Cannabis Health Search

Mad Cow Disease and cannabis research

Overview

Mad cow disease is an infectious disease in the brain of cattle. Variant Creutzfeldt-Jakob disease (vCJD) is the human form of mad cow.

Science and Research

Cannabidiol May be Effective in Preventing Bovine Spongiforme Enzephalopathy (Mad Cow Disease)

J Neurosci 2007;27(36):9537-44
According to basic research of scientists of the National Centre for Scientific Research in Valbonne, France, cannabidiol (CBD) may prevent the development of prion diseases, the most known being BSE (bovine spongiforme enzephalopathy), which is often called mad cow disease. It is believed that the BSE may be transmitted to human beings. In humans, it is known as Creutzfeldt-Jakob disease.

The infectious agent in prion diseases is believed to be a specific type of misfolded protein called prion. Misfolded prion proteins carry the disease between individuals and cause deterioration of the brain. The French researchers reported that the non- psychoactive cannabis constituent CBD inhibited the accumulation of prion proteins in both mouse and sheep prion- infected cells, whereas other cannabinoids were either weak or not effective. Moreover, after infection with mouse scrapie, a prion disease, CBD limited accumulation of the prion protein in the brain and significantly increased the survival time of infected mice. CBD inhibited the nerve damaging effects of prions in a concentration-dependent manner. Researchers noted that CBD may be a promising agent for the treatment of prion diseases.

(Source: Dirikoc S, Priola SA, Marella M, Zsuerger N, Chabry J. Nonpsychoactive cannabidiol prevents prion accumulation and protects neurons against prion toxicity. J Neurosci 2007;27(36):9537-44.)

 

 
Prion diseases are transmissible neurodegenerative disorders characterized by the accumulation in the CNS of the protease-resistant prion protein (PrPres), a structurally misfolded isoform of its physiological counterpart PrPsen. Both neuropathogenesis and prion infectivity are related to PrPres formation. Here, we report that the nonpsychoactive cannabis constituent cannabidiol (CBD) inhibited PrPres accumulation in both mouse and sheep scrapie-infected cells, whereas other structurally related cannabinoid analogs were either weak inhibitors or noninhibitory.
 
Moreover, after intraperitoneal infection with murine scrapie, peripheral injection of CBD limited cerebral accumulation of PrPres and significantly increased the survival time of infected mice. Mechanistically, CBD did not appear to inhibit PrPres accumulation via direct interactions with PrP, destabilization of PrPres aggregates, or alteration of the expression level or subcellular localization of PrPsen. However, CBD did inhibit the neurotoxic effects of PrPres and affected PrPres-induced microglial cell migration in a concentration-dependent manner.
 
Our results suggest that CBD may protect neurons against the multiple molecular and cellular factors involved in the different steps of the neurodegenerative process, which takes place during prion infection. When combined with its ability to target the brain and its lack of toxic side effects, CBD may represent a promising new anti-prion drug.
 
Distributed without profit to those who have expressed a prior interest in receiving the included information for research and educational purposes.
 

Pot smoking could stop Mad Cow Disease?

A NEW Zealand pro-cannabis group believes it has scientific evidence that cannabis can stop the development of mad cow disease the New Zealand Press Association reported today. The National Organization for the Reform of Marijuana Laws (Norml) sited a French study showing cannabidiol might be effective in preventing bovine spongiform encephalopathy (BSE), also known as mad cow disease.

Scientists at the National Center for Scientific Research in France found cannabidiol – a non-psychoactive ingredient, may prevent the development of prion diseases (progressive neurodegenerative disorders), the most well known of which is BSE, Norml said.

Researchers found cannabidiol inhibited the accumulation of prion proteins in infected mice and sheep.

Norml spokesman Chris Fowlie said the discovery added to the scientific evidence supporting a bill from a New Zealand Greens MP  to legalise the medicinal use of cannabis. Mr Fowlie also said:

“(It) should be supported by any MP with a clear head. Unfortunately most politicians act like mad cows whenever cannabis is mentioned.”

 

 

 

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Cannabidiol Prevents Prion Accumulation and Protects Neurons against Prion Toxicity

  1. Sevda Dirikoc
  2. Suzette A. Priola
  3. Mathieu Marella
  4. Nicole Zsürger
  5. Joëlle Chabry

 Author Affiliations

  1. Institut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 6097, Centre National de la Recherche Scientifique, 06560 Valbonne, France,
  2. Laboratory of Persistent Viral Diseases, National Institutes of Health, National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, Hamilton, Montana 59840, and
  3. Scripps Research Institute, La Jolla, California 92037
  1. Correspondence should be addressed to Dr. Joëlle Chabry, Institut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 6097, Université de Nice-Sophia Antipolis, Centre National de la Recherche Scientifique, 660, route des lucioles, 06560 Valbonne, France. chabry@ipmc.cnrs.fr

Abstract

Prion diseases are transmissible neurodegenerative disorders characterized by the accumulation in the CNS of the protease-resistant prion protein (PrPres), a structurally misfolded isoform of its physiological counterpart PrPsen. Both neuropathogenesis and prion infectivity are related to PrPres formation. Here, we report that the nonpsychoactive cannabis constituent cannabidiol (CBD) inhibited PrPres accumulation in both mouse and sheep scrapie-infected cells, whereas other structurally related cannabinoid analogs were either weak inhibitors or noninhibitory.

 

Moreover, after intraperitoneal infection with murine scrapie, peripheral injection of CBD limited cerebral accumulation of PrPres and significantly increased the survival time of infected mice. Mechanistically, CBD did not appear to inhibit PrPres accumulation via direct interactions with PrP, destabilization of PrPres aggregates, or alteration of the expression level or subcellular localization of PrPsen. However, CBD did inhibit the neurotoxic effects of PrPres and affected PrPres-induced microglial cell migration in a concentration-dependent manner.

 

Our results suggest that CBD may protect neurons against the multiple molecular and cellular factors involved in the different steps of the neurodegenerative process, which takes place during prion infection. When combined with its ability to target the brain and its lack of toxic side effects, CBD may represent a promising new anti-prion drug.