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MEBO TMAU TESTING CURRENTLY SUSPENDED INDEFINITELY

MEBO - UBIOME study 2018

'PRESS RELEASE'

NCT03582826
ClinicalTrials.gov

MEBO Gut Microbiome Study
"Microbial Basis of Systemic Malodor and PATM Conditions (PATM)"
Funded by uBiome Research Grant

"Microbial Basis of Systemic Malodor and PATM Conditions (PATM)"

Dynamics of the Gut Microbiota in
Idiopathic Malodor Production
& PATM

Started May 2018 - Ongoing

Current people sent kits : 100/100
3 kits per person

NO LONGER RECRUITING

Participation info : LINK English

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Full details : https://goo.gl/TMw8xu
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TMAU UK end total:262
TMAU UK ends 23/01/20
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TMAU (Dominican)
Metabolomic Profiling Study
NCT02683876

Start : Aug 2016
Stage 1 : 27 Canadian volunteers to test
Latest click here (26 oct) :
17 samples returned


Note : Stage 1 is Canada only.
Return cut-off date : passed
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Analysis start in/before Nov
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London TMAU meeting with Prof Liz Shephard
19th Oct 11am - 1pm
St Mary's Hospital
Praed St, Paddington
London W2 1NY
click to read more
more details : karen.james@meboresearch.org

MEBO Research Clinical Trials

Click here to read details of the MEBO Clinical Trials
NCT03582826 - Ongoing not recruiting
Microbial Basis of Systemic Malodor and PATM Conditions (PATM)
United States 2018 - ongoing

NCT02683876 - Completed
Exploratory Study of Relationships Between Malodor and Urine Metabolomics
Canada and United States 2016 - ongoing

NCT03451994 - Completed
Exploratory Study of Volatile Organic Compounds in Alveolar Breath
United Kingdom and United States 2013 - ongoing

NCT02692495 - Completed
Evaluation of Potential Screening Tools for Metabolic Body Odor and Halitosis
United Kingdom 2009 - 2012

Saturday, September 4, 2010

New HBRI FMO research paper

Dr John Cashman of the Human Biomolecular Research Institute in San Diego is probably the most prolific researcher (of the few researching) of the FMO group of enzymes. This month he has published another research paper. It looks as if it is to do with FMO enzyme sources for research labs, so likely has no direct connection with TMAU other than it may make research on the FMO enzymes easier in the future.

Oligomerization and kinetic characterization of human FMO3 and FMO5 expressed as maltose binding protein fusions.
Reddy RR, Ralph EC, Motika MS, Zhang J, Cashman JR.

1 Human Biomolecular Research Institute;
Abstract
The flavin-containing monooxygenase (FMO) family of enzymes oxygenates nucleophilic xenobiotics and endogenous substances. Human FMO3 and FMO5 are the predominant FMO forms in adult liver. These enzymes are naturally membrane-bound, and recombinant proteins are commercially available as microsomal preparations from insect cells (i.e., Supersome FMO). Alternatively, FMO3 has previously been expressed as a soluble protein, through use of an N-terminal maltose binding protein (MBP) fusion. In the current study, MBP fusions of both human FMO3 and FMO5 were prepared to >90% purity in the presence of detergent, characterized for biochemical and kinetic parameters, and the parameters were compared to those of Supersome FMO samples. Although MBP-FMO enzymes afforded lower rates of turnover compared with the corresponding Supersome FMOs, both types of FMO showed identical substrate dependencies and similar responses to changes in assay conditions. Interestingly, the FMO3 enzymes showed a 2-fold activation of k(cat)/K(m) n the presence of Triton X-100. Oligomeric analysis of MBP-FMO3 also showed disassociation from a high-order oligomeric form to a monomeric status in the presence of Triton X-100. This report serves as the first direct comparison between Supersome FMOs and the corresponding MBP-fusions, and the first report of a detergent-based activation of k(cat)/K(m) that corresponds to changes in oligomerization.
The full paper can be read for free here:
http://dmd.aspetjournals.org/content/34/1/19.long

One interesting note was that FMO5 seems to be quite abundant in the small intestine. It does not seem to be known what role FMO5 plays, although often people with TMAU feel they have mild 'gut issues'. Perhaps FMO5 plays a detoxifying role in the gut, without which the ecology tends to get unfavorably 'out of control'

Update : It now seems it is unlikely FMO5 has an important role in humans. It seems to be very 'substrate specific' and deals with very few substrates, and although the RNA may be found in adult human cells, this does not mean it turns into FMO5 protein.

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