Medical Hypotheses
Volume 67, Issue 5 , Pages 1027-1033, 2006

Are prions related to the emergence of early life?☆

  • Omar Lupi

      Affiliations

    • Post-Graduation Course of Dermatology (UFRJ, UNI-RIO and Instituto de Dermatologia Prof. Rubem Azulay/Santa Casa do Rio de Janeiro), Rua Frei Leandro, 16/501, 22.470-210 Rio de Janeiro, RJ, Brazil
    • UFRJ – Cidade Universitária, Ilha do Fundão, Zip. 21.941-590, Rio de Janeiro, RJ, Brazil
    • Cryopraxis and Silvestre Laboratory, Cryopraxis, BioRio, Pólo de Biotecnologia do Rio de Janeiro, Av. 24 s/no, Brazil
    • Corresponding Author InformationCorresponding author. Post-Graduation Course of Dermatology (UFRJ, UNI-RIO and Instituto de Dermatologia Prof. Rubem Azulay/Santa Casa do Rio de Janeiro), Rua Frei Leandro, 16/501, 22.470-210 Rio de Janeiro, RJ, Brazil. Tel.: +55 21 2537 7665; fax: +55 21 2521 5812.
    • ,
  • Paula Dadalti

      Affiliations

    • Cryopraxis and Silvestre Laboratory, Cryopraxis, BioRio, Pólo de Biotecnologia do Rio de Janeiro, Av. 24 s/no, Brazil
    • ,
  • Eduardo Cruz

      Affiliations

    • Cryopraxis and Silvestre Laboratory, Cryopraxis, BioRio, Pólo de Biotecnologia do Rio de Janeiro, Av. 24 s/no, Brazil
    • ,
  • Paul R. Sanberg

      Affiliations

    • Center of Excellence for Aging & Brain Repair, and Departments of Neurosurgery, Anatomy, Pharmacology and Therapeutics, and Pathology, University of South Florida College of Medicine, Tampa, FL, USA
    • ,
  • The Cryopraxis’ Task Force for Prion Research

Received 27 April 2006; accepted 28 April 2006. published online 30 June 2006.

Summary 

DNA and RNA are the modern cellular molecules related to the storage and processing of the genetic information. However, in the Earth primeval environment conditions, these two molecules are far from being the best option for this function due to their great complexity and sensibility to heat. Experiments have been showing that proteins are very stable and reliable molecules even in very extreme conditions and, under certain circumstances, could be related to the transmission of certain phenotypes that are inherited in a non-Mendelian manner.

Prions, infective proteins that are associated to several neurological diseases among mammals by replacing their dominant native state of prion protein by a misfolded one, are remarkably resistant to even the most extreme environments. Furthermore, prions are also associated to the transmission of certain fungal traits in an epigenetical model. These two characteristics support the hypothesis that prions are a possible relic of early stage peptide evolution and may represent the reminiscence of a very ancient analogical code of biological transmission of information rather than the digital one represented by modern nucleic acids.

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

☆ Statement of prior presentation: This material or similar material has not been and will not be submitted in any other publication before its appearance in the Proceedings of the Royal Society Biology.

PII: S0306-9877(06)00335-5

doi:10.1016/j.mehy.2006.04.056

Medical Hypotheses
Volume 67, Issue 5 , Pages 1027-1033, 2006

Article Tools