Bovine spongiform encephalopathy
hideBovine spongiform encephalopathy (BSE), commonly known as mad-cow disease (MCD), is a fatal, neurodegenerative disease in cattle, that causes a spongy degeneration in the brain and spinal cord. BSE has a long incubation period, about 4 years, usually affecting adult cattle at a peak age onset of four to five years, all breeds being equally susceptible. In the United Kingdom, the country worst affected, more than 179,000 cattle have been infected and 4.4 million slaughtered during the eradication programme.
It is believed by most scientists that the disease may be transmitted to human beings who eat the brain or spinal cord of infected carcasses. In humans, it is known as new variant Creutzfeldt-Jakob disease (vCJD or nvCJD), and by February 2009, it had killed 164 people in Britain, and 42 elsewhere with the number expected to rise because of the disease's long incubation period. Between 460,000 and 482,000 BSE-infected animals had entered the human food chain before controls on high-risk offal were introduced in 1989.
A British inquiry into BSE concluded that the epidemic was caused by cattle, who are normally herbivores, being fed the remains of other cattle in the form of meat and bone meal (MBM), which caused the infectious agent to spread. The origin of the disease itself remains unknown. The infectious agent is distinctive for the high temperatures at which it remains viable; this contributed to the spread of the disease in Britain, which had reduced the temperatures used during its rendering process. Another contributory factor was the feeding of infected protein supplements to very young calves.
For more information about Bovine spongiform encephalopathy, read the full article at
Wikipedia.
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News tagged with mad cow disease
Researchers find new piece of BSE puzzle
Nov 20, 2009 |
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A new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease (CJD) could be a step closer based on new results from scientists at the University of Leeds. The team has found ...
Scientists uncover evolutionary origins of prion disease gene
Sep 28, 2009 |
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A University of Toronto-led team has uncovered the evolutionary ancestry of the prion gene, which may reveal new understandings of how the prion protein causes diseases such as bovine spongiform encephalopathy (BSE), also ...
IOM report released on species-jumping diseases
Sep 22, 2009 |
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Significant weaknesses undermine the global community's abilities to prevent, detect early, and respond efficiently to potentially deadly species-crossing microbes, such as the pandemic H1N1 influenza virus sweeping the globe, ...
Gene mutation alone causes transmissible prion disease
Medicine & Health / Neuroscience
Aug 26, 2009 |
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For the first time, Whitehead Institute researchers have shown definitively that mutations associated with prion diseases are sufficient to cause a transmissible neurodegenerative disease.
Top food scientist to target hidden fish allergens, pork, with new tests
Jun 29, 2009 |
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The odds of contracting mad cow disease from banned or adulterated bovine protein lurking in raw or processed food for humans or meat-bone meal for livestock have declined over the past decade. So have the ...
Swine flu having powerful impact on us
May 06, 2009 |
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The new influenza A (H1N1), known as the swine flu, demonstrates the power of people's perceptions of risk. Sales of face masks are breaking all records not only in Mexico but also in Sweden. Hotel guests are being isolated ...
Humans are responsible for swine flu
May 01, 2009 |
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Swine flu. Bird flu. Mad cow disease. SARS. These diseases have all spread from animals to humans in one form or another. But animals aren't to blame for outbreaks of animal-borne diseases -- humans are.
Iron is involved in prion disease-associated neuronal demise
Mar 13, 2009 |
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Imbalance of iron homeostasis is a common feature of prion disease-affected human, mouse, and hamster brains, according to a new study by Dr. Neena Singh and colleagues at Case Western Reserve University School of Medicine, ...
Antibody key to treating variant CJD, scientists find
Mar 04, 2009 |
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Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.
