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Verfasst von:Marie-Cardine, Anne [VerfasserIn]   i
 Kirchgessner, Henning [VerfasserIn]   i
 Schraven, Burkhart [VerfasserIn]   i
Titel:Molecular alterations of the Fyn-complex occur as late events of human T cell activation
Verf.angabe:Anne Marie‐Cardine, Henning Kirchgessner and Burkhart Schraven
Jahr:1999
Umfang:13 S.
Teil:volume:29
 year:1999
 number:4
 pages:1175-1187
 extent:13
Fussnoten:First published: 28 March 2006 ; Gesehen am 08.03.2021
Titel Quelle:Enthalten in: European journal of immunology
Ort Quelle:Weinheim : Wiley-VCH, 1971
Jahr Quelle:1999
Band/Heft Quelle:29(1999), 4, Seite 1175-1187
ISSN Quelle:1521-4141
Abstract:Two-dimensional gel electrophoresis of anti-p59fyn immunoprecipitates obtained from non-transformed resting human T lymphocytes resulted in the identification of an oligomeric protein complex which is constitutively formed between Fyn and several additional phosphoproteins (pp43, pp72, pp85, the protein tyrosine kinase Pyk2, as well as the two recently cloned adaptor proteins, SKAP55 and SLAP-130). With the exception of pp85, these proteins seem to preferentially interact with Fyn since they are not detectable in Lck immunoprecipitates prepared under the same experimental conditions. Among the individual members of the Fyn-complex pp85, SKAP55 and pp43 are constitutively phosphorylated on tyrosine residue(s) in vivo and likely interact with Fyn via its src homology 2 (SH2)-domain. In contrast to non-transformed T lymphocytes, continuously proliferating transformed human T cell lines express an altered Fyn-complex. Thus, despite normal expression and tyrosine phosphorylation, SKAP55 does not associate with Fyn in Jurkat cells and in other human T cell lines. Instead two novel proteins interact with Fyn among which one has previously been identified as α-tubulin. Importantly, almost identical alterations of the Fyn-complex as observed in Jurkat cells are induced in non-transformed T lymphocytes following mitogenic stimulation. These data suggest that Fyn and its associated proteins could be involved in the control of human T cell proliferation. Moreover, the analogous constitutive alterations in transformed T cell lines could indicate that deregulation of the Fyn-complex might be functionally associated with the malignant phenotype of these cells.
DOI:doi:10.1002/(SICI)1521-4141(199904)29:04<1175::AID-IMMU1175>3.0.CO;2-Z
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 ; Verlag: https://dx.doi.org/https://doi.org/10.1002/(SICI)1521-4141(199904)29:04<1175::AID-IMMU1175>3.0.CO;2-Z
 Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/%28SICI%291521-4141%28199904%2929%3A04%3C1175%3A%3AAID-IMMU1175%3E3.0.CO ...
 DOI: https://doi.org/10.1002/(SICI)1521-4141(199904)29:04<1175::AID-IMMU1175>3.0.CO;2-Z
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Protein kinase
 Signal transduction
 T lymphocyte
K10plus-PPN:1750736020
Verknüpfungen:→ Zeitschrift

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