T cell activation signals upregulate p38 map k1nase activity

L. Wang, P. H. Schäfer, J. K. Davis, S. A. Wads Worth, John Siekierka

Research output: Contribution to journalArticleResearchpeer-review

Abstract

p38 mitogen- activated protein (MAP) kinase defines a .subgroup of the mammalian MAP kinase family which is induced in response to various stimuli, such as physicochemical stress, and treatment with proinflarmnatory cytokines. However, the function of p38 in the regulation of I' cell responses has not been thoroughly examined. Therefore, we have, examined the activity of p38 follow ing T cell receptor (TCR) mediated signaling, using the human T cell clone IIA-1.70 or human T cells freshly isolated from peripheral blood. Here wr demonstrate that stimulation of clone HA-1.70 with either specific antigen or the superantigen Staphylococcal Enterotoxin B (SKB) leads to p38 activation and the release of Tumor Necrosis Factor IT (TNFrv). MAP kinase activated protein kinase-2 (MAPKAPK-2), a substrate of p;t8 m nro. is also activated by T cell signaling. This activation ran be blocked by CycSosporin A. a potent inhibitor of TCH-mediated signal transduction. Freshly isolated peripheral T cells can also be stimulated to activate the p38 pathway and release TNFa. We also demonstrate that a specific p38 inhibitor blocks p3H and MAPKAPK-2 activation in the T cell, but does not inhibit T cell production of TNFa. This is in contrast to TNFa production by human monocytes, where inhibition of p38 activity prevents TNFa production. Therefore, T cell activation signals can activate p38, but it appears that activation is not absolutely required for TNFo release.

Original languageEnglish
JournalFASEB Journal
Volume11
Issue number9
StatePublished - 1 Dec 1997

Fingerprint

T-cells
Up-Regulation
Chemical activation
T-Lymphocytes
Mitogen-Activated Protein Kinases
Clone Cells
Cell signaling
Superantigens
Signal transduction
p38 Mitogen-Activated Protein Kinases
T-Cell Antigen Receptor
Protein Kinases
Monocytes
Signal Transduction
Blood
Tumor Necrosis Factor-alpha
Cells
Cytokines
Antigens
Substrates

Cite this

Wang, L., Schäfer, P. H., Davis, J. K., Wads Worth, S. A., & Siekierka, J. (1997). T cell activation signals upregulate p38 map k1nase activity. FASEB Journal, 11(9).
Wang, L. ; Schäfer, P. H. ; Davis, J. K. ; Wads Worth, S. A. ; Siekierka, John. / T cell activation signals upregulate p38 map k1nase activity. In: FASEB Journal. 1997 ; Vol. 11, No. 9.
@article{cccd945e25ef4d4f8bc7d4f704e1ea5f,
title = "T cell activation signals upregulate p38 map k1nase activity",
abstract = "p38 mitogen- activated protein (MAP) kinase defines a .subgroup of the mammalian MAP kinase family which is induced in response to various stimuli, such as physicochemical stress, and treatment with proinflarmnatory cytokines. However, the function of p38 in the regulation of I' cell responses has not been thoroughly examined. Therefore, we have, examined the activity of p38 follow ing T cell receptor (TCR) mediated signaling, using the human T cell clone IIA-1.70 or human T cells freshly isolated from peripheral blood. Here wr demonstrate that stimulation of clone HA-1.70 with either specific antigen or the superantigen Staphylococcal Enterotoxin B (SKB) leads to p38 activation and the release of Tumor Necrosis Factor IT (TNFrv). MAP kinase activated protein kinase-2 (MAPKAPK-2), a substrate of p;t8 m nro. is also activated by T cell signaling. This activation ran be blocked by CycSosporin A. a potent inhibitor of TCH-mediated signal transduction. Freshly isolated peripheral T cells can also be stimulated to activate the p38 pathway and release TNFa. We also demonstrate that a specific p38 inhibitor blocks p3H and MAPKAPK-2 activation in the T cell, but does not inhibit T cell production of TNFa. This is in contrast to TNFa production by human monocytes, where inhibition of p38 activity prevents TNFa production. Therefore, T cell activation signals can activate p38, but it appears that activation is not absolutely required for TNFo release.",
author = "L. Wang and Sch{\"a}fer, {P. H.} and Davis, {J. K.} and {Wads Worth}, {S. A.} and John Siekierka",
year = "1997",
month = "12",
day = "1",
language = "English",
volume = "11",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "9",

}

Wang, L, Schäfer, PH, Davis, JK, Wads Worth, SA & Siekierka, J 1997, 'T cell activation signals upregulate p38 map k1nase activity', FASEB Journal, vol. 11, no. 9.

T cell activation signals upregulate p38 map k1nase activity. / Wang, L.; Schäfer, P. H.; Davis, J. K.; Wads Worth, S. A.; Siekierka, John.

In: FASEB Journal, Vol. 11, No. 9, 01.12.1997.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - T cell activation signals upregulate p38 map k1nase activity

AU - Wang, L.

AU - Schäfer, P. H.

AU - Davis, J. K.

AU - Wads Worth, S. A.

AU - Siekierka, John

PY - 1997/12/1

Y1 - 1997/12/1

N2 - p38 mitogen- activated protein (MAP) kinase defines a .subgroup of the mammalian MAP kinase family which is induced in response to various stimuli, such as physicochemical stress, and treatment with proinflarmnatory cytokines. However, the function of p38 in the regulation of I' cell responses has not been thoroughly examined. Therefore, we have, examined the activity of p38 follow ing T cell receptor (TCR) mediated signaling, using the human T cell clone IIA-1.70 or human T cells freshly isolated from peripheral blood. Here wr demonstrate that stimulation of clone HA-1.70 with either specific antigen or the superantigen Staphylococcal Enterotoxin B (SKB) leads to p38 activation and the release of Tumor Necrosis Factor IT (TNFrv). MAP kinase activated protein kinase-2 (MAPKAPK-2), a substrate of p;t8 m nro. is also activated by T cell signaling. This activation ran be blocked by CycSosporin A. a potent inhibitor of TCH-mediated signal transduction. Freshly isolated peripheral T cells can also be stimulated to activate the p38 pathway and release TNFa. We also demonstrate that a specific p38 inhibitor blocks p3H and MAPKAPK-2 activation in the T cell, but does not inhibit T cell production of TNFa. This is in contrast to TNFa production by human monocytes, where inhibition of p38 activity prevents TNFa production. Therefore, T cell activation signals can activate p38, but it appears that activation is not absolutely required for TNFo release.

AB - p38 mitogen- activated protein (MAP) kinase defines a .subgroup of the mammalian MAP kinase family which is induced in response to various stimuli, such as physicochemical stress, and treatment with proinflarmnatory cytokines. However, the function of p38 in the regulation of I' cell responses has not been thoroughly examined. Therefore, we have, examined the activity of p38 follow ing T cell receptor (TCR) mediated signaling, using the human T cell clone IIA-1.70 or human T cells freshly isolated from peripheral blood. Here wr demonstrate that stimulation of clone HA-1.70 with either specific antigen or the superantigen Staphylococcal Enterotoxin B (SKB) leads to p38 activation and the release of Tumor Necrosis Factor IT (TNFrv). MAP kinase activated protein kinase-2 (MAPKAPK-2), a substrate of p;t8 m nro. is also activated by T cell signaling. This activation ran be blocked by CycSosporin A. a potent inhibitor of TCH-mediated signal transduction. Freshly isolated peripheral T cells can also be stimulated to activate the p38 pathway and release TNFa. We also demonstrate that a specific p38 inhibitor blocks p3H and MAPKAPK-2 activation in the T cell, but does not inhibit T cell production of TNFa. This is in contrast to TNFa production by human monocytes, where inhibition of p38 activity prevents TNFa production. Therefore, T cell activation signals can activate p38, but it appears that activation is not absolutely required for TNFo release.

UR - http://www.scopus.com/inward/record.url?scp=33750184835&partnerID=8YFLogxK

M3 - Article

VL - 11

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 9

ER -

Wang L, Schäfer PH, Davis JK, Wads Worth SA, Siekierka J. T cell activation signals upregulate p38 map k1nase activity. FASEB Journal. 1997 Dec 1;11(9).