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Titolo:
HEAVY-CHAIN DIMERS AS WELL AS COMPLETE ANTIBODIES ARE EFFICIENTLY FORMED AND SECRETED FROM DROSOPHILA VIA A BIP-MEDIATED PATHWAY
Autore:
KIRKPATRICK RB; GANGULY S; ANGELICHIO M; GRIEGO S; SHATZMAN A; SILVERMAN C; ROSENBERG M;
Indirizzi:
SMITHKLINE BEECHAM PHARMACEUT,DEPT GENE EXPRESS SCI,709 SWEDELAND RD KING OF PRUSSIA PA 19406 SMITHKLINE BEECHAM PHARMACEUT,DEPT PROT BIOCHEM KING OF PRUSSIA PA 19406 SMITHKLINE BEECHAM PHARMACEUT,DEPT MOLEC VIROL & HOST DEF KING OF PRUSSIA PA 19406
Titolo Testata:
The Journal of biological chemistry
fascicolo: 34, volume: 270, anno: 1995,
pagine: 19800 - 19805
SICI:
0021-9258(1995)270:34<19800:HDAWAC>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION MOLECULE; LUMINAL ER PROTEINS; BINDING-PROTEIN; IMMUNOGLOBULIN SUPERFAMILY; GENE; EXPRESSION; MELANOGASTER; COMPARTMENT; ENCODES; MEMBER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
R.B. Kirkpatrick et al., "HEAVY-CHAIN DIMERS AS WELL AS COMPLETE ANTIBODIES ARE EFFICIENTLY FORMED AND SECRETED FROM DROSOPHILA VIA A BIP-MEDIATED PATHWAY", The Journal of biological chemistry, 270(34), 1995, pp. 19800-19805

Abstract

We have constructed a stable Drosophila cell line coexpressing heavy chain (HC) and Light chain (LC) immunoglobulins of a humanized monoclonal antibody (mAb) that recognizes the F antigen of respiratory syncytial virus Tempest, P. R, Bremmer, P., Lambert, M., Taylor, G., Furze, J. M, Carr, F. J., and Harris, W. J. (1991) Bio/Technology 9, 266-271. These cells efficiently secrete antibody with substrate binding activity indistinguishable from that produced from vertebrate cell lines. Significantly, the Drosophila homologue of the immunoglobulin binding chaperone protein (BiP), hsc72, was found to interact specifically withthe immunoglobulin HC in an ATP-dependent fashion, similar to the BiP-HC interaction known to occur in vertebrate cells. This is, in fact, the first substrate ever shown to interact specifically with Drosophila hsc72. Most surprisingly, expression of heavy chains in the absence of LC led to the efficient secretion of heavy chain dimers. Moreover, this secretion occurred in association with hsc72. This dramatically contrasts with what is seen in vertebrate cells where in the absence ofLC, HC remains sequestered inside the cell in stable association withBiP. Our results clearly suggest that Drosophila Hip can substitute for its mammalian counterpart and chaperone the secretion of active IgG. However, the finding that Drosophila Hip can also uniquely chaperoneheavy chain dimers indicates mechanistic differences that may relate to the evolved need for retaining immature IgGs in vertebrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/08/20 alle ore 17:02:52