Prion proteins: Physiological functions and role in neurological disorders

Research output: Contribution to journalReview article

Wei Hu, Bernd Kieseier, Elliot Frohman, Todd N. Eagar, Roger N. Rosenberg, Hans Peter Hartung, Olaf Stüve

Stanley Prusiner was the first to promote the concept of misfolded proteins as a cause for neurological disease. It has since been shown by him and other investigators that the scrapie isoform of prion protein (PrPSc) functions as an infectious agent in numerous human and non-human disorders of the central nervous system (CNS). Interestingly, other organ systems appear to be less affected, and do not appear to lead to major co-morbidities. The physiological function of the endogenous cellular form of the prion protein (PrPC) is much less clear. It is intriguing that PrPc is expressed on most tissues in mammals, suggesting not only biological functions outside the CNS, but also a role other than the propagation of its misfolded isotype. In this review, we summarize accumulating in vitro and in vivo evidence regarding the physiological functions of PrPC in the nervous system, as well as in lymphoid organs.

Original languageEnglish (US)
Pages (from-to)1-8
Number of pages8
JournalJournal of the Neurological Sciences
Volume264
Issue number1-2
DOIs
StatePublished - Jan 15 2008

PMID: 17707411

Altmetrics

Cite this

Standard

Prion proteins : Physiological functions and role in neurological disorders. / Hu, Wei; Kieseier, Bernd; Frohman, Elliot; Eagar, Todd N.; Rosenberg, Roger N.; Hartung, Hans Peter; Stüve, Olaf.

In: Journal of the Neurological Sciences, Vol. 264, No. 1-2, 15.01.2008, p. 1-8.

Research output: Contribution to journalReview article

Harvard

Hu, W, Kieseier, B, Frohman, E, Eagar, TN, Rosenberg, RN, Hartung, HP & Stüve, O 2008, 'Prion proteins: Physiological functions and role in neurological disorders' Journal of the Neurological Sciences, vol. 264, no. 1-2, pp. 1-8. https://doi.org/10.1016/j.jns.2007.06.019

APA

Hu, W., Kieseier, B., Frohman, E., Eagar, T. N., Rosenberg, R. N., Hartung, H. P., & Stüve, O. (2008). Prion proteins: Physiological functions and role in neurological disorders. Journal of the Neurological Sciences, 264(1-2), 1-8. https://doi.org/10.1016/j.jns.2007.06.019

Vancouver

Hu W, Kieseier B, Frohman E, Eagar TN, Rosenberg RN, Hartung HP et al. Prion proteins: Physiological functions and role in neurological disorders. Journal of the Neurological Sciences. 2008 Jan 15;264(1-2):1-8. https://doi.org/10.1016/j.jns.2007.06.019

Author

Hu, Wei ; Kieseier, Bernd ; Frohman, Elliot ; Eagar, Todd N. ; Rosenberg, Roger N. ; Hartung, Hans Peter ; Stüve, Olaf. / Prion proteins : Physiological functions and role in neurological disorders. In: Journal of the Neurological Sciences. 2008 ; Vol. 264, No. 1-2. pp. 1-8.

BibTeX

@article{d4c7d73795b8453e80902a92a9314b5c,
title = "Prion proteins: Physiological functions and role in neurological disorders",
abstract = "Stanley Prusiner was the first to promote the concept of misfolded proteins as a cause for neurological disease. It has since been shown by him and other investigators that the scrapie isoform of prion protein (PrPSc) functions as an infectious agent in numerous human and non-human disorders of the central nervous system (CNS). Interestingly, other organ systems appear to be less affected, and do not appear to lead to major co-morbidities. The physiological function of the endogenous cellular form of the prion protein (PrPC) is much less clear. It is intriguing that PrPc is expressed on most tissues in mammals, suggesting not only biological functions outside the CNS, but also a role other than the propagation of its misfolded isotype. In this review, we summarize accumulating in vitro and in vivo evidence regarding the physiological functions of PrPC in the nervous system, as well as in lymphoid organs.",
keywords = "Adaptive immunity, Aging, Alzheimer disease, Cognition, Down syndrome, Innate immunity, Lymphocytes, Neuroprotection, PrP, Primary progressive aphasia, Prion protein, Prnp, Wilson disease",
author = "Wei Hu and Bernd Kieseier and Elliot Frohman and Eagar, {Todd N.} and Rosenberg, {Roger N.} and Hartung, {Hans Peter} and Olaf St{\"u}ve",
year = "2008",
month = "1",
day = "15",
doi = "10.1016/j.jns.2007.06.019",
language = "English (US)",
volume = "264",
pages = "1--8",
journal = "Journal of the neurological sciences",
issn = "0022-510X",
publisher = "Elsevier",
number = "1-2",

}

RIS

TY - JOUR

T1 - Prion proteins

T2 - Journal of the neurological sciences

AU - Hu, Wei

AU - Kieseier, Bernd

AU - Frohman, Elliot

AU - Eagar, Todd N.

AU - Rosenberg, Roger N.

AU - Hartung, Hans Peter

AU - Stüve, Olaf

PY - 2008/1/15

Y1 - 2008/1/15

N2 - Stanley Prusiner was the first to promote the concept of misfolded proteins as a cause for neurological disease. It has since been shown by him and other investigators that the scrapie isoform of prion protein (PrPSc) functions as an infectious agent in numerous human and non-human disorders of the central nervous system (CNS). Interestingly, other organ systems appear to be less affected, and do not appear to lead to major co-morbidities. The physiological function of the endogenous cellular form of the prion protein (PrPC) is much less clear. It is intriguing that PrPc is expressed on most tissues in mammals, suggesting not only biological functions outside the CNS, but also a role other than the propagation of its misfolded isotype. In this review, we summarize accumulating in vitro and in vivo evidence regarding the physiological functions of PrPC in the nervous system, as well as in lymphoid organs.

AB - Stanley Prusiner was the first to promote the concept of misfolded proteins as a cause for neurological disease. It has since been shown by him and other investigators that the scrapie isoform of prion protein (PrPSc) functions as an infectious agent in numerous human and non-human disorders of the central nervous system (CNS). Interestingly, other organ systems appear to be less affected, and do not appear to lead to major co-morbidities. The physiological function of the endogenous cellular form of the prion protein (PrPC) is much less clear. It is intriguing that PrPc is expressed on most tissues in mammals, suggesting not only biological functions outside the CNS, but also a role other than the propagation of its misfolded isotype. In this review, we summarize accumulating in vitro and in vivo evidence regarding the physiological functions of PrPC in the nervous system, as well as in lymphoid organs.

KW - Adaptive immunity

KW - Aging

KW - Alzheimer disease

KW - Cognition

KW - Down syndrome

KW - Innate immunity

KW - Lymphocytes

KW - Neuroprotection

KW - PrP

KW - Primary progressive aphasia

KW - Prion protein

KW - Prnp

KW - Wilson disease

UR - http://www.scopus.com/inward/record.url?scp=36549072881&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36549072881&partnerID=8YFLogxK

U2 - 10.1016/j.jns.2007.06.019

DO - 10.1016/j.jns.2007.06.019

M3 - Review article

VL - 264

SP - 1

EP - 8

JO - Journal of the neurological sciences

JF - Journal of the neurological sciences

SN - 0022-510X

IS - 1-2

ER -

ID: 16784775