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Titolo:
IMMORTALIZED RAT PROXIMAL TUBULE CELLS PRODUCE MEMBRANE-BOUND AND SOLUBLE MEGALIN
Autore:
JUNG FF; BACHINSKY DR; TANG SS; ZHENG G; DIAMANT D; HAVERAN L; MCCLUSKEY RT; INGELFINGER JR;
Indirizzi:
MASSACHUSETTS GEN HOSP,PEDIAT RENAL RES LAB,BARTLETT HALL EXTENS 411 BOSTON MA 02114 MASSACHUSETTS GEN HOSP,PEDIAT RENAL RES LAB BOSTON MA 02114
Titolo Testata:
Kidney international
fascicolo: 2, volume: 53, anno: 1998,
pagine: 358 - 366
SICI:
0085-2538(1998)53:2<358:IRPTCP>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
DENSITY-LIPOPROTEIN-RECEPTOR; NEPHRITIS ANTIGENIC COMPLEX; PASSIVE HEYMANN NEPHRITIS; BRUSH-BORDER ANTIGENS; LDL-RECEPTOR; ALPHA-2-MACROGLOBULIN RECEPTOR; MEDIATES ENDOCYTOSIS; IN-VIVO; APOLIPOPROTEIN-J/CLUSTERIN; GLYCOPROTEIN 330/MEGALIN;
Keywords:
MEGALIN (GP330); RECEPTOR ASSOCIATED PROTEIN; IMMORTALIZED RAT PROXIMAL TUBULE CELLS; GLYCOPROTEIN RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
71
Recensione:
Indirizzi per estratti:
Citazione:
F.F. Jung et al., "IMMORTALIZED RAT PROXIMAL TUBULE CELLS PRODUCE MEMBRANE-BOUND AND SOLUBLE MEGALIN", Kidney international, 53(2), 1998, pp. 358-366

Abstract

Megalin (gp330), a glycoprotein receptor found on renal proximal tubule cells and several other epithelial cells, is deduced to be a type Iintegral membrane protein, but may also exist as a cell surface form lacking a cytoplasmic domain. Furthermore, soluble megalin products have been detected in urine, and in culture medium of a rat yolk sac carcinoma cell line, combined with receptor associated protein (RAP). Permanent renal cell lines expressing megalin were unavailable until the recent description of two immortalized rat proximal tubule cell lines (IRPTC). The present study demonstrated megalin on IRPTC surface by immunofluorescence, without surface staining for RAP, which was, however, readily detected within cells. Antibodies to ectodomain megalin epitopes immunoprecipitated megalin products both from cell lysates and culture medium, whereas antibodies to cytoplasmic domain epitopes precipitated megalin only from lysates. Western blots showed two major megalin products in medium, a prominent band al similar to 200 kDa, and a fainter band above 400 kDa, slightly below intact megalin in cell lysates. Anti-receptor associated protein antibodies immunoprecipitated megalin from IRPTC lysates, but not from media. We propose that portions of megalin are spontaneously produced by IRPTC, probably either by cleavage in the ectodomain or release of forms lacking a cytoplasmic domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 13:54:08