p59fyn tyrosine kinase regulates p56lck tyrosine kinase activity and early TCR-mediated signaling

Sang kyou Lee; Andrey Shaw; Stephen E. Maher; Alfred L.M. Bothwell

doi:10.1093/intimm/6.10.1621

p59^fyn tyrosine kinase regulates p56^lck tyrosine kinase activity and early TCR-mediated signaling

Sang kyou Lee, Andrey Shaw, Stephen E. Maher, Alfred L.M. Bothwell

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

To study the role of p59^fyn in T cell activation, we used antisense RNA to inhibit p59^fyn expression in a T cell clone. Transfectants with reduced levels of p59^fyn were functionally impaired in their responses to antigen, Con A + recombinant IL-1 and cross-linking with anti-TCR mAb. Induction of tyrosine phosphorylation on most intracellular substrates was greatly reduced. We also noted that the Ick kinase activity was greatly reduced even though the amount of Ick protein was equivalent to that present in parental D10 cells. Our results suggest that the protein tyrosine kinase p59^fyn is critical in TCR-mediated signaling and also suggests that p59^fyn may regulate p56^fyn tyrosine kinase activity.

Original language	English
Pages (from-to)	1621-1627
Number of pages	7
Journal	International Immunology
Volume	6
Issue number	10
DOIs	https://doi.org/10.1093/intimm/6.10.1621
Publication status	Published - 1994 Oct

Bibliographical note

Funding Information:
WB thank K. Arai for the gift of the pNeoSRctll plasmid. Rabbit polyclonal antibodies specific to the 059**" protein were kindly provided by J. Bolen. This work was supported by NIH grant GM40924

All Science Journal Classification (ASJC) codes

Immunology and Allergy
Immunology

Access to Document

10.1093/intimm/6.10.1621

Cite this

@article{275361d485484089a7a060f0aeb94532,

title = "p59fyn tyrosine kinase regulates p56lck tyrosine kinase activity and early TCR-mediated signaling",

abstract = "To study the role of p59fyn in T cell activation, we used antisense RNA to inhibit p59fyn expression in a T cell clone. Transfectants with reduced levels of p59fyn were functionally impaired in their responses to antigen, Con A + recombinant IL-1 and cross-linking with anti-TCR mAb. Induction of tyrosine phosphorylation on most intracellular substrates was greatly reduced. We also noted that the Ick kinase activity was greatly reduced even though the amount of Ick protein was equivalent to that present in parental D10 cells. Our results suggest that the protein tyrosine kinase p59fyn is critical in TCR-mediated signaling and also suggests that p59fyn may regulate p56fyn tyrosine kinase activity.",

author = "Lee, {Sang kyou} and Andrey Shaw and Maher, {Stephen E.} and Bothwell, {Alfred L.M.}",

note = "Funding Information: WB thank K. Arai for the gift of the pNeoSRctll plasmid. Rabbit polyclonal antibodies specific to the 059**{"} protein were kindly provided by J. Bolen. This work was supported by NIH grant GM40924",

year = "1994",

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doi = "10.1093/intimm/6.10.1621",

language = "English",

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journal = "International Immunology",

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AU - Lee, Sang kyou

AU - Shaw, Andrey

AU - Maher, Stephen E.

AU - Bothwell, Alfred L.M.

N1 - Funding Information: WB thank K. Arai for the gift of the pNeoSRctll plasmid. Rabbit polyclonal antibodies specific to the 059**" protein were kindly provided by J. Bolen. This work was supported by NIH grant GM40924

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AB - To study the role of p59fyn in T cell activation, we used antisense RNA to inhibit p59fyn expression in a T cell clone. Transfectants with reduced levels of p59fyn were functionally impaired in their responses to antigen, Con A + recombinant IL-1 and cross-linking with anti-TCR mAb. Induction of tyrosine phosphorylation on most intracellular substrates was greatly reduced. We also noted that the Ick kinase activity was greatly reduced even though the amount of Ick protein was equivalent to that present in parental D10 cells. Our results suggest that the protein tyrosine kinase p59fyn is critical in TCR-mediated signaling and also suggests that p59fyn may regulate p56fyn tyrosine kinase activity.

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