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Titolo:
Identification of low density lipoprotein receptor-related protein-2/megalin as an endocytic receptor for seminal vesicle secretory protein II
Autore:
Ranganathan, S; Knaak, C; Morales, CR; Argraves, WS;
Indirizzi:
Med Univ S Carolina, Dept Cell Biol & Anat, Charleston, SC 29425 USA Med Univ S Carolina Charleston SC USA 29425 nat, Charleston, SC 29425 USA McGill Univ, Dept Anat & Cell Biol, Montreal, PQ H3A 2B2, Canada McGill Univ Montreal PQ Canada H3A 2B2 Biol, Montreal, PQ H3A 2B2, Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 9, volume: 274, anno: 1999,
pagine: 5557 - 5563
SICI:
0021-9258(19990226)274:9<5557:IOLDLR>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROSTATE SPECIFIC ANTIGEN; RAT EPIDIDYMAL FLUID; ALPHA-2-MACROGLOBULIN RECEPTOR; ALPHA(2)-MACROGLOBULIN RECEPTOR; APOLIPOPROTEIN-J/CLUSTERIN; MEDIATES ENDOCYTOSIS; ORGAN DISTRIBUTION; GENE FAMILY; 2 MEMBERS; SVS-II;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Argraves, WS Med29425 S Carolina, Dept Cell Biol & Anat, 171 Ashley Ave, Charleston, SC Med Univ S Carolina 171 Ashley Ave Charleston SC USA 29425 SC
Citazione:
S. Ranganathan et al., "Identification of low density lipoprotein receptor-related protein-2/megalin as an endocytic receptor for seminal vesicle secretory protein II", J BIOL CHEM, 274(9), 1999, pp. 5557-5563

Abstract

The low density lipoprotein receptor-related protein-2/megalin (LRP-2) is an endocytic receptor that is expressed on the apical surfaces of epithelial cells lining specific regions of the male and female reproductive tracts. In the present study, immunohistochemical staining revealed that LRP-2 is also expressed by epithelial cells lining the ductal region and the ampullaof the rat seminal vesicle. To identify LRP-2 ligands in the seminal vesicle, we probed seminal vesicle fluid with I-125-labeled LRP-2 in a gel-blot overlay assay. A 100-kDa protein (under non-reducing conditions) was found to bind the radiolabeled receptor. The protein was isolated and subjected to protease digestion, and the proteolytic fragments were subjected to mass spectroscopic sequence analysis. As a result, the 100-kDa protein was identified as the seminal vesicle secretory protein II (SVS-II), a major constituent of the seminal coagulum. Using purified preparations of SVS-II and LRP-2, solid-phase binding assays were used to show that the SVS-II bound to the receptor with high affinity (K-d = 5.6 nM). The binding of SVS-II to LRP-2 was inhibited using a known antagonist of LRP-2 function, the 39-kDa receptor-associated protein RAP. Using a series of recombinant subfragments ofSVS-II, the LRP-2 binding site was mapped to a stretch of repeated 13-residue modules located in the central portion of the SVS-II polypeptide. To evaluate the ability of LRP-2 to mediate I-125-SVS-II endocytosis and lysosomal degradation, ligand clearance assays were performed using differentiatedmouse F9 cells, which express high levels of LRP-2, Radiolabeled SVS-II was internalized and degraded by the cells, and both processes were inhibitedby antibodies to LRP-2 or by RAP. The results indicate that LRP-2 binds SVS-II and can mediate its endocytosis leading to lysosomal degradation.

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Documento generato il 29/09/20 alle ore 23:46:28