Comments on: Fishing expedition reveals unexpected link between Alzheimer's and prion diseases

By: Hesitant Iconoclast

Hesitant Iconoclast — Sat, 28 Feb 2009 21:58:59 +0000

Some articles already out there on this topic are suggesting that the prion proteins are gained from eating meat/beef, and that this is the link. What do you think about this proposal, Ed?
The link does strike me as tenuous, but I would appreciate knowing your thoughts on it?

By: Stagyar zil Doggo

Stagyar zil Doggo — Sat, 28 Feb 2009 11:22:51 +0000

MarkH:
Would it be correct to say that Kuru and vCJD (or is it nvCJD?) are essentially the same disease, with the exception that the former is acquired by eating affected human brains whereas the latter is acquired by eating infected bovine brains?

By: MarkH

MarkH — Thu, 26 Feb 2009 21:25:12 +0000

My understanding is since cannibalism was discouraged in endemic areas, Kuru has ceased to exist. Several distinct prion diseases exist, some only in specific animal populations that luckily don’t seem to jump into humans like one currently afflicting deer in north America.

By: Angler

Angler — Thu, 26 Feb 2009 11:38:49 +0000

I never thought that you’ll use the term fishing for this. But actually I had a wonderful insight about your topic and it impressed me. Oh well, thanks for the post buddy. And I hope you could also clarify those issues that are posted in your comments box. God bless

By: natural cynic

natural cynic — Thu, 26 Feb 2009 07:13:45 +0000

As an addendum, the lack of a prion protein in knockout mice may not be noticeable in an uncompetitive mouse lab environment, but it could give a minor developmental advantage in primitive humans in their environment.

By: natural cynic

natural cynic — Thu, 26 Feb 2009 06:54:15 +0000

A Willow:
Wouldn’t the protein be selected against,or is the frequency of disease too low to make a difference?
The function of the prion protein is unknown AFAIK. Possible functions include trace metallic ion transport and formation of synapses with other proteins.
From an evolutionary view, the diseases considered here are late developing: Alzheimer’s in old age [>50], the same with CJD and kuru. This is long past the age of reproduction so there would be virtually no selection pressure against them – especially in a primitive society where the average age for an adult dying is 40-45. People died from something else before the diseases could be observable.

By: Nathan Myers

Nathan Myers — Thu, 26 Feb 2009 05:28:37 +0000

Ewan: Everyone hoping for exposure sends pre-pub papers to Ed in hopes he’ll write them up, ready to post on publication date. Someday soon, grant applications and C.V.’s will proudly cite him. Ed will be the king-maker. Nobel prizes will be competed for only among those Ed has anointed as Worthy of Wider Exposure.

By: Ewan

Ewan — Thu, 26 Feb 2009 04:30:25 +0000

Good grief, Ed. I just went to look at the article, and you’ve already got an 1100-word post up?
Colour me impressed. Geez.

By: A. Willow

A. Willow — Thu, 26 Feb 2009 03:41:26 +0000

These are probably stupid questions,I’m more interested than knowledgable here,but how is it,if mice lacking the prion protein are/seem normal,i.e. the protein is not essential,it can have such devastating effects when it misfunctions? Especially when it can be linked to more than one disease.Wouldn’t the protein be selected against,or is the frequency of disease too low to make a difference? Is the function of normal prion proteins known?

By: Ed Yong

Ed Yong — Wed, 25 Feb 2009 22:38:41 +0000

I mentioned scrapie, but it’s a separate diseases to CJD and BSE – afflicts goats and sheep. Kuru, it seems, is also a distinct disease.