Stimulation of cellular sphingomyelin import by the chemokine connective tissue-activating peptide III.

Details

Serval ID
serval:BIB_CD68EE918605
Type
Article: article from journal or magazin.
Collection
Publications
Title
Stimulation of cellular sphingomyelin import by the chemokine connective tissue-activating peptide III.
Journal
Journal of Biological Chemistry
Author(s)
Stoeckelhuber M., Dobner P., Baumgartner P., Ehlert J., Brandt E., Mentele R., Adam D., Engelmann B.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Publication state
Published
Issued date
2000
Volume
275
Number
48
Pages
37365-37372
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: ppublish
Abstract
The selective import of phospholipids into cells could be mediated by proteins secreted from the cells into the extracellular compartment. We observed that the supernatants obtained from suspensions of thrombin-activated platelets stimulated the exchange of pyrene (py)-labeled sphingomyelin between lipid vesicles in vitro. The proteins with sphingomyelin transfer activity were purified and identified as the chemokine connective tissue-activating peptide III (CTAP-III) and platelet basic protein. Isolated CTAP-III stimulated the exchange of py-sphingomyelin between lipid vesicles but did not affect the translocations of py-labeled phosphatidylcholine and phosphatidylethanolamine. CTAP-III rapidly increased the transfer of py-sphingomyelin from low density lipoproteins into peripheral blood lymphocytes, other immune cells, and fibroblasts. In the presence of heparin, CTAP-III was unable to insert sphingomyelin into the peripheral blood lymphocytes. The activation energy of the py-sphingomyelin transfer suggested that the translocation proceeded entirely in a hydrophobic environment. [(3)H]Sphingomyelin transferred to the cells by CTAP-III was hydrolyzed to [(3)H]ceramide and [(3)H]sphingosine after activation with tumor necrosis factor alpha. The generation of the [(3)H]sphingolipid messengers was catalyzed by acid sphingomyelinase. Our results identify CTAP-III as the first mediator of the selective (endocytosis-independent) cellular import of sphingomyelin allowing the paracrine modulation of the sphingolipid signaling.
Keywords
Biological Transport, Blood Coagulation Factors/pharmacology, Blood Platelets/drug effects, Blood Platelets/metabolism, Humans, Peptides, Sphingomyelins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
24/05/2013 16:00
Last modification date
01/04/2020 12:07
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