Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X).

Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Research Abstract Details 

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Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Abstract Text:

Chaoyang Li,Poki Wong,Tao Pan,Fan Xiao,Shaoman Yin,Binggong Chang,Shin-Chung Kang,James Ironside,Man-Sun Sy,

The normal PrP(C) (cellular prion protein) contains sLe(X) [sialyl-Le(X) (Lewis X)] and Le(X). sLe(X) is a ligand of selectins. To examine whether PrP(C) is a ligand of selectins, we generated three human PrP(C)-Ig fusion proteins: one with Le(X), one with sLe(X), and the other with neither Le(X) nor sLe(X). Only Le(X)-PrP(C)-Ig binds E-, L- and P-selectins. Binding is Ca(2+)-dependent and occurs with nanomolar affinity. Removal of sialic acid on sLe(X)-PrP(C)-Ig enables the fusion protein to bind all selectins. These findings were confirmed with brain-derived PrP(C). The selectins precipitated PrP(C) in human brain in a Ca(2+)-dependent manner. Treatment of brain homogenates with neuraminidase increased the amounts of PrP(C) precipitated. Therefore the presence of sialic acid prevents the binding of PrP(C) in human brain to selectins. Hence, human brain PrP(C) interacts with selectins in a manner that is distinct from interactions in peripheral tissues. Alternations in these interactions may have pathological consequences.

Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Publishing Authors By Initials

C Li,P Wong,T Pan,F Xiao,S Yin,B Chang,SC Kang,J Ironside,MS Sy,

For similar membrane glycoproteins: cell adhesion molecules: selectins research abstracts see: membrane glycoproteins: cell adhesion molecules: selectins research

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Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Journal Published:

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

Journal: The Biochemical journal

VOLUME: 406

Page Numbers: 333-41

Journal Abbreviation: Biochem. J.

ISSN: 1470-8728

DAY: 1

MONTH: Sep

YEAR: 2007

Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2984726

Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Keywords Mesh Terms:

KEYWORDS: Selectins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X). Information

Substance Name: Neuraminidase

Registry Number: EC 3.2.1.18

Grant and Affiliation Information for Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X).

AFFILIATION: Institute of Pathology, School of Medicine, Case Western Reserve University, Cleveland, OH 44107-1712, U.S.A.

Country: England

AGENCY: United States NINDS

GRANT: NS-045981-02

ACRONYM: NS

MEDLINETA: Biochem J

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