It looks like you're using an Ad Blocker.

Please white-list or disable AboveTopSecret.com in your ad-blocking tool.

Thank you.

 

Some features of ATS will be disabled while you continue to use an ad-blocker.

 

NEWS: "Mad Cow-like" Prions Possible in Sheep Milk?

page: 2
7
<< 1    3 >>

log in

join
share:

posted on Dec, 3 2005 @ 11:19 AM
link   

Originally posted by mattison0922

Originally posted by soficrow
mattison - nucleation aside, I think the evidence does show a strong link between prions and cancer. The association seems to be related to prions infecting stem cells, and as well, to prions' ability to hitchhike on viruses (as well as other microbes). A key virus in this process would be the Rous virus - but I believe there are more. So we're seeing what amounts to a multi-dimensional bouncing - not just between species, but cross-kingdom too - and responsive to every kind of environmental contamination... Talk about complex adaprive systems interracting - needless to say the pathways and results are ...complicated.

Sofi... would be interested to examine said evidence sometime. Please forward some refs. when the opportunity presents itself. When you state there is a strong link between please prions and cancer it pretty much just leaves me wanting.



I know - sorry. Can't get to it right now, but did not want to let it pass either. I promise the refs will come.






Can you perhaps be more descriptive: ie: is there evidence to suggest that prions actually induce genetic changes at relevant loci?



Yes. Also, epigenetics requires rethinking the concept of "genetic inheritance."




I am completely unfamiliar with Rous virus, and probably am not going to search it at this hour.... Perhaps tomorrow.



A cancer virus - discovered in 1920's - confirmed later. Now receiving new attention.




Ultimately, proteins are produced by the genes that encode them. ...I can certainly see the relation between epigenetics, and proteins, but the link you are making between these and prions escapes me. Can you perhaps elaborate?


Prions may be far more important than genes in influencing protein production. That's the heresy.


Again - more later.





Certainly the protein atlas is a great project, right up in my links with the PDB database. But again the relevance between this database and the topic of this thread escapes me.


EVOLUTION can occur in a way never previously shown. Geneticists have discovered that the strange proteins called prions can temporarily give yeast cells new powers which can then be quickly, and permanently, assimilated into their chromosomes.



...As you are well aware, epigenetic changes can have huge phenotypic effects without altering the actual genetic information. Awesome stuff.




IMO - the evidence shows that prions' impacts go beyond epigenetic and also cause (or contribute to causing) permanent genetic mutations - hence the evolutionary crisis.


.phrase

[edit on 3-12-2005 by soficrow]




posted on Dec, 3 2005 @ 11:25 AM
link   
Authorities currently recognize about six prion diseases, all of which infect brain tissue and cause brain diseases like Mad Cow (BSE), variant CJD, and fatal familial insomnia. No other prion strains or prion-related diseases are acknowledged officially as related to prions. This official position reflects a policy of denial: a conspiracy of silence.

According to the official spin, Mad Cow and other prion diseases are caused mainly by eating infected brain tissue - and have no effect whatsoever on any part of the body except the brain. Bull puckey. The official spin is about population control, and protecting industry profits - not scientific rigor. If the range of prion strains and prion-related diseases is not acknowledged, then their control will not be regulated, and industry profits are preserved.

It doesn't take a brain surgeon to see that if Mad Cow prions take decades to get from the gut to the brain, they're gonna make a few stops along the way. Fact is, on their way to the brain prions bump into new cells, experience environmental change - and respond by creating new strains.

Different prion strains infect different cells - and cause different diseases and symptoms.

* "...the biochemical isoform of PrP(Sc) found is influenced by the cell type in which it accumulates" - and it does accumulate in peripheral tissues.

* "Diverse human disorders, …arise from misfolding and aggregation of an underlying protein."

* "Prions, once dismissed as an impossibility, have now gained wide recognition as extraordinary agents that cause a number of infectious, genetic and spontaneous disorders"

* "…this hypothesis would shed some light on other diseases not presently classified as prion diseases and in the process of ageing."

* Also see: Games played by rogue proteins in prion disorders and Alzheimer's disease.

Officially recognized infectious prion strains are found in the brain, spinal cord, immune system, nervous systems, muscle, and various organs and glands including the spleen, liver, pancreas, and kidneys. Contrary to popular medical myth, their presence in these diverse locations does have an effect on health and well-being.


The existence of so many different prion strains blocked general acceptance of the prion hypothesis for a time. Old-school scientists argued that because proteins don't have genetic material, prions can't evolve and create new strains. The mystery of prion strains was solved when researchers proved that prions create new strains by shape-shifting - they literally just fold into a slightly different shape to create a new strain - and cause a new disease or modify an existing one.

In fact, even a change in temperature can cause an existent prion to shape-shift, misfold in a different way, create a new infectious prion strain - and cause a different disease.


"Prion shape affects nature of infection"

“UCSF scientists have demonstrated for the first time that a change in the folded shape of a prion protein changes its infectious properties – including the prion’s ability to jump 'species barriers.' The research, based on studies of prion infectivity in yeast, solves one of the great puzzles about prions: If they are infectious proteins with no genetic material of their own and no ability to mutate genetically, how can a single prion exist in different strains that can cause different diseases?

…Studies of the melting temperatures of the prions and their resistance to breakdown by enzymes indicated that the conditions generated prions with different physical properties.

...shape change accounts for strain differences, and it lays the groundwork for research to determine the physical differences that allow a prion to change shape and cause different diseases. ...The studies show that a single infectious protein can adopt different, distinct, self-propagating shapes and that these conformational differences underlie the differences in prion strains

***

The same protein can misfold in various ways to create new prion strains.

......Scientists have grappled for years with one of the central tenets of the protein-only hypothesis, namely, that a single prion protein, when unaltered by genetic mutation, can give rise to different strains of prions with varying infectivity and other properties. The two research groups established that the strains could be accounted for by different misfolded conformations of the same protein. ...In test tube experiments, the researchers demonstrated that the protein conformations produced at different temperatures propagated themselves as distinct strains - providing templates for the folding of other proteins into the same shapes. Further structural analyses of two of the strains confirmed that the proteins were, indeed, folded differently. ...what we are learning about how to make proteins misfold into different conformations will be directly relevant to understanding mammalian prions, and perhaps even to trying to understand the strain phenomenon in mammalian prions. This includes how strains can affect the virulence of a disease or how likely it is to jump a species.

***

Prion folding produces strains




Infectious prions enter the body in various ways, not just by eating contaminated food or drinking contaminated water. The way a disease enters the body is called the "vector," the route it uses to get in is called "transmission," and the place it enters the body is called the "point of entry." The places where] diseases exist in the world are called "reservoirs."

The article above talks about milk as a vector with transmission via the oral route, the stomache as the point of entry, and cattle as a reservoir.

As stated above, infectious prions are known to "cause a number of infectious, genetic and spontaneous disorders." This means that prions have a huge variety of vectors, reservoirs in the world, points of entry, and impacts on the human body. It is generally recognized now that "...prion (PrP) diseases, can spread not only through the food supply, but through organ transplants, contaminated medical instruments, the blood supply, or pharmaceuticals made from animal products (like vaccines)." However, the reality is even more threatening to the future of the human species.



Prion vectors, modes of transmission, points of entry, and reservoirs.

Milk, Meat, and Blood

2001 - "We found highest levels of mutant PrP in the brain and spinal cord, intermediate levels in skeletal muscle, heart, and testis and low levels in kidney, lung, spleen, intestine, and stomach. Up to 70% of the PG14 PrP expressed in peripheral tissues. ...Histological analysis of skeletal muscle, one of the peripheral tissues with the highest level of PG14 PrP, revealed features indicative of a progressive, primary myopathy, including central nuclei, necrotic and regenerating fibers, and variable fiber size. These results indicate that the PG14 mutation structurally alters the protein in a way that promotes conversion to a PrP(Sc)-like state, regardless of the tissue context, and suggest that accumulation of PrP(Sc) can have deleterious effects on skeletal muscle cells as well as on neurons.

2002 - "This finding indicates that previous attempts to quantify BSE and scrapie prions in milk or non-neural tissues, such as muscle, may have underestimated infectious titers by as much as a factor of 10,000, raising the possibility that prions could be present in these products in sufficient quantities to pose risk to humans..."

2002 - Prion transmission in blood and urine: what are the implications for recombinant and urinary-derived gonadotrophins?
(Gonadotrophins are hormones that stimulate the sex glands and control reproductive activity. Think prostate cancer and hormone replacement therapies - for starters.)

2003 - The spectrum of safety: "The culprit prion protein causes no immune response and contains no nucleic acid, making preclinical detection impossible. It is also very resistant to conventional forms of inactivation and decontamination. …there is concern that the prion agent may be transmissible in blood, and evidence from sheep models suggests that it can be."

Urine

A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. "We propose that the detection of UPrP(Sc) can be used to diagnose humans and animals incubating prion diseases, as well as to increase our understanding on the metabolism of PrP(Sc) in vivo."


Soil and Water

2003 - "How does chronic wasting disease (CWD) in deer and elk spread from animal to animal? … University of Wisconsin-Madison researchers show that prions - infectious proteins considered to be at the root of the disease - literally stick to some soil types, suggesting that the landscape may serve as an environmental reservoir for the disease."
Note: The prions get into the soil via urine.

"It is possible that infectious prions have leached into the water supply, government scientists admit. …The main risks to human health are contamination of water supplies from buried animals, or carcasses awaiting disposal, and pollution of the air from burning pyres."
Note: In addition, prions from urine also will leach from soil to contaminate groundwater, and like prions from other sources, go on to contaminate waterways and the oceans.

"Although composting reaches high enough temperatures for a long enough time to kill most pathogens ...it would be highly unlikely that composting would inactivate prions." Source: Composting Does Not Inactivate Prions

Insects

* "Fly larvae and mites were exposed to brain-infected material and were readily able to transmit scrapie (prions) to hamsters. New lines of evidence have confirmed that adult flies are also able to express prion proteins. Several cell types found on the human skin, including keratinocytes, fibroblasts and lymphocytes, are susceptible to the abnormal infective isoform of the prion protein, which transforms the skin to produce a potential target for prion infection."

* "Considering the huge amount of fly larvae that affects each animal, it is important to discuss the possibility that these ectoparasites could theoretically act as reservoirs and vectors for CWD and other prion diseases. It is critical to recognize all the possible factors involved in CWD transmission since ectoparasites could be handled in an easier way than the environmental persistence of infectious prions."

* Mites as vectors for scrapie.

* Characteristics of scrapie isolates derived from hay mites

* Also see: Winter survival of larvae and pupae of the blowfly, Lucilia sericata (Diptera: Calliphoridae). "...low temperatures did not appear to be the primary cause of high overwintering mortality in the field which, it is suggested, is more likely to be the result of the action of biotic mortality factors."


Microbes

* This 1986 paper describes how proteinaceous capsids - prions - use viruses as vehicles of transmission, and how the subsequent RNA interference silences genes.
* Viral influences on aflatoxin formation by Aspergillus flavus. Appl Microbiol Biotechnol 24:248-252. Schmidt FR, Lemke PA, Esser K (1986). Not available online.

* "Epidemiological observations indicate that a microbial vector is responsible for the transmission of natural prion disease in sheep and goats … A similar phenomenon was already described with a protein antigen of the ameba Naegleria gruberi. ...It is proposed that many microbial proteins may be capable of replicating themselves in mammalian cells eliciting and sustaining thereby degenerative and/or autoimmune reactions subsequent to infections with microorganisms.”

* PrPc (prion) expression influences the establishment of herpes simplex virus type 1 latency.

* "...lack of PrP(c) expression favors the establishment of HSV latency whereas HSV replication proceeds more efficiently in neuronal tissue that expresses (prion) protein. The data further suggest that PrP(c) may be involved in a metabolic pathway that culminates in apoptosis of neurons that have been infected by neurotropic viruses."


Genetic and Infectious

1993 - "Discovery of mutations in the PrP genes of humans with GSS and familial CJD established that prion diseases are both genetic and infectious."





In short, the world now is contaminated fairly completely with infectious prions - all of which may affect different cells, and cause different diseases. People can "catch" prion diseases from a variety of places, including from prions hitchhiking on a flu virus for example - and the prions may cause genetic mutations that are passed on to the victims' children.


.



posted on Dec, 4 2005 @ 12:26 PM
link   
As promised mattison.


Note: The premise here is that all disease-causing (pathogenic) misfolded proteins are infectious prions, not just the officially recognized misfolded PrP prion. For example:

The misfolded isoform of the protein called "a-smooth muscle actin" (ASMA) can be considered an infectious prion strain.

ASMA can infect connective tissue and smooth muscle stem cells anywhere in the body. ASMA underlies a huge number of acquired/infectious and genetic diseases including arthritis, asthma, COPD, heart disease, osteoporosis and atherosclerosis, Crohn's disease, high blood pressure, fibromuscular dysplasia (FMD) - and cancer.
Note: ASMA is the marker for myofibroblasts and FMD testing.

FMD is important to understanding ASMA-related disease - FMD appears to be a stage in the larger disease process where ASMA uses the vascular system to spread through the body. FMD was discovered/acknowledged officially in the USA in 1938 when a case was proved to have been transmitted congenitally. FMD commonly is categorized as a disease of the blood vessels but historically was recognized to be an angiopathy that involved the lymphatics and immune system.

In all ASMA-related diseases, this misfolded protein works the same way - by taking over partially differentiated stem cells for connective tissue and/or smooth muscle. The key connective tissue "stem cell" in ASMA-related diseases is the "fibroblast."

Stem cells are the "master cells" that differentiate to form all the different specialized cells in the body. Specialized cells are built from stem cells, and make up all of the body's various different tissues, organs, and body parts.

As a side note: "A stem cell is more than a committed progenitor; it also responds to influences from the extracellular environment," explains Ronald McKay, chief of the laboratory of molecular biology at the National Institute of Neurological Disorders and Stroke.

Fibroblasts[ /url] are precursor cells, or "stem cells" present in most if not all connective tissue. There are four kinds of connective tissue: blood, bone, cartilage, and connective tissue proper. Fibroblasts are more differentiated than stem cells, but still are able to differentiate further into various other more specialized connective tissue cells.

The disease process

ASMA takes over fibroblasts simply by coming into direct contact with other similarly shaped actin proteins in the stem cell. These proteins replicate into ASMA on contact - the stem cell is taken over as the replicas multiply or proliferate.

The taken-over or mutant stem cell becomes an abnormal myofibroblast. As more stem cells are taken over, abnormal myofibroblasts multiply in tissue, replace normal cells, and abnormal tissue is formed - this process of abnormal tissue formation now is called tissue remodeling or aberrant wound healing. Pathologists categorize the abnormal tissue as dysplasia, fibroplasia, or hyperplasia, as in FMD.

Sometimes, these "plasias" go on to become cancerous. The old mystery is "Why?" Why does some dysplasia and fibroplasia progress to hyperplasia, metaplasia and neoplasia - but not others? The answer is complicated - but generally speaking, what happens to abnormal myofibroblasts once they form depends on other factors, including where they go in the body and what they do - further mutation into cancer occurs only if certain other triggering factors are also present.

The point is - the disease process starts when ASMA prions take over fibroblasts, and turns them into aberrant myofibroblasts.


Stem cells', fibroblasts' and abnormal myofibroblasts' role in the development of cancer was recognized in the early 1950's, around the time Linus Pauling discovered the actin protein's a and b conformations. After an initial rush to develop stem cell therapies as treatment for a variety of cancers and other diseases, immune compatibility was identified as a growing problem - cryogenic facilities to store bone marrow for autologous transplant were built in the early 1960's. The fibroblast-cancer association then was ignored or suppressed for several decades, but is now being revisited. For example:


2003 - Stem cells and breast cancer: A field in transit. Nat Rev Cancer. 2003 Nov;3(11):832-44. Smalley M, Ashworth A. The Breakthrough Breast Cancer Research Centre, Institute of Cancer Research, Fulham Road, London SW3 6JB, UK. PMID: 14668814

2003 - Mutant Stem Cells May Seed Cancer

2004 - "We generated expression profiles of cancer-associated fibroblasts using oligochip arrays and compared them to those of uninvolved fibroblasts. ...The distinct molecular expression profiles of cancer-associated fibroblasts in colon cancer metastasis support the notion that these fibroblasts form a favorable microenvironment for cancer cells."
Role of cancer-associated stromal fibroblasts in metastatic colon cancer to the liver and their expression profiles. Oncogene. 2004 Sep 23;23(44):7366-77. Nakagawa H, Liyanarachchi S, Davuluri RV, Auer H, Martin EW Jr, de la Chapelle A, Frankel WL. Division of Human Cancer Genetics, Comprehensive Cancer Center, The Ohio State University, Columbus 43210, USA. PMID: 15326482

2005 - "Although the link between Helicobacter pylori infection and gastric cancer is well established, new research suggests that stem cells play an important role in the development of this malignant disease. JeanMarie Houghton and colleagues recently showed that H. pylori-induced inflammation in mice caused the migration of stem cells originating from bone marrow to the stomach, where they subsequently developed into gastric tumours.1Previous evidence suggests that bone-marrow-derived cells have a reparative function on being recruited to areas of injury or inflammation. The idea that these cells might also play a role in the development of cancer revisits a concept that arose partly from the observation in the 1970s that only 1% of leukemia cells grow into colonies in vitro, an ability that later earned these cells the label "cancer stem cells."2 Houghton and colleagues' research suggests that similar stem cells may give rise to gastric cancer, a finding that presents a new way of thinking about the pathogenesis of a disease that is the second leading cause of cancer-related deaths worldwide, killing nearly 600 000 people each year."
Do stem cells cause gastric cancer? CMAJ. 2005 Feb 1;172(3):325-6. Secko D. PMID: 15684111

2005 - "The identification of neurospheres from adult brain tumors, and specifically from an adult GBM, is strengthening the case for the importance of cancer "stem" cells in the genesis of these malignancies. A thorough genetic dissection of such cells on a larger scale should give new insights for the therapeutic targeting of these cancer "queen-bee" cells."
Molecular Cancer 2004 Oct 6;3:25. Genetic alterations and in vivo tumorigenicity of neurospheres derived from an adult glioblastoma. Tunici P, Bissola L, Lualdi E, Pollo B, Cajola L, Broggi G, Sozzi G, Finocchiaro G. Istituto Nazionale Neurologico Besta, Dept. Experimental Neurology, Milano, Italy. pat.tunici@libero.it PMID: 15469606


Glossary of Stem Cell-Related Terms
Stem Cell Glossary



posted on Dec, 4 2005 @ 01:29 PM
link   

Originally posted by mattison0922

Marg, I know this wasn't directed at me, but I'll make an effort to field it.


Thanks matt, and you explanation is welcome, sorry it took this long for the reply.



Cancer and TSEs (prion diseases) are both molecular diseases, ie: there is a difficulty at the cellular level, it manifests itself on the organismal and systemic levels, but is distinctly a cellular disorder.


Yes I understand the nature of cancer.



Cancers arise as a consequence of errors/mutations in particular genes that are related to some aspect of cellular growth. You can think of cancer very simply actually:


Yes I understand but can prion be the cause of the mutations in our genes? We have an explanation for cancer but do we have a reason as why cancer happens?



Most specialists believe that for cancer to occur, at least 3 or 5 critical cell cycle control genes must be affected.


Yes find it very interesting that we actually do no know much as what makes cells behave they way they do and grow out of control.



In the case of a TSE, somehow one of these proteins becomes 'misshapen' in an affected animal. This misshaped protein induces (nucleates) the proteins that are folded correctly to adopt this new, harmful shape. This process continues until the proteins form large aggregates, eventually killing the cells.


That is what I am trying to point out, Matt actually the way protein behave sounds like what cancel do the cells.

Can this be the pre cancer state?

Can we say that cancer and prion disease may be linked? or could it be one the beginning of the other one?

That should be a great research topic.


[edit on 4-12-2005 by marg6043]

[edit on 4-12-2005 by marg6043]



posted on Dec, 4 2005 @ 07:10 PM
link   

As promised mattison.


Thanks Sofi, It’s taken me a little bit to analyze and sort through all the info. I think I’ve a decent grasp of what you’re trying to say.


Note: The premise here is that all disease-causing (pathogenic) misfolded proteins are infectious prions, not just the officially recognized misfolded PrP prion.

I suppose I can live with this particular definition, provided that there is a basis for the infectious presumption… that is infection between organisms… not different cells within the same organism.


For example:

The misfolded isoform of the protein called "a-smooth muscle actin" (ASMA) can be considered an infectious prion strain.

Okay… now you’re going to have to sell me. Certainly, I am no authority on prions, but I have done a fair amount of reading about them, and I’ve never heard this. Furthermore, I did a variety of pubmed searches to verify this claim, and was unable to do so. Though, I don’t believe Pubmed to be the end all of knowledge, and I am certainly open to your perspective. Does any mainstream medical research come out and proclaim this directly, or is this based on your own research?


ASMA can infect connective tissue and smooth muscle stem cells anywhere in the body. ASMA underlies a huge number of acquired/infectious and genetic diseases

Okay… this seems like a leap to me… maybe I’m not reading enough into it. Actin is present in pretty much every cell type in the body. Alpha obviously distinguishes it from the other major isoforms: beta and gamma… alpha tends to be located in the muscle tissue specifically, whereas the beta and gamma forms are associated with intracellular motility and resource distribution. While I am not super-familiar with aMSA per se, isn’t it just the alpha isoform of actin present in smooth muscle?


FMD is important to understanding ASMA-related disease - FMD appears to be a stage in the larger disease process where ASMA uses the vascular system to spread through the body. FMD was discovered/acknowledged officially in the USA in 1938 when a case was proved to have been transmitted congenitally.

Yes, but congenitally is certainly not an infection per se. If the issue is infection, then congenital disorders, as horrible and debilitating as they may be don’t fall under the heading of infectious disease and are thus, not prions. Am I missing something here?


In all ASMA-related diseases, this misfolded protein works the same way - by taking over partially differentiated stem cells for connective tissue and/or smooth muscle. The key connective tissue "stem cell" in ASMA-related diseases is the "fibroblast."

Point taken, but again, can this be really considered ‘infection’ in the classical sense of the definition. This is more akin to an autoimmune disorder, and not an infectious disease.


As a side note: "A stem cell is more than a committed progenitor; it also responds to influences from the extracellular environment," explains Ronald McKay, chief of the laboratory of molecular biology at the National Institute of Neurological Disorders and Stroke.

Well isn’t that pretty much the theme of a Stem Cell: interpret its specific location within an organism/system and differentiate appropriately. The stem cell is a cell with a specific ‘goal’ of responding to the environment.


The disease process

ASMA takes over fibroblasts simply by coming into direct contact with other similarly shaped actin proteins in the stem cell. These proteins replicate into ASMA on contact - the stem cell is taken over as the replicas multiply or proliferate.

The taken-over or mutant stem cell becomes an abnormal myofibroblast. As more stem cells are taken over, abnormal myofibroblasts multiply in tissue, replace normal cells, and abnormal tissue is formed - this process of abnormal tissue formation now is called tissue remodeling or aberrant wound healing. Pathologists categorize the abnormal tissue as dysplasia, fibroplasia, or hyperplasia, as in FMD.

Again, while this is all terribly unfortunate for those afflicted, and in no way am I discounting the significance of these types of disorders, but I just don’t see them as infections, and I’m therefore missing the link between AMSA and prions.


Sometimes, these "plasias" go on to become cancerous. The old mystery is "Why?" Why does some dysplasia and fibroplasia progress to hyperplasia, metaplasia and neoplasia - but not others? The answer is complicated - but generally speaking, what happens to abnormal myofibroblasts once they form depends on other factors, including where they go in the body and what they do - further mutation into cancer occurs only if certain other triggering factors are also present.

Okay… I see the link you’re shooting for between FMD and Cancer, and even AMSA and cancer, but the prion link still escapes me because of the infectious thing. Furthermore, it sounds like there are a bunch of possible factors that could potentially contribute to the development of cancer from these plasias. Though in essence, you are correct, any uncontrolled, inappropriate growth of cells can become cancerous. Though none of this solidifies a link between cancer and prions in my own mind.


The point is - the disease process starts when ASMA prions take over fibroblasts, and turns them into aberrant myofibroblasts.

Okay… but in my mind, the fundamental issue here is whether or not AMSA can be defined as a prion. Without some sort of demonstrated infectivity, it seems like it cannot.



posted on Dec, 4 2005 @ 07:15 PM
link   

Originally posted by marg6043
Yes I understand but can prion be the cause of the mutations in our genes? We have an explanation for cancer but do we have a reason as why cancer happens?

Well, this is the million dollar question, huh? Yes and no. We know the reason, ie: mutation, but we don't necessarily know the reason for the mutation.


That is what I am trying to point out, Matt actually the way protein behave sounds like what cancel do the cells.

Can this be the pre cancer state?

Can we say that cancer and prion disease may be linked? or could it be one the beginning of the other one?

Could be... certainly sofi seems to think so. I certainly wouldn't ever say there can't possibly be a link.

But, Marg, you are correct in earlier statement. Cells are incredibly complex things. We are really just beginning to understand the way many of the complex components interact. I think computers need to be a little more developed, but hopefully we'll have a better handle on these questions in the next ten years or so.



posted on Dec, 4 2005 @ 07:16 PM
link   
ASMA has two isoforms - not generally talked about, but antibody for testing available through at least one lab supplier - will see if I can find the link.

Re: FMD/ASMA cross-species infectivity:

The occurrence of fibromuscular dysplasia in the arteries of domestic turkeys.

Fibromuscular dysplasia in intramuscular arteries of Japanese quail (Coturnix coturnix japonica).


Do you see where I'm going with this?

[edit on 4-12-2005 by soficrow]



posted on Dec, 4 2005 @ 07:25 PM
link   

Originally posted by soficrow
ASMA has two isoforms - not generally talked about, but antibody for testing available through at least one lab supplier - will see if I can find the link.

Re: FMD/ASMA cross-species infectivity:

The occurrence of fibromuscular dysplasia in the arteries of domestic turkeys.

Fibromuscular dysplasia in intramuscular arteries of Japanese quail (Coturnix coturnix japonica).


Do you see where I'm going with this?

[edit on 4-12-2005 by soficrow]


Sofi, these two links obviously speak to the question I was complaining about.

My next question would have to do with the stability of the isoform of ASMA in question. Do you have any links/refs that discuss this. I can see where you are going, but the ability of the isoform in question to survive not only the cooking but digestive process would be where I'd like to take this next.

But... I think your statement Re: FMD/ASMA cross-species infectivity is somewhat misleading. FMD occurs in these critters, probably in an analogous manner to the mechanism in humans, but this doesn't imply infection per se. Simply because these organisms can acquire these diseases doesn't imply they can spread them.

Any info re: this?



posted on Dec, 4 2005 @ 07:26 PM
link   
Thanks Matt I am going to be honest but I am still trying to graps the information, biology is a topic I enjoy very much but I am not expert by any means.

I guess that is why I don't understand many things.

I hope that with time we get to understand the relations of cancer and prions if is one after all.



posted on Dec, 4 2005 @ 07:33 PM
link   

Originally posted by marg6043
... I don't understand many things...

I hope that with time we get to understand the relations of cancer and prions if is one after all.


Marg, I agree with you on both counts.

Seems like the more I learn, the less I feel like I 'know.'



posted on Dec, 4 2005 @ 07:50 PM
link   

Originally posted by mattison0922

My next question would have to do with the stability of the isoform of ASMA in question. Do you have any links/refs that discuss this. I can see where you are going, but the ability of the isoform in question to survive not only the cooking but digestive process would be where I'd like to take this next.



The Crohn's disease link in the first paragraph, plus the fact that ASMA/myofibroblasts are commonly linked to colon cancer - indicate ASMA's ability to survive in the digestive tract. Ie: Leading-Edge Myofibroblasts in Human Colon Cancer

...Sorry - don't have anything on heat. Good question. Will see what I can find.




But... I think your statement Re: FMD/ASMA cross-species infectivity is somewhat misleading. FMD occurs in these critters, probably in an analogous manner to the mechanism in humans, but this doesn't imply infection per se. Simply because these organisms can acquire these diseases doesn't imply they can spread them.

Any info re: this?



FMD is commonly recognised as being "familial" and "acquired." The latest studies in France found FMD cases studied to be roughly 10% familial and 90% acquired - about the same spread as acknowledged prion diseases. Ie: Orphanet: "The disorder seems to be inherited in 10% of cases."

FMD prevalence in the USA does imply infectivity: In the US: The reported incidence of FMD in adults is 0.6% via angiography and 1.1% via autopsy.


.



posted on Dec, 4 2005 @ 07:51 PM
link   

Originally posted by mattison0922

Originally posted by marg6043
... I don't understand many things...

I hope that with time we get to understand the relations of cancer and prions if is one after all.


Marg, I agree with you on both counts.

Seems like the more I learn, the less I feel like I 'know.'


Ditto. Ditto.



But this all is great fun, dontcha think?



posted on Dec, 5 2005 @ 09:18 AM
link   

Originally posted by soficrow
The Crohn's disease link in the first paragraph, plus the fact that ASMA/myofibroblasts are commonly linked to colon cancer - indicate ASMA's ability to survive in the digestive tract. Ie: Leading-Edge Myofibroblasts in Human Colon Cancer

Okay... quick question... survive or found in... Does the ASMA survive passage into the intestines, or does it happen to appear there? I'm not a physiologist, but isn't the intestinal tract composed of smooth muscle tissue? Given this, is it unreasonable to find ASMA in the intestines? And finally, can we assume that it survives passage through the digestive system simply because it's found there?

Still looking at your other info



posted on Dec, 5 2005 @ 09:47 AM
link   

Originally posted by mattison0922

Originally posted by soficrow
The Crohn's disease link in the first paragraph, plus the fact that ASMA/myofibroblasts are commonly linked to colon cancer - indicate ASMA's ability to survive in the digestive tract. Ie: Leading-Edge Myofibroblasts in Human Colon Cancer

Okay... quick question... survive or found in... Does the ASMA survive passage into the intestines, or does it happen to appear there?


Hmmm. It's found there at various stages in the disease process, so obviously it's surviving there.

...The question of where and how prions originate is another track - am working on a post. It's too complicated to sew up quickly.





I'm not a physiologist, but isn't the intestinal tract composed of smooth muscle tissue? Given this, is it unreasonable to find ASMA in the intestines?


The ASMA found is pathogenic, specifically associated with myofibroblasts - and also is found in other smooth muscle and connective tissue throughout the body in various other diseases.

So is it unreasonable to find the pathogenic isoform of ASMA in the intestines, associated with intestinal disease? The same one that's associated with a wide variety of "different" diseases in other parts of the body? ...Seems like a predictable part of the package imo.




And finally, can we assume that it survives passage through the digestive system simply because it's found there?


I would say yes. And don't forget your basic anatomy - pathogens like prions pass from the gut to the lymphatics then to the blood. (They're tiny, and they don't trigger an immune response.)




clarification

[edit on 5-12-2005 by soficrow]



posted on Dec, 5 2005 @ 11:08 AM
link   
regarding an earlier statement:
No one can say for certain if some people are "immune"...

What they CAN say, is that some people exposed to prions dont show any sign of contamination even decades after exposure...

and animals also... it is a theory at this point, that some genetic types dont allow contamination as easily as others...

as far as it being a "poor vs rich" thing... anyone who thinks so would be fooling themselves...
the elites are just as worried that they will get contaminated as well... perhaps more so, since routinely they understand the threat better than the average population "joe". (because of info that is not released to the sheeple population)

prions are in everything... and can contaminate anything organic that uses protiens... so no one can hide from them...

So the theory is formed from the assumption that we all should be infected, and for some reason, most aren't... this is even considering the variant non lethal forms of the protien. Some people still test clean for prion protien formation.

As Sofi has pointed out, there are still new diseases being discovered that have their roots in prion causes... even a study that links heart disease...
for all we know, 50-80% of disease could actually be caused by prion protien defects...

so theorys are what they are, and right now... the theorys fall in two classes...
the "some are immune" side (due to nonpervasive contamination)
and the "we are all screwed" side. (due to unseen contamination that is pervasive)

Does that clarify my statement earlier well enough?
IMO that there is some immunity to some prion diseases in some people...
and that is only a theory at this point... a rather hopeful one... as the option looks very bad for humanity.



posted on Dec, 5 2005 @ 12:15 PM
link   

Originally posted by soficrow

Hmmm. It's found there at various stages in the disease process, so obviously it's surviving there.

...The question of where and how prions originate is another track - am working on a post. It's too complicated to sew up quickly.

I guess that's the question: What is the origin of the ASMA you're referring to in the intestinal tract.


So is it unreasonable to find the pathogenic isoform of ASMA in the intestines, associated with intestinal disease? The same one that's associated with a wide variety of "different" diseases in other parts of the body? ...Seems like a predictable part of the package imo.

Hmmm... this statement leads me to believe we're on the same page, but gut instinct says no. What do you think?


I would say yes. And don't forget your basic anatomy - pathogens like prions pass from the gut to the lymphatics then to the blood. (They're tiny, and they don't trigger an immune response.)


Forget? Please... you can't forget what you never knew in the first place.


Like I said, I am no phyisiologist.


[edit on 5-12-2005 by mattison0922]



posted on Dec, 5 2005 @ 01:04 PM
link   

LazarustheLong

so theorys are what they are, and right now... the theorys fall in two classes...
the "some are immune" side (due to nonpervasive contamination)
and the "we are all screwed" side. (due to unseen contamination that is pervasive)



There is a third theory: that we are witnessing a rapid escalation of the evolutionary process, not necessarily an evolutionary crisis destined to result in extinction.

IMO - prions mediate between apparently disparate parts of the ecological system, and are effecively an inter-communications sub-system that works to re-establish harmony. In this view, "disease" is part of the adaptive process, and will lead to evolutionary change.

RE: No effects to prion exposure after decades.

Prion diseases can take decades to manifest - and may not present with recognizable symptoms. Also, prion-related diseases are multifactorial - everything influences everything about them - amount of exposure, exposure to other contaminations, co-infections, the works. The right combination of factors might delay onset for 5 decades - the wrong combination could result in rapidly progressive disease that kills in 6 months.

However - whether or not the disease manifests, it may be transmissble genetically or congenitally. Which would explain the epidemic of "age-related" and other chronic disease in children.



Originally posted by mattison0922


So is it unreasonable to find the pathogenic isoform of ASMA in the intestines, associated with intestinal disease? The same one that's associated with a wide variety of "different" diseases in other parts of the body? ...Seems like a predictable part of the package imo.

Hmmm... this statement leads me to believe we're on the same page, but gut instinct says no. What do you think?



Not sure i get your question - but - if you're suggesting that pathogenic ASMA is a natural product in the body, and supposed to be there - then no, we're not on the same page.

...FYI - Merck led a campaign in 2003 (?) to say FMD/ASMA tissue remodeling was a "natural consequence of aging." It's not - and the campaign was shot down fairly quickly. The notion of myofibroblasts/ASMA being natural is just the same campaign, repackaged. It too will be shot down.




.



posted on Dec, 5 2005 @ 01:23 PM
link   
Supposedly, most disease is "genetic," and we hear a lot about genetic susceptibility these days. But the fact is, most cancer- and disease-causing genetic mutations are new.

So the question is: What's causing all these new mutations?

Answer: Different strains of infectious prions, in conjunction with: medical and other radiation exposure, medical drugs that break polymers, environmental contaminations, and contaminated food, air and water.


Of interest:

"Prions and other misfolded proteins can cause a wide variety of diseases, including the human version of mad cow, Alzheimer's, Parkinson's, diabetes, cystic fibrosis, and even cancer."

"Misfolded proteins are the basis of a number of seemingly unconnected diseases, including age-related diseases like type II diabetes, Alzheimer's and Parkinson's, as well as 'mad cow' (BSE) and other prion diseases."

Nature: "...misfolded proteins are behind diseases as diverse as type II diabetes, CJD and Alzheimer's."

ScienceDaily: "Patients suffering from diseases as varied as Type II diabetes, Alzheimer's, Parkinson's and dozens of lesser known maladies have one thing in common: they suffer from a large build up of amyloids, tissue that's created when millions upon millions of misfolded proteins stick together and form a mass that the body can't get rid of on its own."

"A variety of debilitating diseases including diabetes, Alzheimer's, Huntington's, Parkinson's, and prion-based diseases are linked to stress within the endoplasmic reticulum (ER). ...Our results demonstrate a direct mechanism(s) by which misfolded proteins lead to cellular damage and death."




Despite reality, the genetics myth has spurred research to genetically engineer prion-immune cattle in the USA,


Cows immune to BSE near reality

A major advance towards producing prion-free cows that would be immune to mad cow disease has been made by researchers at companies in the US and Japan.

Their principal aim is to make genetically modified cattle that produce pharmaceuticals in their milk. But the companies hope that also making the animals resistant to BSE (bovine spongiform encephalopathy) will reassure consumers.



...and to try to breed prions out of sheep flocks in the European Union. But it's not working.


A NEW form of scrapie, the prion disease that affects sheep, could derail European Union plans to breed scrapie out of Europe's flock.

...an EU monitoring programme that started in 2002 has found that 20 per cent of the sheep and goats that tested positive for scrapie also have unusual prions. ...Both the Norwegian and the European tissue caused the same unusual brain changes, suggesting that the animals it came from all had the same, previously unrecognised, form of scrapie."

Sue Bellworthy and colleagues at the UK’s Veterinary Laboratories Agency (VLA) report that two ewes experimentally infected with BSE in a flock in Warwickshire in 2000 gave birth to lambs in 2003 that died of BSE this year. This is the first confirmation of “vertical” transmission of BSE from mother to offspring. It has been suspected but never proved in cattle.




The idea that prion-immune cattle can be genetically engineered is a joke - the modern equivalent of snake-oil, nothing more than an investment rip-off scam - and will fail for several reasons:

1. There already are many more prion strains than are officially recognized - GM cattle are immune to only one or two specific strains;
2. New prion strains are created regularly through various industrial processes, and when normal proteins are exposed to environmental contamination - again, GM cattle aren't immune to new prion strains;
3. Existent prions create new strains when exposed to common environmental changes, like shifts in temperature - GM cannot possibly keep pace with the rate new strains appear;
4. Infected animals and people excrete prions in their urine, so soil and water are and will remain reservoirs for old and new prion strains;
5. Prions are transmitted vertically and horizontally, despite industry's gyrations and denial of the epidemiological evidence - GM does not even address this very real problem, never mind solve it.




"Discovery of mutations in the PrP genes of humans with GSS and familial CJD established that prion diseases are both genetic and infectious."

"Epidemiological observations indicate that a microbial vector is responsible for the transmission of natural prion disease in sheep and goats … A similar phenomenon was already described with a protein antigen of the ameba Naegleria gruberi. ...It is proposed that many microbial proteins may be capable of replicating themselves in mammalian cells eliciting and sustaining thereby degenerative and/or autoimmune reactions subsequent to infections with microorganisms.”

"Fly larvae and mites were exposed to brain-infected material and were readily able to transmit scrapie (prions) to hamsters. New lines of evidence have confirmed that adult flies are also able to express prion proteins. Several cell types found on the human skin, including keratinocytes, fibroblasts and lymphocytes, are susceptible to the abnormal infective isoform of the prion protein, which transforms the skin to produce a potential target for prion infection."




Epidemic prion-related disease is being (mis)handled as a "marketing opportunity" - not a public health crisis. Everyone will be at risk until this focus shifts - especially our children.


...The above statement might be seen as contradicting my response to LazarustheLong, above - but in the end it's not.



posted on Dec, 7 2005 @ 11:05 AM
link   
From the Nature article:


[Prions suspected in milk

Adriano Aguzzi, the lead researcher on the study, has not detected prions in milk itself, because it is difficult to analyse for the abnormal proteins. But he says he expects to find them.

"It is unlikely that the prions are not in the milk," says Aguzzi, a pathologist at the University of Zurich Hospital, Switzerland. "And the prospect is not a pleasant one."

Neil Cashman, a prion researcher at the University of British Columbia in Vancouver, is worried too. People have looked for prions in the milk of cows with BSE and haven't found any, he says. "But they haven't looked in cows with mammary-gland infection and BSE."

"This raises very serious questions," concludes Cashman.




Apparently, prions are most likely to be found in milk when there is a viral co-infection. Prions hitchhike on viruses.


Also see:

* Source: Grand Forks Agricultural Weekly. Research: Prions may be found in milk

* Vertical Transmission of Bovine Spongiform Encephalopathy Prions Evaluated in a Transgenic Mouse Model



posted on Dec, 7 2005 @ 11:09 AM
link   
Sofi does that mean that our cows can be infected and passing infection in the milk?

With all the process do to the mild products in our nation can that help? I know somebody before me already ask about that but I still wonder.

We don't know much about the type of research is been done to our cattle, all I know is that UGA is doing mad cow diseases research but nothing more.



new topics

top topics



 
7
<< 1    3 >>

log in

join