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Verfasst von:Koopmann, Jens [VerfasserIn]   i
 Post, Markus [VerfasserIn]   i
 Neefjes, Jacques J. [VerfasserIn]   i
 Hämmerling, Günter J. [VerfasserIn]   i
 Momburg, Frank [VerfasserIn]   i
Titel:Translocation of long peptides by transporters associated with antigen processing (TAP)
Verf.angabe:Jens-Oliver Koopmann, Markus Post, Jacques J. Neefjes, Günter J. Hämmerling, Frank Momburg
Jahr:1996
Umfang:9 S.
Fussnoten:Elektronische Reproduktion der Druck-Ausgabe 17. November 2005 ; Gesehen am 17.07.2025
Titel Quelle:Enthalten in: European journal of immunology
Ort Quelle:Weinheim : Wiley-VCH, 1971
Jahr Quelle:1996
Band/Heft Quelle:26(1996), 8, Seite 1720-1728
ISSN Quelle:1521-4141
Abstract:The major histocompatibility complex (MHC)-encoded transporters associated with antigen processing (TAP) translocate peptides from the cytosol into the lumen of the endoplasmic reticulum (ER) where they associate with MHC class I molecules. The length of class I-binding peptides is usually 8-11 amino acids, but examples of significantly longer peptides have been described. The preferred lengths and upper and lower size limits for peptides translocated by TAP have not been determined in detail because in the currently used test systems, peptides are subject to proteolytic degradation. In the present study, three sets of individual peptides or partially randomized peptide libraries ranging between 6 and 40 residues were used that contained a radiolabeled tyrosine and a consensus sequence for ER-specific N-glycosylation at opposite ends, thus ensuring that only nondegraded peptides were monitored in the transport/glycosylation assay. For three different transporters, rat TAP1/2a, rat TAP1/2u and hTAP, the most efficient ATP-dependent transport was observed for peptides with 8-12 amino acids. Hexamers and longer peptides of up to 40 amino acids were also translocated, albeit less efficiently. For two of the three sets of peptides analyzed, rat TAP1/2a showed a less stringent length selection than rat TAP1/2u and human TAP. The superior transport of the decamer of the TNKT. Y series was not due to faster degradation or less efficient glycosylation of shorter or longer length variants. A binding assay with TAP-containing microsomes revealed a high affinity for the radiolabeled decamer (KD = 580 nM), while other length variants were clearly inferior in their binding affinities. Thus, TAP binds and preferentially translocates peptides with a length suitable for binding to MHC class I molecules, but peptides that are considerably longer may also be substrates. About 105 peptide binding sites per cell equivalent of microsomes were determined, providing an estimate for the number of TAP complexes in the ER membrane.
DOI:doi:10.1002/eji.1830260809
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1002/eji.1830260809
 Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/eji.1830260809
 DOI: https://doi.org/10.1002/eji.1830260809
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Antigen processing
 Major histocompatibility complex
 Peptide
 TAP
 Transporter
K10plus-PPN:1931013365
Verknüpfungen:→ Zeitschrift

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