Role of protein kinase c in interleukin 1, anti‐T3, and mitogenic lectin‐induced interleukin 2 secretion

Gordon Mills, Christopher May, Mary Hill, Erwin W. Gelfand

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Activation of T‐lymphocytes by antigen, mitogenic lectins, or antibodies against the T‐cell receptor complex, particularly in the presence of IL1, induces the secretion of the T‐cell growth factor IL2. IL2 then has a major role in regulating the duration and magnitude of the immune response. Interaction of antigen, antibodies against the T‐cell receptor complex, or mitogenic lectins with T‐lymphocytes also induces hydrolysis of membrane phospholipids, leading to the production of diacylglycerol, an activator of the Ca2+‐ and phospholipid‐dependent phosphotransferase, protein kinase C (PKC). Phorbol esters, potent activators of PKC, augment secretion of the T‐cell growth factor, interleukin 2 (IL2). Activation of PKC may therefore serve as an important early event in the production and secretion of IL2. We have determined whether IL2 secretion can be induced in the murine cell T‐lymphocyte line LBRM 331A5, where PKC is inhibited by staurosporine or sphingosine or in cells where PKC is depleted by prolonged incubation with high concentrations of phorbol esters. In cells in which PKC was either inhibited or depleted, antibodies against the T3 portion of the T‐cell receptor complex and the mitogenic lectin phytohemagglutinin (PHA) still triggered IL2 secretion. In addition, the monokine Ill augmented this IL2 secretion irrespective of whether PKC was inhibited or depleted. These data indicate that activation of PKC is not an obligatory step for IL2 secretion in LBRM 331A5 murine T‐lymphocytes.

Original languageEnglish (US)
Pages (from-to)310-317
Number of pages8
JournalJournal of Cellular Physiology
Volume141
Issue number2
DOIs
StatePublished - Jan 1 1989
Externally publishedYes

Fingerprint

Interleukin-1
Protein Kinases
Protein Kinase C
Interleukin-2
Lectins
Chemical activation
Phorbol Esters
Antibodies
Intercellular Signaling Peptides and Proteins
Monokines
Antigens
Sphingosine
Staurosporine
Diglycerides
Phytohemagglutinins
Hydrolysis
Phospholipids
Phosphotransferases
Membranes
Cell Line

ASJC Scopus subject areas

  • Medicine(all)
  • Physiology
  • Clinical Biochemistry
  • Cell Biology

Cite this

Role of protein kinase c in interleukin 1, anti‐T3, and mitogenic lectin‐induced interleukin 2 secretion. / Mills, Gordon; May, Christopher; Hill, Mary; Gelfand, Erwin W.

In: Journal of Cellular Physiology, Vol. 141, No. 2, 01.01.1989, p. 310-317.

Research output: Contribution to journalArticle

@article{e133b7a5f2a24cf49c5b3859a2b352f2,
title = "Role of protein kinase c in interleukin 1, anti‐T3, and mitogenic lectin‐induced interleukin 2 secretion",
abstract = "Activation of T‐lymphocytes by antigen, mitogenic lectins, or antibodies against the T‐cell receptor complex, particularly in the presence of IL1, induces the secretion of the T‐cell growth factor IL2. IL2 then has a major role in regulating the duration and magnitude of the immune response. Interaction of antigen, antibodies against the T‐cell receptor complex, or mitogenic lectins with T‐lymphocytes also induces hydrolysis of membrane phospholipids, leading to the production of diacylglycerol, an activator of the Ca2+‐ and phospholipid‐dependent phosphotransferase, protein kinase C (PKC). Phorbol esters, potent activators of PKC, augment secretion of the T‐cell growth factor, interleukin 2 (IL2). Activation of PKC may therefore serve as an important early event in the production and secretion of IL2. We have determined whether IL2 secretion can be induced in the murine cell T‐lymphocyte line LBRM 331A5, where PKC is inhibited by staurosporine or sphingosine or in cells where PKC is depleted by prolonged incubation with high concentrations of phorbol esters. In cells in which PKC was either inhibited or depleted, antibodies against the T3 portion of the T‐cell receptor complex and the mitogenic lectin phytohemagglutinin (PHA) still triggered IL2 secretion. In addition, the monokine Ill augmented this IL2 secretion irrespective of whether PKC was inhibited or depleted. These data indicate that activation of PKC is not an obligatory step for IL2 secretion in LBRM 331A5 murine T‐lymphocytes.",
author = "Gordon Mills and Christopher May and Mary Hill and Gelfand, {Erwin W.}",
year = "1989",
month = "1",
day = "1",
doi = "10.1002/jcp.1041410212",
language = "English (US)",
volume = "141",
pages = "310--317",
journal = "Journal of Cellular Physiology",
issn = "0021-9541",
publisher = "Wiley-Liss Inc.",
number = "2",

}

TY - JOUR

T1 - Role of protein kinase c in interleukin 1, anti‐T3, and mitogenic lectin‐induced interleukin 2 secretion

AU - Mills, Gordon

AU - May, Christopher

AU - Hill, Mary

AU - Gelfand, Erwin W.

PY - 1989/1/1

Y1 - 1989/1/1

N2 - Activation of T‐lymphocytes by antigen, mitogenic lectins, or antibodies against the T‐cell receptor complex, particularly in the presence of IL1, induces the secretion of the T‐cell growth factor IL2. IL2 then has a major role in regulating the duration and magnitude of the immune response. Interaction of antigen, antibodies against the T‐cell receptor complex, or mitogenic lectins with T‐lymphocytes also induces hydrolysis of membrane phospholipids, leading to the production of diacylglycerol, an activator of the Ca2+‐ and phospholipid‐dependent phosphotransferase, protein kinase C (PKC). Phorbol esters, potent activators of PKC, augment secretion of the T‐cell growth factor, interleukin 2 (IL2). Activation of PKC may therefore serve as an important early event in the production and secretion of IL2. We have determined whether IL2 secretion can be induced in the murine cell T‐lymphocyte line LBRM 331A5, where PKC is inhibited by staurosporine or sphingosine or in cells where PKC is depleted by prolonged incubation with high concentrations of phorbol esters. In cells in which PKC was either inhibited or depleted, antibodies against the T3 portion of the T‐cell receptor complex and the mitogenic lectin phytohemagglutinin (PHA) still triggered IL2 secretion. In addition, the monokine Ill augmented this IL2 secretion irrespective of whether PKC was inhibited or depleted. These data indicate that activation of PKC is not an obligatory step for IL2 secretion in LBRM 331A5 murine T‐lymphocytes.

AB - Activation of T‐lymphocytes by antigen, mitogenic lectins, or antibodies against the T‐cell receptor complex, particularly in the presence of IL1, induces the secretion of the T‐cell growth factor IL2. IL2 then has a major role in regulating the duration and magnitude of the immune response. Interaction of antigen, antibodies against the T‐cell receptor complex, or mitogenic lectins with T‐lymphocytes also induces hydrolysis of membrane phospholipids, leading to the production of diacylglycerol, an activator of the Ca2+‐ and phospholipid‐dependent phosphotransferase, protein kinase C (PKC). Phorbol esters, potent activators of PKC, augment secretion of the T‐cell growth factor, interleukin 2 (IL2). Activation of PKC may therefore serve as an important early event in the production and secretion of IL2. We have determined whether IL2 secretion can be induced in the murine cell T‐lymphocyte line LBRM 331A5, where PKC is inhibited by staurosporine or sphingosine or in cells where PKC is depleted by prolonged incubation with high concentrations of phorbol esters. In cells in which PKC was either inhibited or depleted, antibodies against the T3 portion of the T‐cell receptor complex and the mitogenic lectin phytohemagglutinin (PHA) still triggered IL2 secretion. In addition, the monokine Ill augmented this IL2 secretion irrespective of whether PKC was inhibited or depleted. These data indicate that activation of PKC is not an obligatory step for IL2 secretion in LBRM 331A5 murine T‐lymphocytes.

UR - http://www.scopus.com/inward/record.url?scp=0024463390&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024463390&partnerID=8YFLogxK

U2 - 10.1002/jcp.1041410212

DO - 10.1002/jcp.1041410212

M3 - Article

VL - 141

SP - 310

EP - 317

JO - Journal of Cellular Physiology

JF - Journal of Cellular Physiology

SN - 0021-9541

IS - 2

ER -