Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate.

Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate. Research Abstract Details 

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Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate. Abstract Text:

Nancy Pham,Shaoman Yin,Shuiliang Yu,Poki Wong,Shin-Chung Kang,Chaoyang Li,Man-Sun Sy,

The human prion gene, PRNP, has two allelic forms that encode either a methionine or valine at codon 129. This polymorphism strongly influences the pathogenesis of prion disease. However, the underlying mechanism remains unclear. We compared the conformation between wild-type human prion protein (rPrP(C)) with either a valine or methionine at position 129, using a panel of monoclonal antibodies that are specific for epitopes along the entire protein. We found that rPrP(C(129M)) has a more exposed helix 1 region compared to rPrP(C(129V)). Helix 1 is important in the aggregation process. Accordingly, rPrP(C(129M)) aggregates at a faster rate and forms more aggregate than rPrP(C(129V)). In addition, by using a rPrP with a pathogenic mutation of five additional octapeptide repeat insertions, rPrP((129M)/10OR), as "seeds", we showed that rPrP((129M)/10OR) promotes the aggregation of rPrP(C(129M)) more efficiently than rPrP(C(129V)). These findings provide a possible mechanism underlying the influence of residue 129 on human prion disease.

Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate. Publishing Authors By Initials

N Pham,S Yin,S Yu,P Wong,SC Kang,C Li,MS Sy,

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Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biochemical and biophysical research communication

VOLUME: 368

Page Numbers: 875-81

Journal Abbreviation: Biochem. Biophys. Res. Commun.

ISSN: 1090-2104

DAY: 12

MONTH: 02

YEAR: 2008

Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate. Information

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LANGUAGE: eng

NlmUniqueID: 372516

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Grant and Affiliation Information for Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate.

AFFILIATION: Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland Clinic Research Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA.

Country: United States

AGENCY: United States NINDS

GRANT: NS-045981-01

ACRONYM: NS

MEDLINETA: Biochem Biophys Res Commun

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