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Increased protein synthesis by cells exposed to a 1,800-MHz radio-frequency mobile phone electromagnetic field, detected by proteome profiling.

Gerner C, Haudek V, Schandl U, Bayer E, Gundacker N, Hutter HP, Mosgoeller W - Int Arch Occup Environ Health (2010)

Bottom Line: Quiescent (metabolically inactive) mononuclear cells, did not detectably respond to RF-EME.Our finding of an association between metabolic activity and the observed cellular reaction to low intensity RF-EME may reconcile conflicting results of previous studies.Our observations do not directly imply a health risk.

View Article: PubMed Central - PubMed

Affiliation: Department Med.-1, Institute of Cancer Research, Medical University Vienna, Borschkegasse 8a, 1090 Vienna, Austria.

ABSTRACT

Purpose: To investigate whether or not low intensity radio frequency electromagnetic field exposure (RF-EME) associated with mobile phone use can affect human cells, we used a sensitive proteome analysis method to study changes in protein synthesis in cultured human cells.

Methods: Four different cell kinds were exposed to 2 W/kg specific absorption rate in medium containing 35S-methionine/cysteine, and autoradiography of 2D gel spots was used to measure the increased synthesis of individual proteins.

Results: While short-term RF-EME did not significantly alter the proteome, an 8-h exposure caused a significant increase in protein synthesis in Jurkat T-cells and human fibroblasts, and to a lesser extent in activated primary human mononuclear cells. Quiescent (metabolically inactive) mononuclear cells, did not detectably respond to RF-EME. Since RF exposure induced a temperature increase of less than 0.15 degrees C, we suggest that the observed cellular response is a so called "athermal" effect of RF-EME.

Conclusion: Our finding of an association between metabolic activity and the observed cellular reaction to low intensity RF-EME may reconcile conflicting results of previous studies. We further postulate that the observed increased protein synthesis reflects an increased rate of protein turnover stemming from protein folding problems caused by the interference of radio-frequency electromagnetic fields with hydrogen bonds. Our observations do not directly imply a health risk. However, vis-a-vis a synopsis of reports on cells stress and DNA breaks, after short and longer exposure, on active and inactive cells, our findings may contribute to the re-evaluation of previous reports.

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Related in: MedlinePlus

The RF-EME induced increase of 35S incorporation rates was reproducibly observed in different cell types. ab and c, d show two independent experiments with Jurkat cells. e, f is a representative example for cultured human fibroblasts showing the highest induction of 35S incorporation rates by RF-EME, g, h shows a representative example of quiescent (metabolically inactive) primary human white blood cells (WBC). Here, RF-EME hardly induced detectable increases in 35S incorporation rates; compared to untreated controls (g), activated WBC (i) displayed higher 35S incorporation rates, RF-EME induced a further increase in 35S incorporation rates (j), which indicates that activity renders cells sensitive to RF-EME
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Fig4: The RF-EME induced increase of 35S incorporation rates was reproducibly observed in different cell types. ab and c, d show two independent experiments with Jurkat cells. e, f is a representative example for cultured human fibroblasts showing the highest induction of 35S incorporation rates by RF-EME, g, h shows a representative example of quiescent (metabolically inactive) primary human white blood cells (WBC). Here, RF-EME hardly induced detectable increases in 35S incorporation rates; compared to untreated controls (g), activated WBC (i) displayed higher 35S incorporation rates, RF-EME induced a further increase in 35S incorporation rates (j), which indicates that activity renders cells sensitive to RF-EME

Mentions: We categorized a protein as specifically up-regulated if the normalized integrated 35S autoradiograph spot intensity was at least two-fold greater than the corresponding control cell spot with an ANOVA P-value of less than 0.05. Using this criterion, fourteen proteins were found to be specifically up-regulated and were subsequently identified by mass spectrometry as described in Materials and Methods (Table 1 and supplementary data). Figure 2 provides three examples of proteins specifically up-regulated by RF-EME: heat shock protein 70, ubiquitin carboxyl-terminal hydrolase 14 and 26S protease regulatory subunit 6B. Figure 3 shows peptide fragmentation mass spectra of peptides derived from ubiquitin carboxyl-terminal hydrolase 14 and 26S protease regulatory subunit 6 in order to demonstrate the high degree of reliability of the protein identification procedure used. The RF-EME induced increase in protein synthesis (Fig. 4a–f) was highly reproducible.Fig. 2


Increased protein synthesis by cells exposed to a 1,800-MHz radio-frequency mobile phone electromagnetic field, detected by proteome profiling.

Gerner C, Haudek V, Schandl U, Bayer E, Gundacker N, Hutter HP, Mosgoeller W - Int Arch Occup Environ Health (2010)

The RF-EME induced increase of 35S incorporation rates was reproducibly observed in different cell types. ab and c, d show two independent experiments with Jurkat cells. e, f is a representative example for cultured human fibroblasts showing the highest induction of 35S incorporation rates by RF-EME, g, h shows a representative example of quiescent (metabolically inactive) primary human white blood cells (WBC). Here, RF-EME hardly induced detectable increases in 35S incorporation rates; compared to untreated controls (g), activated WBC (i) displayed higher 35S incorporation rates, RF-EME induced a further increase in 35S incorporation rates (j), which indicates that activity renders cells sensitive to RF-EME
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2902737&req=5

Fig4: The RF-EME induced increase of 35S incorporation rates was reproducibly observed in different cell types. ab and c, d show two independent experiments with Jurkat cells. e, f is a representative example for cultured human fibroblasts showing the highest induction of 35S incorporation rates by RF-EME, g, h shows a representative example of quiescent (metabolically inactive) primary human white blood cells (WBC). Here, RF-EME hardly induced detectable increases in 35S incorporation rates; compared to untreated controls (g), activated WBC (i) displayed higher 35S incorporation rates, RF-EME induced a further increase in 35S incorporation rates (j), which indicates that activity renders cells sensitive to RF-EME
Mentions: We categorized a protein as specifically up-regulated if the normalized integrated 35S autoradiograph spot intensity was at least two-fold greater than the corresponding control cell spot with an ANOVA P-value of less than 0.05. Using this criterion, fourteen proteins were found to be specifically up-regulated and were subsequently identified by mass spectrometry as described in Materials and Methods (Table 1 and supplementary data). Figure 2 provides three examples of proteins specifically up-regulated by RF-EME: heat shock protein 70, ubiquitin carboxyl-terminal hydrolase 14 and 26S protease regulatory subunit 6B. Figure 3 shows peptide fragmentation mass spectra of peptides derived from ubiquitin carboxyl-terminal hydrolase 14 and 26S protease regulatory subunit 6 in order to demonstrate the high degree of reliability of the protein identification procedure used. The RF-EME induced increase in protein synthesis (Fig. 4a–f) was highly reproducible.Fig. 2

Bottom Line: Quiescent (metabolically inactive) mononuclear cells, did not detectably respond to RF-EME.Our finding of an association between metabolic activity and the observed cellular reaction to low intensity RF-EME may reconcile conflicting results of previous studies.Our observations do not directly imply a health risk.

View Article: PubMed Central - PubMed

Affiliation: Department Med.-1, Institute of Cancer Research, Medical University Vienna, Borschkegasse 8a, 1090 Vienna, Austria.

ABSTRACT

Purpose: To investigate whether or not low intensity radio frequency electromagnetic field exposure (RF-EME) associated with mobile phone use can affect human cells, we used a sensitive proteome analysis method to study changes in protein synthesis in cultured human cells.

Methods: Four different cell kinds were exposed to 2 W/kg specific absorption rate in medium containing 35S-methionine/cysteine, and autoradiography of 2D gel spots was used to measure the increased synthesis of individual proteins.

Results: While short-term RF-EME did not significantly alter the proteome, an 8-h exposure caused a significant increase in protein synthesis in Jurkat T-cells and human fibroblasts, and to a lesser extent in activated primary human mononuclear cells. Quiescent (metabolically inactive) mononuclear cells, did not detectably respond to RF-EME. Since RF exposure induced a temperature increase of less than 0.15 degrees C, we suggest that the observed cellular response is a so called "athermal" effect of RF-EME.

Conclusion: Our finding of an association between metabolic activity and the observed cellular reaction to low intensity RF-EME may reconcile conflicting results of previous studies. We further postulate that the observed increased protein synthesis reflects an increased rate of protein turnover stemming from protein folding problems caused by the interference of radio-frequency electromagnetic fields with hydrogen bonds. Our observations do not directly imply a health risk. However, vis-a-vis a synopsis of reports on cells stress and DNA breaks, after short and longer exposure, on active and inactive cells, our findings may contribute to the re-evaluation of previous reports.

Show MeSH
Related in: MedlinePlus