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Titolo:
Stimulation of cellular sphingomyelin import by the chemokine connective tissue-activating peptide III
Autore:
Stoeckelhuber, M; Dobner, P; Baumgartner, P; Ehlert, J; Brandt, E; Mentele, R; Adam, D; Engelmann, B;
Indirizzi:
Univ Munich, Inst Physiol, D-80336 Munich, Germany Univ Munich Munich Germany D-80336 Inst Physiol, D-80336 Munich, Germany Forschungszentrum, Abt Immunol & Zellbiol, D-23845 Borstel, Germany Forschungszentrum Borstel Germany D-23845 biol, D-23845 Borstel, Germany Univ Munich, Chirurg Klin, Abt Klin Chem & Biochem, D-80336 Munich, Germany Univ Munich Munich Germany D-80336 em & Biochem, D-80336 Munich, Germany Univ Kiel, Inst Immunol, D-24105 Kiel, Germany Univ Kiel Kiel Germany D-24105 Kiel, Inst Immunol, D-24105 Kiel, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 48, volume: 275, anno: 2000,
pagine: 37365 - 37372
SICI:
0021-9258(200012)275:48<37365:SOCSIB>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET BASIC-PROTEIN; LIPID TRANSFER PROTEINS; NECROSIS-FACTOR-ALPHA; NEUTRAL SPHINGOMYELINASE; BETA-THROMBOGLOBULIN; CRYSTAL-STRUCTURE; HUMAN-NEUTROPHILS; PLASMA-MEMBRANE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLINOSITOL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Engelmann, B Univ Munich, Inst Physiol, Schillerstr 44, D-80336 Munich, Germany Univ Munich Schillerstr 44 Munich Germany D-80336 h, Germany
Citazione:
M. Stoeckelhuber et al., "Stimulation of cellular sphingomyelin import by the chemokine connective tissue-activating peptide III", J BIOL CHEM, 275(48), 2000, pp. 37365-37372

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 immunecells, and fibroblasts, In the presence of heparin, CTAP-III was unable toinsert sphingomyelin into the peripheral blood lymphocytes. The activationenergy of the py sphingomyelin transfer suggested that the translocation proceeded entirely in a hydrophobic environment, [H-3]Sphingomyelin transferred to the cells by CTAP-III was hydrolyzed to [H-3]ceramide and [H-3]sphingosine after activation with tumor necrosis factor a. The generation of the[H-3]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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 15:03:06