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Amarantus Bioscience Holdings, Inc Message Board

  • laujhawj laujhawj Jan 1, 2013 7:23 PM Flag

    Similarities & Differences Between MANF & CDNF: & Why MANF if Better, if Current Literature Is True


    Amino acids: MANF is 158; CDNF is 187 (these are the minimal; there's a range for both, in other contexts).


    MANF and CDNF have about 60% of their amino acids on commonality. Both are very conserved neurotrophic factor molecules: meaning they exist in many animals, from humans, to mouse, to cattle, to flies, etc).

    MANF is, in fact, more conserved than CDNF because studies have shown that in the beloved fly, Mr. Drasophilia Melanogaster, there's single protein that has higher protein sequence to human MANF than it does w/ human CDNF.

    NOTE: for those who don't think this conservative & high interchangeability of amino acid/protein among species --- is important or relevant --- think back to the discovery, harvest, and application of the class of INSULIN molecules, for diabetics... from the 1920s (when Banting of Canada first isolated it) all the way to the 1970s and 80s, when modern Recombinant DNA allow bacteria to do it: researchers harvested & purified INSULIN molecules straight from DOGS, PIGS, CATTLE, etc. They --- this class of hormonal molecules called "insulin" from the pancreas of the said animals --- ARE "genetically" close enough to ours, to be used IN US without problems!

    It was just not very efficient to slaughter tens of thousands of dogs, pigs, and pigs to harvest and purify this very small and scarce hormonal molecule; thus, using modern Recombinant DNA techniques, as Boyer and Cohen did, during the 1970s and 80s allowed BACTERIA --- in the trillions --- to produce larger quantities of insulin, for global use.

    Anyway, (mature) human MANF is estimated to have 99%, 98%, and 96% amino acid similarity to mature rat, mouse, and cattle.... in addition IT to having much higher similarity to those in fruit flies than CDNF... Again, point here is, MANF is likely more conserved than CDNF...


    MANF is "localized" at the ENDOPLASMIC RETICULUM. I have read a bit, trying to nail down the "localized" parameter of CDNF, but I've not found it yet; so if you have nailed it down, share it with us here.

    This "localized" parameter is important and SUBTLE and confusing at the same time. Without a lot of argument, I will simply ASSERT, using logic, that PERHAPS this is why in the UNIVERSITY OF HELSINKI study as well as in following and other independent studies the authors reported that, in MOUSE MODELS on Parkinson, MANF upregulates during Endoplasmic Reticulum stress (induced on purposed, to see what each molecule could or would do, or not)....

    NOTE: --- this "localized" parameter I am talking about here is NOT what chromosome, or in what base pair in that chromosome each of these two molecules, MANF and CDNF, are... I know that: MANF, for example, is located on chromosome #3, between base pairs of 51,422,478 and 51,426,478.... and CDNF is located on chromosome #10, between base pairs of 14,861,249 and 14,880,574.

    Again, since ALL CELLS in our body that have a nucleus --- where the DNA is stored --- have ALL the genetic information to make us, the organism (even if, through evolution, only embryo cells easily make whole organisms and not adult/somatic cells, even though both somatic/adult cells and embryonic cells have the SAME genetic information)... so this "localization" issue has to do with SPECIALIZATION TASK DICTATION on the DNA's part.

    In other words, while the DNA in the nucleus of ALL CELLS carry our genetic information, only some information is invoked, during a certain condition, and the TASK is dictated to ONE PARTICULAR CELL TYPES or another --- specialized cell types --- to carry out the SYNTHESIS of those needed enzymes or proteins NEEDED .... to do the important tasks at hand...

    Or, it is truer in REVERSE:

    For example, when --- for different reasons, from genetic mutation to severe disease infection --- our body is UNABLE or "unwilling" to produce the necessary enzymes or proteins, whether to fight genetic or infectious cancer cells... we have "problems"... And the "problems" are multi-faceted: sometimes because too many of our healthy cells die, too fast, NATURALLY, due to aging... with little or no replacement cells ...OR, other times..... because the genetic or infectious diseases are too aggressive, and they kill off too much of our healthy cells, again, with little or no good cells to replace those having been "killed"... and, more often than not, a combination of the two...

    IN ANY CASE, all this ranting boils down to this (because I want it)!

    If .......... both CDNF and MANF are more potent or have differential & over lapping protective properties than, say, GDNF....

    ...... and if .... CDNF and MANF are grouped together more closely than GDNF but some how CDNF and GDNF work more similarly in terms of mechanisms...

    .... but if .... MANF works differently and IS LOCALIZED in the ENDOPLASMIC RETICULUM... where the Ribosomes synthesize all enzymes and proteins and where LYSOSOMES (tiny cleaning enzymes WHOSE LACKING or deficiency is the BASIS of most of the known GENETIC diseases we have) are synthesized and packaged....

    .... THEN ........ it is logical --- as I asserted at the outset --- to assume WHY.... of all the studies, so far .... only MANF (and not CDNF).... is shown to be secreted, to start doing its job, when ENDOPLASMIC RETICULUM STRESS is induced in animal with Parkinson Disease... The ER (inside all cells that have nucleus), remember.... is where proteins of all kinds needed by the body different organs are synthesized..... BY RIBOSOMES... so any thing that hinders or clogs up the ENDOPLASMIC RETICULUM... that creates a "traffic jam" --- can and will cause diseases... if nothing is done about it, that is...

    AND, AGAIN.... which molecule --- MANF or CDNF --- responses to Endoplasmic Reticulum "traffic jam" problems? MANF and only MANF....

    CDNF may be wonderful in other protective spheres, or parametes... but if CDNF doesn't respond to ER stress... then it's not that good in dealing with "traffic jam" --- protein misfolding and related problems --- inside the cells, is it?

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