Human cellular prion protein hPrPC is sorted to the apical membrane of epithelial cells

被引：11

作者：

De Keukeleire, B.

Donadio, S.

Micoud, J.

Lechardeur, D.

Benharouga, M.

机构：

[1] Univ Grenoble 1, CEA, CNRS,UMR 5249,Lab Chim & Biol Metaux, Inst Rech Technol & Sci Vivant, F-38054 Grenoble 9, France

[2] INRA, Ctr Rech Jouy En Josas, UBLO, F-78352 Jouy En Josas, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 354卷 / 04期

关键词：

epithelial cells; apical membrane sorting; human PrPC; PrPSc;

D O I：

10.1016/j.bbrc.2007.01.096

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Propagation of the scrapie isoform of the prion protein (PrPSc) depends on the expression of endogenous cellular prion (PrPC). During oral infection, PrPSc propagates, by conversion of the PrPC to PrPSc, from the gastrointestinal tract to the nervous system. Intestinal epithelium could serve as the primary site for PrPC conversion. To investigate PrPC sorting in epithelia cells, we have generated both a green fluorescent protein (EGFP) or hernagglutinin (HA) tagged human PrPC (hPrP(C)). Combined molecular, biochemical, and single living polarized cell imaging characterizations suggest that hPrP(C) is selectively targeted to the apical side of Madin-Darby canine kidney (MDCKII) and of intestinal epithelia (Caco2) cells. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：949 / 954

页数：6

共 25 条

[1] COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments [J].

Benharouga, M ;

Haardt, M ;

Kartner, N ;

Lukacs, GL .

JOURNAL OF CELL BIOLOGY, 2001, 153 (05) :957-970

[2] Sorting proteins to their target membranes [J].

Brown, D ;

Breton, S .

KIDNEY INTERNATIONAL, 2000, 57 (03) :816-824

[3] Prion protein glycosylation is sensitive to redox change [J].

Capellari, S ;

Zaidi, SIA ;

Urig, CB ;

Perry, G ;

Smith, MA ;

Petersen, RB .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (49) :34846-34850

[4]

CITI S, 1998, BIOCHIM BIOPHYS ACTA, V144, P1

[5] NMR structure of the bovine prion protein [J].

Garcia, FL ;

Zahn, R ;

Riek, R ;

Wüthrich, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (15) :8334-8339

[6] Cellular isoform of the prion protein PrPc in human intestinal cell lines:: Genetic polymorphism at codon 129, mRNA quantification and protein detection in lipid rafts [J].

Garmy, Nicolas ;

Guo, Xiao-Jun ;

Taieb, Nadira ;

Tourres, Christian ;

Tamalet, Catherine ;

Fantini, Jacques ;

Yahi, Nouara .

CELL BIOLOGY INTERNATIONAL, 2006, 30 (06) :559-567

[7] Cellular biology of prion diseases [J].

Harris, DA .

CLINICAL MICROBIOLOGY REVIEWS, 1999, 12 (03) :429-+

[8] Transepithelial prion transport by M cells [J].

Heppner, FL ;

Christ, AD ;

Klein, MA ;

Prinz, M ;

Fried, M ;

Kraehenbuhl, JP ;

Aguzzi, A .

NATURE MEDICINE, 2001, 7 (09) :976-977

[9] Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state [J].

Horiuchi, M ;

Caughey, B .

EMBO JOURNAL, 1999, 18 (12) :3193-3203

[10] MOLECULAR-CLONING OF A HUMAN PRION PROTEIN CDNA [J].

KRETZSCHMAR, HA ;

STOWRING, LE ;

WESTAWAY, D ;

STUBBLEBINE, WH ;

PRUSINER, SB ;

DEARMOND, SJ .

DNA-A JOURNAL OF MOLECULAR & CELLULAR BIOLOGY, 1986, 5 (04) :315-324

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