scholarly journals Distribution of a Major Lysosomal Membrane Glycoprotein, LGP85/LIMP II, in Rat Tissues.

2000 ◽  
Vol 23 (4) ◽  
pp. 394-396
Author(s):  
Norihiko TABUCHI ◽  
Kenji AKASAKI ◽  
Hiroshi TSUJI
Keyword(s):  
Lysosomal Membrane ◽  
Rat Tissues ◽  
Membrane Glycoprotein ◽  
Lysosomal Membrane Glycoprotein

scholarly journals Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles.

1988 ◽  
Vol 107 (6) ◽  
pp. 2491-2501 ◽  
Author(s):  
H J Geuze ◽  
W Stoorvogel ◽  
G J Strous ◽  
J W Slot ◽  
J E Bleekemolen ◽  
...  
Keyword(s):  
Lysosomal Membrane ◽  
Membrane Glycoprotein ◽  
Horse Radish Peroxidase ◽  
Western Blots ◽  
Lysosomal Membrane Proteins ◽  
Mannose 6 Phosphate ◽  
Lysosomal Membrane Glycoprotein ◽  
Endocytic Vesicles ◽  
Kinetics Of ◽  
Combined Data

The intracellular distributions of the cation-independent mannose 6-phosphate receptor (MPR) and a 120-kD lysosomal membrane glycoprotein (lgp120) were studied in rat hepatoma cells. Using quantitative immunogold cytochemistry we found 10% of the cell's MPR located at the cell surface. In contrast, lgp120 was not detectable at the plasma membrane. Intracellularly, MPR mainly occurred in the trans-Golgi reticulum (TGR) and endosomes. lgp120, on the other hand, was confined to endosomes and lysosomes. MPR was present in both endosomal tubules and vacuoles, whereas lgp120 was confined to the endosomal vacuoles. In cells incubated for 5-60 min with the endocytic tracer cationized ferritin, four categories of endocytic vacuoles could be discerned, i.e., vacuoles designated MPR+/lgp120-, MPR+/lgp120+, MPR-/lgp120+, and vacuoles nonimmunolabeled for MPR and lgp120. Tracer first reached MPR+/lgp120-, then MPR+/lgp120+, and finally MPR-/lgp120+ vacuoles, which are assumed to represent lysosomes. To study the kinetics of appearance of endocytic tracers in MPR-and/or lgp120-containing pools in greater detail, cells were allowed to endocytose horse-radish peroxidase (HRP) for 5-90 min. The reduction in detectability of MPR and lgp120 antigenicity on Western blots, due to treatment of cell homogenates with 3'3-diaminobenzidine, was followed in time. We found that HRP reached the entire accessible pool of MPR almost immediately after internalization of the tracer, while prolonged periods of time were required for HRP to maximally access lgp120. The combined data suggest that MPR+/lgp120+ vacuoles are endocytic vacuoles, intermediate between MPR+/lgp120-endosomes and MPR-/lgp120+ lysosomes, and represent the site where MPR is sorted from lgp120 destined for lysosomes. We propose that MPR is sorted from lgp120 by selective lateral distribution of the receptor into the tubules of this compartment, resulting in the retention of lgp120 in the vacuoles and the net transport of lgp120 to lysosomes.

Biochemical Analysis of the Movement of a Major Lysosomal Membrane Glycoprotein in the Endocytic Membrane System

1989 ◽  
Vol 106 (4) ◽  
pp. 717-722 ◽  
Author(s):  
Koji Furuno ◽  
Shinji Yano ◽  
Kenji Akasaki ◽  
Yoshitaka Tanaka ◽  
Yasunori Yamaguchi ◽  
...  
Keyword(s):  
Biochemical Analysis ◽  
Membrane System ◽  
Lysosomal Membrane ◽  
Membrane Glycoprotein ◽  
Lysosomal Membrane Glycoprotein

Molecular cloning of p67, a lysosomal membrane glycoprotein from Trypanosoma brucei

1999 ◽  
Vol 98 (1) ◽  
pp. 17-28 ◽  
Author(s):  
Robert J. Kelley ◽  
David L. Alexander ◽  
Chris Cowan ◽  
Andrew E. Balber ◽  
James D. Bangs
Keyword(s):  
Molecular Cloning ◽  
Trypanosoma Brucei ◽  
Lysosomal Membrane ◽  
Membrane Glycoprotein ◽  
Lysosomal Membrane Glycoprotein
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