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Titolo:
CHARACTERIZATION OF THE BETA(2)-MICROGLOBULIN ENDOCYTIC PATHWAY IN RAT PROXIMAL TUBULE CELLS
Autore:
SUNDIN DP; COHEN M; DAHL R; FALK S; MOLITORIS BA;
Indirizzi:
FESLER HALL RM 108,1120 S DR INDIANAPOLIS IN 46202 UNIV COLORADO,SCH MED,DEPT MED,DIV NEPHROL DENVER CO 00000 VET AFFAIRS MED CTR DENVER CO 00000 INDIANA UNIV,SCH MED,DEPT MED INDIANAPOLIS IN 00000 RICHARD L ROUDEBUSH VET AFFAIRS MED CTR INDIANAPOLIS IN 46202
Titolo Testata:
The American journal of physiology
fascicolo: 3, volume: 267, anno: 1994,
parte:, 2
pagine: 60000380 - 60000389
SICI:
0002-9513(1994)267:3<60000380:COTBEP>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-WEIGHT PROTEINS; BRUSH-BORDER MEMBRANES; AMINO-ACID SEQUENCE; BETA-2-MICROGLOBULIN; BINDING; KIDNEY; ANTIGENS; TURNOVER; POLARITY; GOLD;
Keywords:
LOW-MOLECULAR-WEIGHT PROTEIN UPTAKE; RECEPTOR ISOLATION; BETA(2)-MICROGLOBULIN MODIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
D.P. Sundin et al., "CHARACTERIZATION OF THE BETA(2)-MICROGLOBULIN ENDOCYTIC PATHWAY IN RAT PROXIMAL TUBULE CELLS", The American journal of physiology, 267(3), 1994, pp. 60000380-60000389

Abstract

The uptake mechanism(s) of low-molecular-weight proteins by proximal tubule cells remains incompletely characterized. We utilized a biochemical and semiquantitative morphological approach to better characterize the endocytic pathway of an anionic protein, beta(2)-microglobulin (beta(2)M), in the rat proximal tubule. Indirect immunogold techniques revealed beta(2)M was taken up via a classic receptor-mediated endocytic pathway. In vitro biochemical and morphological characterization ofiodinated beta(2)M and gold-conjugated beta(2)M (gold-beta(2)M) binding to isolated brush-border membrane vesicles (BBMV) documented specific and quantitatively similar binding interactions of the modified beta(2)M with BBMV. Kinetic characterization of the in vivo endocytic pathway of gold-beta(2)M was undertaken using microinfusion of individualtubules. beta(2)M initially bound at the apical surface, was internalized into subapical coated vesicles and delivered to endosomal-like structures within 5 min, and, finally, was concentrated in lysosomal-like structures within 15 min. This uptake was inhibited by excess unconjugated beta(2)M In addition, we directly showed that uptake did not occur across the basolateral surface. Finally, by passing solubilized BBMV over beta(2)M affinity columns we were able to isolate binding activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 14:48:49