Electromagnetic field effects: Changes in protein phosphorylation in the Jurkat E6.1 cell line

B. J. Wetzel, G. Nindl, D. N. Vesper, J. A. Swez, A. C. Jasti, M. T. Johnson

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

This study is aimed at expanding the role of electromagnetic field (EMF) therapy for treatment of inflammatory diseases and obtaining new information on the biophysical mechanism of action of weak EMFs. The mechanism of action of EMFs on biological systems is a question that has yet to be answered. Several models have been proposed to explain the coupling of low frequency fields to biological systems, although no consensus has been reached as to which most adequately portrays the true mechanism. Protein phosphorylation is a major cellular metabolic regulator. As such, it has the potential to be a valuable indicator of the impact of EMFs on cellular metabolism. Using a well-controlled EMF exposure system, we examined the regulatory role of EMFs on low molecular weight protein phosphorylation in Jurkat E6.1 cells, a transformed human leukemic T cell line. Jurkat cells were grown to mid-log phase, preloaded with 32P and exposed to EMF (0.1 mT, 60Hz) or sham for 30 minutes. Cell proteins were separated by SDS-polyacrylamide gel electrophoresis and incorporated radioactivity of low molecular weight proteins (18-23kDa) was quantified by AMBIS data analysis. Three of five experiments showed no difference in protein phosphorylation in EMF exposed samples compared to controls, while two experiments revealed an EMF effect. We identified stathmin, an important T cell signaling phosphoprotein, as one of the low molecular weight proteins present in our Jurkat cell system. Stathmin expression as well as its phosphorylation was decreased in samples that were exposed to EMFs compared to controls. These data indicate that phosphorylation of individual proteins might be masked by the presence of numerous other proteins in whole cell lysate experiments. Further studies testing other low molecular weight T cell signaling molecules may validate this hypothesis.

Original languageEnglish
Pages (from-to)203-208
Number of pages6
JournalBiomedical Sciences Instrumentation
Volume37
StatePublished - 2001

Fingerprint

Electromagnetic field effects
Phosphorylation
Electromagnetic Fields
Jurkat Cells
Cells
Proteins
Cell Line
Electromagnetic fields
T-cells
Stathmin
Molecular Weight
Molecular weight
Cell signaling
Electric potential
Biological systems
T-Lymphocytes
Phosphoproteins
Experiments
Radioactivity
Polyacrylates

Keywords

  • Electromagnetic fields
  • EMF
  • Jurkat
  • Protein phosphorylation
  • Stathmin
  • T lymphocyte

ASJC Scopus subject areas

  • Hardware and Architecture

Cite this

Wetzel, B. J., Nindl, G., Vesper, D. N., Swez, J. A., Jasti, A. C., & Johnson, M. T. (2001). Electromagnetic field effects: Changes in protein phosphorylation in the Jurkat E6.1 cell line. Biomedical Sciences Instrumentation, 37, 203-208.

Electromagnetic field effects : Changes in protein phosphorylation in the Jurkat E6.1 cell line. / Wetzel, B. J.; Nindl, G.; Vesper, D. N.; Swez, J. A.; Jasti, A. C.; Johnson, M. T.

In: Biomedical Sciences Instrumentation, Vol. 37, 2001, p. 203-208.

Research output: Contribution to journalArticle

Wetzel, BJ, Nindl, G, Vesper, DN, Swez, JA, Jasti, AC & Johnson, MT 2001, 'Electromagnetic field effects: Changes in protein phosphorylation in the Jurkat E6.1 cell line', Biomedical Sciences Instrumentation, vol. 37, pp. 203-208.
Wetzel, B. J. ; Nindl, G. ; Vesper, D. N. ; Swez, J. A. ; Jasti, A. C. ; Johnson, M. T. / Electromagnetic field effects : Changes in protein phosphorylation in the Jurkat E6.1 cell line. In: Biomedical Sciences Instrumentation. 2001 ; Vol. 37. pp. 203-208.
@article{c37452079b0443a68f8676a4f8401c6c,
title = "Electromagnetic field effects: Changes in protein phosphorylation in the Jurkat E6.1 cell line",
abstract = "This study is aimed at expanding the role of electromagnetic field (EMF) therapy for treatment of inflammatory diseases and obtaining new information on the biophysical mechanism of action of weak EMFs. The mechanism of action of EMFs on biological systems is a question that has yet to be answered. Several models have been proposed to explain the coupling of low frequency fields to biological systems, although no consensus has been reached as to which most adequately portrays the true mechanism. Protein phosphorylation is a major cellular metabolic regulator. As such, it has the potential to be a valuable indicator of the impact of EMFs on cellular metabolism. Using a well-controlled EMF exposure system, we examined the regulatory role of EMFs on low molecular weight protein phosphorylation in Jurkat E6.1 cells, a transformed human leukemic T cell line. Jurkat cells were grown to mid-log phase, preloaded with 32P and exposed to EMF (0.1 mT, 60Hz) or sham for 30 minutes. Cell proteins were separated by SDS-polyacrylamide gel electrophoresis and incorporated radioactivity of low molecular weight proteins (18-23kDa) was quantified by AMBIS data analysis. Three of five experiments showed no difference in protein phosphorylation in EMF exposed samples compared to controls, while two experiments revealed an EMF effect. We identified stathmin, an important T cell signaling phosphoprotein, as one of the low molecular weight proteins present in our Jurkat cell system. Stathmin expression as well as its phosphorylation was decreased in samples that were exposed to EMFs compared to controls. These data indicate that phosphorylation of individual proteins might be masked by the presence of numerous other proteins in whole cell lysate experiments. Further studies testing other low molecular weight T cell signaling molecules may validate this hypothesis.",
keywords = "Electromagnetic fields, EMF, Jurkat, Protein phosphorylation, Stathmin, T lymphocyte",
author = "Wetzel, {B. J.} and G. Nindl and Vesper, {D. N.} and Swez, {J. A.} and Jasti, {A. C.} and Johnson, {M. T.}",
year = "2001",
language = "English",
volume = "37",
pages = "203--208",
journal = "Biomedical Sciences Instrumentation",
issn = "0067-8856",
publisher = "ISA - Instrumentation, Systems, and Automation Society",

}

TY - JOUR

T1 - Electromagnetic field effects

T2 - Changes in protein phosphorylation in the Jurkat E6.1 cell line

AU - Wetzel, B. J.

AU - Nindl, G.

AU - Vesper, D. N.

AU - Swez, J. A.

AU - Jasti, A. C.

AU - Johnson, M. T.

PY - 2001

Y1 - 2001

N2 - This study is aimed at expanding the role of electromagnetic field (EMF) therapy for treatment of inflammatory diseases and obtaining new information on the biophysical mechanism of action of weak EMFs. The mechanism of action of EMFs on biological systems is a question that has yet to be answered. Several models have been proposed to explain the coupling of low frequency fields to biological systems, although no consensus has been reached as to which most adequately portrays the true mechanism. Protein phosphorylation is a major cellular metabolic regulator. As such, it has the potential to be a valuable indicator of the impact of EMFs on cellular metabolism. Using a well-controlled EMF exposure system, we examined the regulatory role of EMFs on low molecular weight protein phosphorylation in Jurkat E6.1 cells, a transformed human leukemic T cell line. Jurkat cells were grown to mid-log phase, preloaded with 32P and exposed to EMF (0.1 mT, 60Hz) or sham for 30 minutes. Cell proteins were separated by SDS-polyacrylamide gel electrophoresis and incorporated radioactivity of low molecular weight proteins (18-23kDa) was quantified by AMBIS data analysis. Three of five experiments showed no difference in protein phosphorylation in EMF exposed samples compared to controls, while two experiments revealed an EMF effect. We identified stathmin, an important T cell signaling phosphoprotein, as one of the low molecular weight proteins present in our Jurkat cell system. Stathmin expression as well as its phosphorylation was decreased in samples that were exposed to EMFs compared to controls. These data indicate that phosphorylation of individual proteins might be masked by the presence of numerous other proteins in whole cell lysate experiments. Further studies testing other low molecular weight T cell signaling molecules may validate this hypothesis.

AB - This study is aimed at expanding the role of electromagnetic field (EMF) therapy for treatment of inflammatory diseases and obtaining new information on the biophysical mechanism of action of weak EMFs. The mechanism of action of EMFs on biological systems is a question that has yet to be answered. Several models have been proposed to explain the coupling of low frequency fields to biological systems, although no consensus has been reached as to which most adequately portrays the true mechanism. Protein phosphorylation is a major cellular metabolic regulator. As such, it has the potential to be a valuable indicator of the impact of EMFs on cellular metabolism. Using a well-controlled EMF exposure system, we examined the regulatory role of EMFs on low molecular weight protein phosphorylation in Jurkat E6.1 cells, a transformed human leukemic T cell line. Jurkat cells were grown to mid-log phase, preloaded with 32P and exposed to EMF (0.1 mT, 60Hz) or sham for 30 minutes. Cell proteins were separated by SDS-polyacrylamide gel electrophoresis and incorporated radioactivity of low molecular weight proteins (18-23kDa) was quantified by AMBIS data analysis. Three of five experiments showed no difference in protein phosphorylation in EMF exposed samples compared to controls, while two experiments revealed an EMF effect. We identified stathmin, an important T cell signaling phosphoprotein, as one of the low molecular weight proteins present in our Jurkat cell system. Stathmin expression as well as its phosphorylation was decreased in samples that were exposed to EMFs compared to controls. These data indicate that phosphorylation of individual proteins might be masked by the presence of numerous other proteins in whole cell lysate experiments. Further studies testing other low molecular weight T cell signaling molecules may validate this hypothesis.

KW - Electromagnetic fields

KW - EMF

KW - Jurkat

KW - Protein phosphorylation

KW - Stathmin

KW - T lymphocyte

UR - http://www.scopus.com/inward/record.url?scp=0035027272&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035027272&partnerID=8YFLogxK

M3 - Article

C2 - 11347389

AN - SCOPUS:0035027272

VL - 37

SP - 203

EP - 208

JO - Biomedical Sciences Instrumentation

JF - Biomedical Sciences Instrumentation

SN - 0067-8856

ER -