Document Detail

Analysis of post-lysosomal compartments.
MedLine Citation:
PMID:  14733906     Owner:  NLM     Status:  MEDLINE    
Lysosomes are acidic intracellular compartments and are regarded as degradative and the end point, of the endocytic pathway. Here we provide evidence for the generation of acid hydrolase poor and non-acidic post-lysosomal compartments in NRK cells that have accumulated non-digestible macromolecules, Texas red-dextran (TR-Dex), within lysosomes. When TR-Dex was fed to the cells for 6h, most of the internalized TR-Dex colocalized with a lysosomal enzyme, cathepsin D. With an increase in the chase period, however, the internalized TR-Dex gradually accumulated in cathepsin D-negative vesicles. These vesicles were positive for a lysosomal membrane protein, LGP85, and their formation was inhibited by treatment of the cells with U18666A, which impairs membrane transport out of late endosomal/lysosomal compartments, thereby suggesting that the vesicles are derived from lysosomes. Interestingly, these compartments are non-acidic as judged for the DAMP staining. The results, therefore, suggest that the excess accumulation of non-digestible macromolecules within lysosomes induces the formation of acid hydrolase poor and non-acidic post-lysosomal compartments. The fact that treatment of the cells with lysosomotropic amines or a microtubule-depolymerization agent resulted in extensive colocalization of TR-Dex with cathepsin D further indicates that the formation of the post-lysosomal compartments depends on the lysosomal acidification and microtubule organization. Furthermore, these results suggest bi-directional membrane transport between lysosomes and the post-lysosomal compartments, which implies that the latter are not resting compartments.
Yuko Hirota; Naoko Masuyama; Toshio Kuronita; Hideaki Fujita; Masaru Himeno; Yoshitaka Tanaka
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  314     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2004 Feb 
Date Detail:
Created Date:  2004-01-21     Completed Date:  2004-03-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  306-12     Citation Subset:  IM    
Division of Pharmaceutical Cell Biology, Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, 812-8582 Fukuoka, Japan.
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MeSH Terms
Androstenes / pharmacology
Antigens, CD36 / biosynthesis
Cathepsin D / biosynthesis,  chemistry
Dextrans / chemistry
Endosomes / metabolism
Enzyme Inhibitors / pharmacology
Fluorescent Dyes / pharmacology
Hydrogen-Ion Concentration
Hydrolases / metabolism
Lysosomal Storage Diseases / metabolism
Lysosome-Associated Membrane Glycoproteins
Lysosomes / metabolism*,  physiology
Membrane Glycoproteins*
Microscopy, Fluorescence
Microtubules / metabolism
Time Factors
Xanthenes / pharmacology
Reg. No./Substance:
0/Androstenes; 0/Antigens, CD36; 0/Enzyme Inhibitors; 0/Fluorescent Dyes; 0/Lysosome-Associated Membrane Glycoproteins; 0/Membrane Glycoproteins; 0/Xanthenes; 139638-11-2/Cd36l2 protein, rat; 3039-71-2/3-beta-(2-(diethylamino)ethoxy)androst-5-en-17-one; 82354-19-6/Texas red; 9004-54-0/Dextrans; EC 3.-/Hydrolases; EC D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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