The Fiber Disease

Human Anatomy, Physiology, and Medicine. Anything human!

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Post by southcity » Sun Dec 10, 2006 2:18 am

Another link to scroll on through. too much info to go through myself, but sky and london, Nadas, Tam, well, have a look. its an excel file and will take a few moments to download.

South ... y01-04.xls

"First they ignore you...
Then they laugh at you...
Then they fight you...
Then you win." - Mahatma Gandhi

King Cobra
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Post by London » Sun Dec 10, 2006 3:04 am

In the SQUID the current circulates around a ring-shaped circuit made from microscopic aluminum wire. There are two breaks in the loop, each bridged by wires just 60 nanometres wide and made from the semiconductor indium arsenide.(TOLD YA!)

At very low temperatures the aluminum becomes superconducting and the current is carried by pairs of electrons with zero electrical resistance.

The team (PARDON ME??? IS THIS A GD GAME NOW, TEAM????) used electric fields to turn the semiconductor nanowires into "quantum dots" -- isolated islands of electrical charge. Electron pairs can jump to and from the islands, so the supercurrent becomes chopped into discrete parcels of two electrons

Nadas Moksha
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Post by Nadas Moksha » Sun Dec 10, 2006 3:16 am

Development of DNA-mediated transfection in Entamoeba histolytica will facilitate basic research toward the control of this protozoan parasite. A transient transfection system was established by using the firefly luciferase gene ligated to the 5' and 3' flanking regions of the amebic hgl1 gene. The optimal construct tested encoded an hgl1-luciferase fusion protein and contained 1 kb of 5' flanking sequence with 16 bases of coding sequence from the hgl1 gene ligated in-frame to the luciferase start codon and 2.3 kb of 3' flanking sequence from hgl1 ligated 3' to the luciferase stop codon. Optimal electroporation conditions in strain HM-1:IMSS trophozoites when using this construct were 500 $\mu F$ and 500 V/cm, which resulted in luciferase activity up to 5000-fold above back-ground 9-12 hr after electroporation. Constructs that contained the luciferase gene without amebic flanking sequences or that contained a simian virus 40 promoter, enhancer, and polyadenylylation signal produced only background levels of luciferase activity. The ability to introduce and express genes in amebae will now permit a genetic analysis of the virulence of this organism, which remains a serious threat to world health.

Since sialylation and de-sialylation are vital events in cell survival, the identification of the time signals involved in the regulation of sialylation could be useful in a strategy for drug design.

The present work has shown that sialidase represents an important factor in the pathogenesis of amebiasis and could be an essential target in drug design against the disease amebiasis. We are currently working on the production of monoclonal antibodies against E. histolytica sialidase.

Barnett JEG, Coring DL, Rasool G (1971) Studies on N-acetyl neuraminic acid aldolase. Biochem J 125:275-284

Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254

Chayen A, Avron B, Nuchamowitz Y, Mirelman D (1988) Appearance of sialoglycoproteins in encysting cells of E. histolytica. Infect Immun 56:673-681

Diamond LS (1968) Techniques of axenic cultivation of E. histolytica schaudin 1903 and E. histolytica-like amoeba. J Parasitol 54:1047-1056

Engstler M, Reuter G, Schauer R (1992) Purification and characterization of a novel sialidase found in procyclic forms of T. brucei. Mol Biochem Parasitol 54:21-30

Engstler M, Reuter G, Schauer R (1993) The developmentally regulated trans-sialidase from T. brucei sialylates PARP. Mol Biochem Parasitol 61:1-14

Feingold C, Mirelman D, Lotan D, Lotan R (1984) Enhancement by retinoic acid of sensitivity of different cell lines to the sialic acid-specific toxin of E. histolytica. Cancer Lett 24:263-271

Feingold C, Bracha R, Wexler A, Mirelman D (1985) Isolation purification and partial characterization of an enterotoxin from extracts of E. histolytica. Infect Immun 48:211-218

Ifyeanyi AU, Leicht JG (1987) A membrane associated neuraminidase in Entamoaeba histolytica trophozoites. Infect Immun 55:181-186

Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685

Leicht GJ, Dickey AD, Udezulu IA, Bailey GB(1985) E. histolytica trophozoites in the lumen and mucus blanket of rat colon studied in vivo. Infect Immun 47:68-73

Muchmore EA, Varki N, Fukuda M, Varki A (1987) Developmental regulation of sialic acid modifications in rat and human colon. FASEB J 1:229-235

Nok AJ, Uemura H (1998) The Trypanosoma brucei rhodesiense trans-sialidase. Parasitol Int 88:56

Pereira MEA (1983) A developmentally regulated neuraminidase activity in T. cruzi. Science 219:1444-1446

Perkin MA, Rocco LJ (1988) Sialic acid dependent binding of P. falciparum merozoite surface antigen pf 200 to human erythrocytes. J Immunol 141:3190-3196

Ravdin JI (1995) Amebiasis. Clin Infect Dis 20:1453-1466

Roggentin P, Rothe B, Lottspeich F, Schauer R (1988) Cloning and sequencing of a Clostridium perfringes sialidase gene. FEBS Lett 238:31-34

Roggentin T, Kleinadam RG, Schauer R, Roggentin P (1994) Effect of site specific mutation on the enzymatic properties of a sialidase from C. perfringes. Glycoconj J 9:234-240

Schenkman S, Jiang MS, Hart GW, Nussensweig V (1991) A novel cell surface trans-sialidase of T. cruzi generates a stage-specific epitope required for invasion of mammalian cells. Cell 65:1117-1125

Silvia ZM, Julio CV, Carlos CM, Arturo FC, Everardo LR (1999) Entamoaeba histolytica: identification and properties of membrane-bound and soluble α-glucosidases. Exp Parasitol 93:109-115

Stanley SL, Tian K, Koester JP, Li E (1995) The serine-rich Entamoeba histolytica protein is a phosphorylated membrane protein containing O-linked terminal N-acetylglucosamine residues. J Biol Chem 270:4121-4126 http://www.geocities/bacciger

Zoology General WEB

Parasites of jellyfish: On construction

http://parasitology.informatik.uni-wuer ... .html.html

Substrate specificity using sialoglycoconjugates revealed strict preference for terminally α-linked sialic acids. Table 3 summarizes the results on substrate specificity analysis. Substrates possessing an α,2,3-linked sialic acid, like Neu5Acα2,3lac, fetuine and bovine mucin, were readily hydrolyzed. The gangliosides GD1 and GM1, having internal sialic acid residues, were unaffected by the enzyme. Also, colomic acid (a homopolymer of α-2,8-linked sialic acid) and Neu5Acα2,6lac were not suitable substrates. Detailed kinetic analysis from initial velocity data revealed Km and Vmax values of 0.059 mM and 769 µM/min, respectively, for Mu-Neu5Ac. The Km and Vmax values for Neu5Ac2, 3lac were 0.144 mM and 2275 µM/min.

Table 3. Substrate specificity of the hydrolysis of glycoconjugate by E. histolytica sialidase. The substrates were adjusted as described in Materials and methods, to contain 1 mM of bound sialic acid in 50 mM acetate buffer, pH 5.5. In the assay using GM1 and GD1, the buffer contained 0.1% Trixton-100. The results are averages of three readings
Substrate Product (Neu5Ac; µU/mg)
MU-α-Neu5Ac 685±25
Neu5Ac2,3-α-lactose 582±30
Neu5Ac2,6-α-lactose 68±15
Colomic acid 30±18
Fetuin 445±35
Mucin 377±35
Ganglioside GM1 30±12
Ganglioside GD1 25±10

The enzyme was also strongly inhibited by Neu5Ac, 2en and weakly by pNPO. Evaluation of the inhibition against Mu-Neu5Ac as substrate revealed competitive patterns (Fig. 3) for both Neu5Ac2en and pNP-oxamic acid with Ki values of 30 µM and 185 µM, respectively. The physiological index of efficiency (Vmax/Km) of the enzyme decreased from 12.94/min to 2.93/min and 4.28/min for Neu5Ac2en and pNPO, respectively, when Mu-Neu5Ac was used as substrate.


Fig. 3. Hanes Wolf plots of initial velocity data of the inhibition of E. histolytica SD-catalyzed hydrolysis of methylumbelliferyl-Neu5Ac (4-MU-Neu5Ac) in the presence of 0.05 mM Neu5Ac2en and 0.2 mM para-nitro-phenyloxamic acid (pNPO). Results are averages of three experiments

Figure 4shows the effect of fetuin on the motility of E. histolytica. At 0.05-0.5 mM fetuin, there was a proportionate increase in the motility of the parasite. In the presence of the sialidase inhibitor Neu5Ac2en, the motility sharply regressed to the non-induced state. Similarly, at 0.05-0.5 mM Neu5Ac2,3lac, there was a sharp increase in the motility of the parasite (Fig. 5). The sialidase inhibitor Neu5Ac2en also inhibited motility when included in the motility-assay cocktail.


Fig. 4. Motility of E. histolytica trophozoites in the presence of different levels of fetuin (FT), the SD inhibitor Neu5Ac2en and a combination of FT and Neu5Ac2en. Results are averages of three experiments


Fig. 5. Motility of E. histolytica trophozoites in the presence of different levels of Neu5Ac2,3lac (SL) the SD inhibitor Neu5Ac2en and a combination of SL and Neu5Ac2en. Results are averages of three experiments

In order to assess the precise role played by the parasite's sialidase, the fluoregenic substrate 4-MU-Neu5Ac was incubated with the trophozoites. A pattern of motility similar to those of Neu5Ac2,3lac and fetuin was observed. This was accompanied by a progressive increase in the level of MU (Fig. 6). A similar increase in the released neuraminic acid (Neu5Ac) was also observed until 15 min. Subsequently, the level started to decrease and this coincided with the emergence of the activity of the enzyme PSL.


Fig. 6. The activity profiles of SD, pyruvate sialate lyase (PSL) and neuraminic acid (NA) of E. histolytica trophozoites incubated in the presence of 4-Mu-Neu5Ac. Results are averages of three experiments. umole Micromoles

In this report, a detailed study was conducted on sialidase from Entamoeba histolytica trophozoites. The purified enzyme is a 65-kDa monomer. like Trypanosoma brucei brucei sialidase (Engstler et al. 1992). Bacterial sialidases have molecular weights of 60-150 kDa (Roggentin et al. 1988). The enzyme has a temperature optimum of 37 °C and a pH optimum of 5.5. It was unstable and lost about 50% activity at 4 °C and was reactivated by re-incubation with dithiothreitol, a reagent that protects SH groups of the enzyme from oxidation. This observation suggests the existence of oxidizable SH residues that cause its reversible inactivation.

The kinetic properties of the enzyme resemble that of other protozoa, like T. brucei and T. cruzi (Schenkman et al. 1991; Engstler et al. 1992; Nok and Uemura 1998), in sensitivity to only α-2,3 linked sialic acids. In contrast however, the enzyme was strongly inhibited by Neu5Ac2en and weakly by pNPO. The increased motility of the parasite in the presence of Neu5Ac2,3-lac and fetuin suggests the involvement of sialidase in the parasite's motility and pathogenesis. The suppression of motility when the sialidase inhibitor Neu5Ac2en was part of the cocktail is further evidence on the role of sialidase in the pathogenicity of the parasite.

Sialoglycoproteins (SGs) have been shown to be important in the enhancement of sensitivity to sialic acid-specific toxin from E. histolytica (Feingold et al. 1984). This toxin is known to induce fluid secretion in ligated intestinal loops of indomethacin-pretreated rats. Since SGs serve as receptors for the E. histolytica toxin, the pathogenesis of amebiasis could be preceded by an initial unmasking event of surface sialic acid by the parasite's sialidase, followed by attachment of the toxin. Feingold et al. (1985) reported the isolation of two cytotoxic factors from E. histolytica trophozoites, one of which is sensitive to sialic acid levels above 5 mg/ml. Our observation could imply that, when such a threshold level of free liberated by sialidase is attained, it triggers the expression of PSL to hydrolyse the sialic acid to pyruvate and N-acetyl mannosamine. This biochemical event may promote the interaction of cytopathic factors with the receptor. Moreover, when Neu5Ac2,3-lac was incubated with intact cells, the level of released freeNeu5Ac decreased with incubation time, coinciding with the appearance of PSL, showing that the Neu5Ac is catabolized. These events could represent signals involved at regulating the level of sialic acid, to avoid the inhibition of the interaction of the cytopathic factors with the receptor.

Both sialyltransferase and trans-sialidase were absent from E. histolytica trophozoites. Moreover, the trophozoites were found not to contain any detectable levels of sialic acid. The lack of sialic acid is consistent with the absence of sialyltransferase and trans-sialidase. Previously, Chayen et al. (1988) reported the presence of sialic acid in cyst forms of E. histolytica. It appears that the uptake of sialic acid in E. histolytica is developmentally regulated, as it also is in the African trypanosome (Engstler et al. 1993). This unique feature could represent an evolutionary linkage between the amitochondrial protist and African trypanosomes. Since sialylation and de-sialylation are vital events in cell survival, the identification of the time signals involved in the regulation of sialylation could be useful in a strategy for drug design.

The present work has shown that sialidase represents an important factor in the pathogenesis of amebiasis and could be an essential target in drug design against the disease amebiasis. We are currently working on the production of monoclonal antibodies against E. histolytica sialidas. ... cember.pdf

Nadas Moksha
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Post by Nadas Moksha » Sun Dec 10, 2006 3:18 am

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King Cobra
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Post by RANDY » Sun Dec 10, 2006 3:47 am


Please explain in laymans terms EXACTLY what this article is talking about and how it directly links to our disease.

If you can not I will believe that you just post and post without any knowledge of what you are posting.

So go ahead, break it down for me in the simplist of terms for everyone here watching this site and then explain how it relates to this disease and what research you are going to do to prove your theory.

This site has become a place where people post and have NO IDEA what they are posting and then the others are conspiracy theorists and nothing more.

Manic postings that is all they are.

In facy I challenge everyone here with these long posts to pick just ONE of them and tell me how you are backing up your reason for posting and how it relates and what you are going tod tto prove how it relates.

The people I have watching this site can't wait to see this one! Simple logical and precise.

Any of the 454 posts will do since none of them compare to the other and they are all over the board with no common thread or plan to prove.

Many people are watching and asking me to ask this question. Pick one post and break it down and show how ti relates to this disease.

Who will be first?
During the End Times, Good will battle Evil. Where do you stand?

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Post by Deena » Sun Dec 10, 2006 4:23 am

Oh, pick me, pick me!!

Well, dah!! I'm kinda thinkin' here that our wonderful world, once upon a time, maybe is no longer. In fact, it is anything but. What does this have to do with it? Everybody's research is proving time and time again, just who we can and cannot trust. It is backing up anybody's doubt as to who has done this or is at least, responsible. Cause who'd ever think it to be true?? We certainly don't want to believe it but hey!! Here you have it. Post after post.
Alright, I pick Nadas last post...How the hell are we supposed to rid ourselves of this whatever fiber...microorganism thing if it's impossible to get our immune systems where they belong. Yeah, I suppose food plays a big part in it, ya think??? Shoot, we are probably feeding the little bastards what they want us to. But we or anyone else for that matter would never know it. Now why do you suppose that is??!!! Cuz it's just one more thing kept a big fat friggin secret from WE THE PEOPLE! This sorry ass medical association is a joke. They make us ill any way they can so they make their $$. The circle of $Life$

Now what do I win, dammit!?


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Post by Maggie Mae » Sun Dec 10, 2006 4:41 am

Deena, you got kahonas bout' a big fat...cigar....naw, how bout' a big fat doob..???? Due to work restrictions I am forced to smoke Valerian...

I have been subscribing to this site for quite a while now...good database...and images..!!! Pick one, any one...

Someone is going to leak classified documents Randy, and I know this will happen, soon. I have prayed ernestly and the Lord just about always gives me what I ask, and in this case, just to PROVE my point, because honestly, I believe you already know.
Conspiracy REALIST.
Link: ... index.html

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Post by Deena » Sun Dec 10, 2006 5:16 am

Maggie Mae~ :arrow: :mrgreen:

And here I forgot the obvious...If chemtrails are getting us, can you imagine what it's doing to all the crops? Shoot, then they get watered, and layered and dusted and watered and layered....and WE THE PEOPLE. No wonder we can't get a leg up on this.

Randy~Stupid question and now I don't feel like the low man on the totum pole anymore. Thank you.

I really don't want to be a farmer and I certainly don't want my own cow but it does appear to be a little more promising. Just a little, tho.
Don't have to worry about public much to think about!

King Cobra
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Post by London » Sun Dec 10, 2006 5:49 am

sweet lil MM- I liked your link....I spotted those bacteriapahges right off the bat. Looks like there we have our synthetic spider. I think we do have the spider silk in us too.

Hey, well, I think this will kind of back up your link there:

Digital Organisms (duh, the kind they make on a computer)

Programs designed to "evolve" solutions to mathematical problems support the idea that complexity in nature emerges in small, often apparently unremarkable, steps.

Complex biological organisms have long been thought to develop through a series of intermediary evolutionary adaptations, rather than in single giant evolutionary leaps.

Seeing every step along the way in an evolutionary sequence that unfolds over millions of years is of course impossible. But researchers at Michigan State University and the California Institute of Technology in the US have found a way to see this process unfold in its entirety without any 'missing links'.

"Our work allowed us to see how the most complex functions are built up from simpler and simpler functions," says Richard Lenski, a biologist at Michigan State University.

Charles Ofria, a computer scientist at Michigan State University, who was involved with the research, says it may help computer programmers make more efficient evolutionary algorithms.

"One of the beautiful aspects of this work is that it allows us to better understand how nature overcomes difficulties inherent in solving complex problems," he says. "We can then apply these concepts when trying to decide how best to solve computational problems we are faced with."

Simple origins
The researchers created populations of identical "digital organisms", using a computer modeling application called Avida. At the start, each digital organism was incapable of solving logical problems. But with each replication, there was a 20 per cent chance of a random mutation in "offspring". This mutation altered the nature of the digital organism and in some cases resulted in one that could perform a logical operation.

During 15,000 generations or so, the researchers found it was impossible for a population of digital organisms to solve the most difficult logic problems, if that was all that the computer rewarded.

Electronic evolution
But the outcome changed dramatically if the digital organisms lived in environments that would also reward them if they performed some simpler functions. In that case, the evolving programs were able to bridge the gap and eventually solve even the most complex logic problems.

Evidence of a gradual biological evolutionary process is found in complex structures that retain features related to earlier evolutionary steps. The human eye, for example, contains crystalline proteins that are related to those that perform enzymatic functions unrelated to vision.

The researchers say their computer model will let biologists study individual evolutionary steps for the first time. "Darwinian evolution affects DNA and computer code in much the same way," says Christoph Adami, who leads the Digital Life Laboratory at the California Institute of Technology. "This allows us to study evolution in this electronic medium."

Lenski adds that some mutations, which initially looked as if they would not be advantageous to an organism, turned out to be crucial stepping stones in the long run.

Now what I wanna know is why......

what is the purpose of microwaving us with radiation (huh Keely girl?)
when they know good and well wtf it does to us?

It's not nice to fool Mother nature.....and you know what my 2001, five year old genoming book says? Even back then they were working on extending life but Hey, I' m not talking for 20+ years here.....I'm talking about forever.....hell, I do not think I even would want to do that.

Do you guys? The book also discusses the dust>the radipactive dust!

and also how they can reverse enginere the brain and the audiopath which I believe is what they are doing to us.

I like your positive talk MM, I did!

Death Adder
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Post by msc » Sun Dec 10, 2006 5:57 am

from msc

everyone start reseachings gelatin microbeads, MACS MICROBEADS,
look up webstites where prof kligman used macs microbeads. they used
magnetics used in this and shows exactly what my friend sees the balls with the white worms shooting out of them. look up japanese companies
and their work with kligman, turnkey engineering corp and other corps
there was a website that shows how they are made very lengthly. the pdr book shows edgma causes abberations of chromosones edgma are microbeads and used in polymerization and used in renova and we can't imagine how many other products that we all use, try shampoos, conditioners look at everything you use body washes, medications look up patents they have more chemicals in them apparently then what the labels state on products. i have to go have work early. God Bless you.

King Cobra
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Post by London » Sun Dec 10, 2006 6:08 am

Skytroll, this is a very short film for you on biofilms and last about 45 seconds max. ... ob2_h.html

MSC, thanks, I will. Hey, tonight I read about the deformed frogs from the retoinic acid.....

Death Adder
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Post by msc » Sun Dec 10, 2006 6:25 am

from msc

one thing more and very very important, we all have to find a product we all used with these types of chemicals in them. print out patent 4877805
on page 7 and 8 list the chemicals used besides lecithin, kobo pigments
and chemicals that are the on the retinoid makeup composition. you need to find out if any medication you used had these retinoids in them
or soy lecithins that cause biofilms anything that had lipids, hydrophilics and lipophilicis, hydrophobics anything that had biological on it. the words EDGMA and HDPE, silicone silica fiber optics. we need to find a common
product or person you came in contact with that used them. everything is about polymerization that is were fibers, threads, ligands plastics all come from being polymerized and look to see if your products use the words nano particles. your patents are the best place to find the words nano and lipids etc. we know it is nano, with know it is plastic silica silicone, was it in medicine we all used, are optic fiber lights a danger to our health things like that we need to find in common. we have to start listing those things we have used and tie it together with the nano research we used. thanks let do this before the holidays get here. lets make it the holiday nobody will forget including those who did this and may they be behind bars before the holdiays get here. that is my goal
they took enough Christmas's from my children they will not take anymore.


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