effect in your symptoms (if you don't mind me asking)?

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    AN ARTICLE TODAY IN ALS NEWS

    #AAN2018 – H.P. Acthar Gel Shows Promise as Therapy to Delay Progression of ALS
    APRIL 20, 2018 Patricia InacioBY PATRICIA INACIO IN NEWS.
    #AAN2018 – H.P. Acthar Gel Shows Promise as Therapy to Delay Progression of ALS

    H.P. Acthar Gel, an experimental injectable therapy, may help delay progression of amyotrophic lateral sclerosis (ALS), a new analysis reveals.

    The data is scheduled to be presented at the 70th annual meeting of the American Academy of Neurology (AAN) in Los Angeles, April 21–27, in a presentation titled, “Post hoc analysis using PRO-ACT database to evaluate Repository Corticotropin Injection (H.P. Acthar® Gel) as a potential treatment for ALS.” The presentation is part of a session titled General Neurology.

    Researchers explored the effects of H.P. Acthar Gel (repository corticotropin injection, or RCI) on disease progression in adults with ALS. The therapy, sold under the brand name Acortan (among others) is used in several inflammatory diseases, including multiple sclerosis and systemic lupus erythematosus.

    The therapy is under investigation for ALS and received U.S. Food and Drug Administration (FDA) fast track designation and orphan drug status.

    H.P. Acthar Gel, developed by Mallinckrodt, contains a highly purified preparation of the adrenocorticotropic hormone (ACTH) and may have anti-inflammatory, neuroprotective, and neuroregenerative effects that could delay or even halt ALS progression.

    ACTH stimulates the release of naturally produced steroid hormones by the adrenal gland, located on top of the kidneys, such as cortisol, corticosterone, and aldosterone. These steroid hormones are involved in the regulation of many biological functions, including immune response, metabolism, and blood pressure.

    Researchers used data from two studies — a pilot study of RCI and the Pooled Resource Open-Access ALS Clinical Trials (PRO-ACT) database — to assess the impact of the therapy on ALS progression.

    In the pilot study, ALS patients were randomized to receive subcutaneous injections of H.P. Acthar Gel (16 U, 0.2 mL) or a volume-matched placebo once daily for 36 weeks. In total, 43 ALS patients received H.P. Acthar Gel.

    Following the 36 weeks, participants either stop the treatment or continue daily H.P. Acthar Gel injections during a 48-week open-label extension phase.

    The study main outcome is to assess the changes from baseline up to the 36 weeks in the ALS Functional Rating Scale (ALSFRS). Researchers analysed this parameter every month. Additional parameters evaluated include decline in pulmonary function test scores, survival, and occurrence of adverse events.

    Researchers also performed a case-matched control analysis using placebo-treated patients from PRO-ACT. H.P. Acthar Gel-treated patients were paired with up to three patients from PRO-ACT using seven variables associated with disease progression.

    At baseline, the mean ALSFRS scores were 27.8 in the H.P. Acthar Gel-treated group and 27.2 in the PRO-ACT control group.

    The case-match control analysis revealed that after 36 weeks of treatment, the ALSFRS scores of H.P. Acthar Gel-treated patients declined by a mean of 4.3 points and by 6.6 points in the control group – a statistically significant difference.

    For the post-hoc analysis (looking at the data after a study has been concluded), researchers generated a prediction algorithm that used the baseline characteristics to generate a 36-week estimate of patients’ response. They compared it to the changes in ALSFRS scores from the H.P. Acthar Gel pilot study.

    For the 21 patients who completed the study, the changes in progression in ALSFRS scores were smaller, but still similar to that predicted by the algorithm.

    Overall, these results “suggest potential RCI efficacy in the treatment of ALS and support further study of RCI for ALS in controlled trials,” researchers concluded.

    AN INTERESTING STEP FORWARD - ANNB

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    MND REARCH BLOG (MNDA)
    Stuck in FUS – the story of arginines, MND and FTD

    APRIL 22, 2018 MARTINA SLAPKOVAL
    In recent news, a number of press releases highlighted a paper published in the journal Cell, in which scientists, under the leadership of the University of Toronto’s Professor Peter St George-Hyslop, and in collaboration with University of Cambridge, described the process of how the FUS protein leads to the development of motor neurone disease (MND) and frontotemporal dementia (FTD).

    MND and FTD – what is the connection?

    We know that there is a link between MND and FTD, which in most part is caused by a mutation in the C9ORF72 gene, causing familial MND in around 35% of people with the disease and FTD in 25% of cases. Mistakes in the gene disrupt normal processes leading to toxic accumulation of TDP-43 protein in the neurons, and their subsequent death. There is however another protein toxic to neurons which results in the development of MND and FTD – the one that makes it slightly easier for us science writers to come up with witty titles: FUS (see one of our previous articles ‘What’s the FUS all about’).

    Specifically, this gene mutation is found in about 4% of people with familial MND and around 1% with sporadic MND. The corrupted FUS gene leads to mistakes in the way FUS protein completes its main role; that is, helping to transport RNA and essential cargos along the cell (especially to the axon and dendrites – projections of the cell body). The FUS protein then gets trapped in the neuron where it forms aggregates. Interestingly, while in FTD this incorrect functioning of the FUS protein is still observed, it hasn’t yet been shown that this is due to a mutation in the FUS gene. (Read more about MND, FTD and FUS in a paper by Nolan et al. (2016).)

    So what is the news?

    All of the above information is a pretty established knowledge by now. So what did the new paper show? The main purpose of the study was to investigate the exact process by which the FUS protein creates clumps in the neurons and how this could potentially be prevented.

    The FUS protein is able to undergo reversible state change, a so called ‘phase transition’– this allows switching from a dispersed liquid form to a droplet-like state or gel-like aggregates (also called phase separation – as the liquid separates into compartments) to accommodate to its surroundings. This property is required for FUS to form temporary structures that take up, transport, and then release important cargos that control the efficient function and survival of synapses at the distant connecting end of neurons, the synapse.

    In healthy cells, FUS can easily switch between the three states to fulfil its role to transport RNA in the solid form and release it as it turns into liquid. In neurodegenerative diseases, and specifically MND and FTD, the FUS protein can get stuck in the solid form, trapping the RNAs and form toxic aggregations within the cell. Understanding how this ‘reversible phase transition’ works is crucial to understand the disease and highlight potential therapeutic targets.

    Phase transition
    Three states of the FUS protein: dispersed, droplets, and gel-like.
    The researchers attributed the fault to an improper ‘methylation’ of the FUS protein. One of the properties of the FUS protein is that, in order to function properly, it attaches a chemical structure called the ‘methyl group’ to one of its amino acids – arginine (remember that proteins are composed of a number of amino acids that are dependent on the sequence of chemical bases in DNA). In normally-functioning FUS, the arginine amino acids making up the protein are heavily methylated.

    In FTD however, the FUS protein is ‘hypomethylated’ (hypo = less than the norm) which leads to toxic accumulation of FUS in neurons. What is more, hypomethylation of only less than 5% of the FUS protein can result in triggering of the irreversible gel-like state. It has therefore been suggested that fluctuations in arginine methylation might be responsible for controlling the ability of FUS to be able to undergo reversible state change. So what can we do with these findings?

    Using a number of experiments, the liquid/solid state of FUS was manipulated by using varying levels of salts. This led to the observation that reducing salt levels results in less dispersed state and increased phase separation (i.e. formation of droplets). The researchers could then observe the circumstances under which FUS will stay in the dispersed form even in the lowest salt levels. And indeed, when the affected arginine was replaced with other amino acids, or when other amino acids within FUS were reshuffled, the phase separation process was not observed (and the FUS protein stayed in the liquid form).

    Next, the team investigated this using frog neurons to clearly visualise nerve axons and their endings, which is where ‘the real action’ occurs (i.e. where the electrical signal is transmitted from one neuron to another). The group mutated the FUS protein in the neurons by either reducing the number of building blocks of the protein that could be methylated, or by introducing changes in order to increase aggregation of the FUS protein.

    The team demonstrated that a protein called Transportin1 acts as chaperone – assistant and guide – that prevents the FUS protein from aggregating in the neuronal nucleus. By tagging the transportin with a fluorescent marker, they could see its movement with the FUS protein attached along the axon. This showed the importance of Transportin1 to maintain the ability of FUS to transition normally and to potentially ‘rescue’ some of the aggregation of the FUS protein.

    This important work shows that the protein Transportin1 and the methylation of arginine, building block of the FUS protein, play a vital role in preventing aggregation of the protein in MND and FTD. By identifying the specific changes that may stop the formation of the toxic aggregates in FUS, the race is now on to use enzymes that can modulate the amino acids in FUS and have a protective role for the protein (keep it from turning into the irreversible solid state).

    How does this fall into the ‘finding a cure’ puzzle?

    Year on year we see an increase in the number of significant findings that lead us closer to solving the MND cause/cure puzzle faster. The study described above is a great example of this; while it is not THE solution we are all hoping for, it provides a clearer picture of one segment of the whole MND jigsaw. Techniques that were used to find out how FUS behaves, how it can be manipulated and what can prevent its toxic aggregation, can be translated into studying different variations of MND, also caused by toxic aggregation of a protein (such as TDP-43 or SOD1).

    RESEARCH IS HOPEFULLY BEGINNING TO MOVE FORWARD.

    ANNB

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