New Creutzfeld-Jakob-like Dementia Discovered In 16 Americans - New Scientist

[hatrack]

A NEW form of fatal dementia has been discovered in 16 Americans, 10 of whom have already died of the condition. It resembles Creutzfeldt-Jakob disease - with patients gradually losing their ability to think, speak and move - but has features that make it distinct from known forms of CJD.

No one yet knows how the disease originates, or under what conditions it might spread. Nor is it clear how many people have the condition. "I believe the disease has been around for many years, unnoticed," says Pierluigi Gambetti, director of the US National Prion Disease Pathology Surveillance Center at Case Western Reserve University in Cleveland, Ohio. Cases may previously have been mistaken for other forms of dementia.

Since Gambetti's team wrote a paper describing an initial 11 cases referred to his centre between 2002 and 2006 (Annals of Neurology, vol 63, p 697), another five have come to light.

EDIT

http://www.newscientist.com/article/mg19926643.700-ten-people-die-from-new-cjdlike-disease.html?DCMP=ILC-hmts&nsref=news2_head_mg19926643.700

Sorry, that's all I could get - subscription service.

[still_one]

1. might possibly be mad cow disease /nt

[Trillo]

2. Dying like this is probably not so bad.

we all have to go sometime. By destroying the brain first, one would think one would be less aware of the process.

[hatrack]

3. From what I've read, it's horrible

Intense, grisly hallucinations, extreme pain, loss of muscle coordination.

[Trillo]

6. It probably is very frightening to others watching the process.

If something attacks the brain, like this disease is reported to do, then without a brain, or some significant portions of it, how can that person possibly be aware of such symptoms? Typical Alzheimers is probably similar -- a kindness bestowed by nature.

I once watched a person having an epileptic seizure on the floor. They sure looked like they were in pain. Later, I asked about it. The person claimed they didn't remember it. So maybe they were in pain while it was happening, but afterward, there was no apparent memory of the pain.

[Howzit]

7. It isn't an all or nothing disease, but a slow degradation more like a series of strokes

Just imagine you find you just can't find the words anymore. That you just can't pronounce them anymore. Imagine progressive loss of coordination. Imaging your thinking becoming more and more irrational, but knowing something is very wrong.

All this before you become oblivious. Not like drinking yourself into oblivion. Not pleasant at all.

[kristopher]

4. Original article clip - this is going into a totally new area of prion research

Start>>Human prion diseases or transmissible spongiform encephalopathies may be sporadic, inherited, or acquired by infection.<1> Creutzfeldt-Jakob disease (CJD) is the most common phenotype and occurs in all three forms. In the sporadic form, CJD is classified into five subtypes, which can be readily distinguished based on clinical features, type and distribution of brain lesions, and pattern of prion protein (PrP) immunostaining.<2><3> Fatal insomnia, a much rarer phenotype, includes sporadic and inherited forms, and is characterized by loss of ability to sleep and preferential thalamic degeneration.<4> Gerstmann-Sträussler-Scheinker disease (GSS), the third phenotype, occurs exclusively as a heritable disease invariably associated with a mutation in the PrP gene open reading frame (ORF) and is characterized by the presence of prion amyloid plaques.<4>

Despite their heterogeneity, all sporadic human prion diseases described to date have been associated with abnormal PrP (commonly called PrPSc but henceforth referred to as PrPr), which is resistant to treatment with proteases and is considered the diagnostic hallmark of these diseases.<1> PrPr is derived from normal or cellular PrP (PrPC) via a posttranslational transition from -helical to -sheet-rich conformations. PrPC and PrPr are quite different. Whereas PrPC is soluble in nondenaturing detergents and is completely digested when exposed to appropriate concentrations of proteinase K (PK), PrPr is detergent insoluble and its C-terminal region resists PK treatment.<5> Based on the size of their PK-resistant fragments, at least three major PrPr types are recognized, which codistribute with specific disease phenotypes: (1) PrPr type 1, which on PK treatment generates an approximately 21kDa fragment; (2) PrPr type 2, generating an approximately 19kDa fragment; and (3) PrP7-8, a PrP internal fragment of 7 to 8kDa.<4-6> Both PrPr types 1 and 2 have been observed associated with distinct subtypes of CJD. To date, PrP7-8 has been consistently observed only in GSS. Therefore, the conformational changes, which render PrPr pathogenic and in many but not all cases infectious, may engender different species or strains of PrPr that can be recognized based on their distinct protease-resistant fragments and by their associated clinicopathological phenotype.<5><7-12>

Studies mostly based on experimental models recently have shown that PK-resistant PrP (PrPr) is associated with varying quantities of a PrP isoform that, as PrPr, is detergent insoluble but sensitive to protease digestion (PrPs).<11-15> The relation of PrPs with PrPr and the role that PrPs plays in the pathogenesis of prion diseases remains uncertain.<16-18>

Here we report 11 patients with a human disease characterized by the presence of detergent-insoluble PrP that is predominantly sensitive to protease digestion and forms unusual immunohistochemical patterns. Furthermore, the small amount of PrPr present generates a distinct profile on immunoblot. Several affected patients have family histories of dementia but lack mutations in the PrP gene ORF. We refer to this condition as protease-sensitive prionopathy (PSPr). PSPr broadens the spectrum of human prion diseases and raises several important issues related to the nature of these diseases in light of their association with different PrP isoforms. Among prion diseases, PSPr is not rare. Because the presenting clinical signs often suggest the diagnosis of non-Alzheimer's dementia, PSPr may be even more prevalent than our data indicate because many PSPr cases might currently be classified within this group of dementias. Parts of this study have been presented previously.<19>


End>>These mouse models and now our cases raise issues with the definition of prion diseases. Currently, it is unclear whether PSPr is transmissible because time-consuming transmissibility experiments to different lines of Tg mice and in vitro PrP replication are still ongoing. Should PSPr not be transmissible, the question is whether it is a prion disease. A similar question can be raised for GSS, of which to date only one subtype has been shown to be consistently transmissible.<4> The issue is further compounded by the recent evidence that amyloid , the pathogenic peptide of Alzheimer's disease, has the propensity to replicate after inoculation into susceptible Tg mice in a conformation-dependent fashion reminiscent of prions.<36> These findings appear to blur the once tight association of prion diseases and transmissibility. It may be more practical to apply the label of prion diseases to all conditions in which the PrP is abnormal and appears to play a central role in the pathology, as in all prion diseases known to date and in PSPr.<37> In contrast, one might reserve the qualification of transmissible to those prion diseases that can be transmitted to recipients expressing relatively normal amounts of wild-type PrP.<36>

The finding that several PSPr patients had first-degree relatives diagnosed with dementia necessitates a search for an underlying genetic cause. In AD, the discovery of mutations outside the gene of the amyloid precursor protein (the central protein in AD, as PrP is in prion diseases) has provided a wealth of information regarding pathogenetic mechanisms of AD.<38> Similarly, the discovery of a mutation outside the PrP gene ORF capable of generating a prion disease may greatly expand our understanding of pathogenetic mechanisms and the role of PrP in prion diseases.

Here is the link, but I'm not sure if it is open access: http://www3.interscience.wiley.com/cgi-bin/fulltext/119883040/HTMLSTART

[Speck Tater]

5. In Nov, 2000, time traveler John Titor predicted a big outbreak of CJD

that would turn into a pandemic.

Of course it's hard to take his claim of being a time traveler seriously, but he did mention that the US would go to war with Iraq, but NOT find any WMDs in Iraq. This prediction was made before 9/11.

http://www.johntitor.com/