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  Influence of 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE) on the localization of cathepsin B and cathepsin L in human lung tumor cells

Ulbricht, B., Henny, H., Horstmann, H., Spring, H., Faigle, W., & Spiess, E. (1997). Influence of 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE) on the localization of cathepsin B and cathepsin L in human lung tumor cells. European Journal of Cell Biology: EJCB, 74(3), 294-301.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-BC49-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-1E5D-2
Genre: Journal Article
Alternative Title : Influence of 12(S)-HETE on the localization of cathepsin B and cathepsin L in human lung tumor cells

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EurJCellBiol_74_1997_294.pdf (Any fulltext), 24MB
 
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 Creators:
Ulbricht, Bettina1, Author              
Henny, Heike, Author
Horstmann, Heinz1, 2, Author              
Spring, Herbert, Author
Faigle, Wolfgang, Author
Spiess, Eberhard, Author
Affiliations:
1Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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Free keywords: 12 Hydroxy 5,8,10,14 eicosatetraenoic Acid pharmacology : Cathepsin B metabolism : Cathepsins metabolism
 Abstract: Cathepsins B and L are catabolic lysosomal enzymes but are likely candidates for extracellular proteolysis in normal and malignant processes. The signal mediator 12(S)-HETE selectively triggers a shot-gun release of cathepsin B. We have therefore investigated the intracellular distribution of cathepsins in unstimulated and 12(S)-HETE-stimulated tumor cells. Cathepsins B and L have only limited colocalization, which is found in the regions of synthesis and sorting (endoplasmic reticulum, Golgi, trans Golgi network). Treatment by 12(S)-HETE scatters cathepsin B but not cathepsin L and proform of cathepsin B. Colocalization with both mannose 6-phosphate receptors is very limited for both cathepsins. But extensive colocalization of cathepsin B and the endosomal/lysosomal marker CD63 (LIMP-I) documents the main fraction of the enzyme in these compartments. The supposed non-lysosomal fraction of cathepsin B is very likely the secretable material which follows a regulated secretory pathway. Storage and regulated secretion in tumor cells support extracellular proteolysis as a means in invasion which may lead to metastasis. But the mechanisms by which cells might acquire and eventually apply this means is still unknown

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Language(s): eng - English
 Dates: 1997-11
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664992
Other: 7118
 Degree: -

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Title: European Journal of Cell Biology : EJCB
  Other : Eur. J. Cell Biol.
Source Genre: Journal
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Publ. Info: Stuttgart : Wissenschaftliche Verlagsgesellschaft.
Pages: - Volume / Issue: 74 (3) Sequence Number: - Start / End Page: 294 - 301 Identifier: ISSN: 0070-2463
CoNE: https://pure.mpg.de/cone/journals/resource/954925486755