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Titolo:
CYTOTOXICITY OF KDEL-TERMINATED RICIN TOXINS CORRELATES WITH DISTRIBUTION OF THE KDEL RECEPTOR IN THE GOLGI
Autore:
TAGGE E; CHANDLER J; TANG BL; HONG WJ; WILLINGHAM MC; FRANKEL A;
Indirizzi:
MED UNIV S CAROLINA,DEPT MED,HOLLINGS CANC CTR,ROOM 306,171 ASHLEY AVE CHARLESTON SC 29425 MED UNIV S CAROLINA,DEPT MED,HOLLINGS CANC CTR CHARLESTON SC 29425 MED UNIV S CAROLINA,DEPT SURG CHARLESTON SC 29425 MED UNIV S CAROLINA,DEPT PATHOL CHARLESTON SC 29425 NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 0511 SINGAPORE
Titolo Testata:
The Journal of histochemistry and cytochemistry
fascicolo: 2, volume: 44, anno: 1996,
pagine: 159 - 165
SICI:
0022-1554(1996)44:2<159:COKRTC>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
A-CHAIN; ENDOPLASMIC-RETICULUM; ESCHERICHIA-COLI; CELLS; EXPRESSION; RIBOSOMES; INCREASES; SEQUENCE; BINDING; SIGNAL;
Keywords:
RICIN; KDEL RECEPTOR; CYTOTOXICITY; GOLGI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
E. Tagge et al., "CYTOTOXICITY OF KDEL-TERMINATED RICIN TOXINS CORRELATES WITH DISTRIBUTION OF THE KDEL RECEPTOR IN THE GOLGI", The Journal of histochemistry and cytochemistry, 44(2), 1996, pp. 159-165

Abstract

DNAs encoding ricin toxin A chain (RTA), with or without a C-terminalendoplasmic reticulum retention signal KDEL, were subcloned into pGEX2T bacterial expression plasmid. After transformation of JM105 E. colicells and induction with isopropylthio-beta-galactoside (IPTG), fusion proteins were bound to an immobilized glutathione matrix and recombinant ricin A chains released with thrombin. Both recombinant wild-typeRTA and RTA with KDEL had immunological reactivity and catalytic activity indistinguishable from plant RTA. The bacterial RTA products reassociated with plant ricin B chain (RTB) similarly to plant RTA. Cell cytotoxicities were measured on seven cell lines for each A-chain and heterodimer. Although KDEL sequences enhanced cytotoxicity in most cases, significant variability was observed. In each case, addition of KDEL enhanced A-chain cytotoxicity more than holotoxin cytotoxicity. Three cell lines showed reduced KDEL enhancement of both RTA and ricin cytotoxicity. The concentration of KDEL receptor was examined on each cell line by immunofluorescence microscopy with an antireceptor monoclonal antibody. Differences in sensitivity to KDEL-containing toxins correlated with altered distribution of KDEL receptor between endoplasmic reticulum (ER) and Golgi compartments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/10/20 alle ore 01:45:37