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B Raposa University of Pécs, Hungary
University of Pécs, Hungary

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R Pónusz University of Pécs, Hungary

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G Gerencsér University of Pécs, Hungary

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F Budán University of Pécs, Hungary

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Z Gyöngyi University of Pécs, Hungary

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A Tibold University of Pécs, Hungary

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D Hegyi University of Pécs, Hungary

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I Kiss University of Pécs, Hungary

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Á Koller University of Physical Education, Hungary

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T Varjas University of Pécs, Hungary

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It has been reported that some of the food additives may cause sensitization, inflammation of tissues, and potentially risk factors in the development of several chronic diseases. Thus, we hypothesized that expressions of common inflammatory molecules – known to be involved in the development of various inflammatory conditions and cancers – are affected by these food additives. We investigated the effects of commonly used food preservatives and artificial food colorants based on the expressions of NFκB, GADD45α, and MAPK8 (JNK1) from the tissues of liver. RNA was isolated based on Trizol protocol and the activation levels were compared between the treated and the control groups. Tartrazine alone could elicit effects on the expressions of NFκB (p = 0.013) and MAPK8 (p = 0.022). Azorubine also resulted in apoptosis according to MAPK8 expression (p = 0.009). Preservatives were anti-apoptotic in high dose. Sodium benzoate (from low to high doses) dose-dependently silenced MAPK8 expression (p = 0.004 to p = 0.002). Addition of the two preservatives together elicited significantly greater expression of MAPK8 at half-fold dose (p = 0.002) and at fivefold dose (p = 0.008). This study suggests that some of the food preservatives and colorants can contribute to the activation of inflammatory pathways.

  • 1.

    Amin KA , Abdel Hameid IIH , Abd Elsttar AH : Effect of food azo dyes tartrazine and carmoisine on biochemical parameters related to renal, hepatic function and oxidative stress biomarkers in young male rats. Food Chem. Toxicol. 48, 29942999 (2010)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 2.

    Banning A , Regenbrecht CRA , Tikkanen R : Increased activity of mitogen activated protein kinase pathway in flotillin-2 knockout mouse model. Cell Signal. 26, 198207 (2014)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 3.

    Bateman B , Warner JO , Hutchinson E , Dean T , Rowlandson P , Gant C , Grundy J , Fitzgerald C , Stevenson J : The effects of a double blind, placebo-controlled, artificial food colourings and benzoate preservative challenge on hyperactivity in a general population sample of preschool children. Arch. Dis. Child. 89, 506551 (2004)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 4.

    Brahmachari S , Pahan K : Sodium benzoate, a food additive and a metabolite of cinnamon, modifies T-cells at multiple steps and inhibits adoptive transfer of experimental allergic encephalomyelitis. J. Immunol. 179, 275283 (2007)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 5.

    Brasier AR : The NF-κB regulatory network. Cardiovasc. Toxicol. 6, 111130 (2006)

  • 6.

    Chequer FM , Venâncio VP , Bianchi ML , Antunes LM : Genotoxic and mutagenic effects of erythrosine B, a xanthene food dye, on HepG2 cells. Food Chem. Toxicol. 50, 34473451 (2012)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 7.

    Chomczynski P , Sacchi N : Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156159 (1987)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 8.

    European Parliament and of the Council [EC]: Regulation No. 1333/2008: establishing a common authorisation procedure for food additives, food enzymes and food flavourings. OJ. L. 354, 133 (2008)

    • Search Google Scholar
    • Export Citation
  • 9.

    European Food Safety Agency [EFSA]: Assessment of the results of the study by McCann et al. (2007) on the effects of some colours and sodium benzoate on children’s behaviour. EFSA J. 660, 153 (2008)

    • Search Google Scholar
    • Export Citation
  • 10.

    Gao Y , Li C , Yin H , An X , Jin H : Effect of food azo dye tartrazine on learning and memory functions in mice and rats, and the possible mechanisms involved. J. Food Sci. 76, 125129 (2011)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 11.

    Gilmore TD : Introduction to NF-κB: players, pathways, perspectives. Oncogene 25, 66806684 (2006)

  • 12.

    Görena AC , Bilsela G , Şimşeka A , Bilsela M , Akçadağa F , Topala K , Ozgenb H : HPLC and LC-MS/MS methods for determination of sodium benzoate and potassium sorbate in food and beverages: performances of local accredited laboratories via proficiency tests in Turkey. Food Chem. 175, 273279 (2015)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 13.

    Jarskog LF : Apoptosis in schizophrenia: pathophysiologic and therapeutic considerations. Curr. Opin. Psychiatry 19, 307312 (2006)

  • 14.

    Kitano K , Fukukawa T , Ohtsuji Y , Masuda T , Yamaguchi H : Mutagenicity and DNA-damaging activity caused by decomposed products of potassium sorbate reacting with ascorbic acid in the presence of Fe salt. Food Chem. Toxicol. 40, 15891594 (2002)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 15.

    Klock A , Herrmann BG : Cloning and expression of the mouse dual-specificity mitogen-activated protein (MAP) kinase phosphatase Mkp3 during mouse embryogenesis. Mech. Develop. 116, 243247 (2002)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 16.

    Leathwood PD , Richardson DP , Sträter P , Todd PM , van Trijp HC : Consumer understanding of nutrition and health claims: sources of evidence. Br. J. Nutr. 98, 474484 (2007)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 17.

    Mamur S , Yüzbaşıoğlu D , Ünal F , Yılmaz S : Does potassium sorbate induce genotoxic or mutagenic effects in lymphocytes? Toxicol. In Vitro 24, 790794 (2010)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 18.

    Mielke K , Brecht S , Dorst A , Herdegen T : Activity and expression of JNK1, p38 and ERK kinases, c-Jun N-terminal phosphorylation, and c-jun promoter binding in the adult rat brain following kainate-induced seizures. Neuroscience 91, 471483 (1999)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 19.

    Miotto B , Struhl K : JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone acetylase and blocks replication licensing in response to stress. Mol. Cell 7, 6271 (2011)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 20.

    Peretz G , Bakhrat A , Abdu U : Expression of the Drosophila melanogaster GADD45 homolog (CG11086) affects egg asymmetric development that is mediated by the c-Jun N-terminal kinase pathway. Genetics 177, 16911702 (2007)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 21.

    Poul M , Jarry G , Elhkim MO , Poul JM : Lack of genotoxic effect of food dyes amaranth, sunset yellow and tartrazine and their metabolites in the gut micronucleus assay in mice. Food Chem. Toxicol. 47, 443448 (2009)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 22.

    Reagan-Shaw S , Nihal M , Ahmad N : Dose translation from animal to human studies revisited. FASEB J. 22, 659661 (2007)

  • 23.

    Sasaki YF , Kawaguchi S , Kamaya A , Ohshita M , Kabasawa K , Iwama K , Taniguchi K , Tsuda S : The comet assay with 8 mouse organs results with 39 currently used food additives. Mutat. Res. 519, 103119 (2002)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 24.

    Sheikh MS , Hollander MC , Fornace AJ : Role of Gadd45 in apoptosis. Biochem. Pharmacol. 59, 4345 (2000)

  • 25.

    Soares BM , Araújo TM , Ramos JA , Pinto LC , Khayat BM , De Oliveira Bahia M , Montenegro RC , Burbano RM , Khayat AS : Effects on DNA repair in human lymphocytes exposed to the food dye tartrazine yellow. Anticancer Res. 35, 14651474 (2015)

    • Search Google Scholar
    • Export Citation
  • 26.

    Solinas G , Vilcu C , Neels JG , Bandyopadhyay GK , Luo JL , Naugler W , Grivennikov S , Wynshaw-Boris A , Scadeng M , Olefsky JM , Karin M : JNK1 in hematopoietically derived cells contributes to diet-induced inflammation and insulin resistance without affecting obesity. Cell Metab. 6, 386397 (2007)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 27.

    Takekawa M , Saito H : A family of stress-inducible GADD45-like proteins mediate activation of the stress-responsive MTK1/MEKK4 MAPKKK. Cell 95, 521530 (1998)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 28.

    Tsuda S , Murakami M , Matsusaka N , Kano K , Taniguchi K , Sasaki YF : DNA damage induced by red food dyes orally administered to pregnant and male mice. Toxicol. Sci. 61, 9299 (2001)

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 29.

    Türkoğlu S : Genotoxicity of five food preservatives tested on root tips of Allium cepa L. Mutat. Res. 626, 414 (2007)

  • 30.

    Zheng X , Zhang Y , Chen Y , Castranova V , Shi X , Chen F : Inhibition of NF-κB stabilizes gadd45α mRNA. Biochem. Biophys. Res. Commun. 329, 9599 (2005)

    • Crossref
    • Search Google Scholar
    • Export Citation
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Editor-in-Chief

László ROSIVALL (Semmelweis University, Budapest, Hungary)

Managing Editor

Anna BERHIDI (Semmelweis University, Budapest, Hungary)

Co-Editors

  • Gábor SZÉNÁSI (Semmelweis University, Budapest, Hungary)
  • Ákos KOLLER (Semmelweis University, Budapest, Hungary)
  • Zsolt RADÁK (University of Physical Education, Budapest, Hungary)
  • László LÉNÁRD (University of Pécs, Hungary)
  • Zoltán UNGVÁRI (Semmelweis University, Budapest, Hungary)

Assistant Editors

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  • Zsuzsanna MIKLÓS (Semmelweis University, Budapest, Hungary)
  • György NÁDASY (Semmelweis University, Budapest, Hungary)

Hungarian Editorial Board

  • György BENEDEK (University of Szeged, Hungary)
  • Zoltán BENYÓ (Semmelweis University, Budapest, Hungary)
  • Mihály BOROS (University of Szeged, Hungary)
  • László CSERNOCH (University of Debrecen, Hungary)
  • Magdolna DANK (Semmelweis University, Budapest, Hungary)
  • László DÉTÁRI (Eötvös Loránd University, Budapest, Hungary)
  • Zoltán GIRICZ (Semmelweis University, Budapest, Hungary and Pharmahungary Group, Szeged, Hungary)
  • Zoltán HANTOS (Semmelweis University, Budapest and University of Szeged, Hungary)
  • Zoltán HEROLD (Semmelweis University, Budapest, Hungary) 
  • László HUNYADI (Semmelweis University, Budapest, Hungary)
  • Gábor JANCSÓ (University of Pécs, Hungary)
  • Zoltán KARÁDI (University of Pecs, Hungary)
  • Miklós PALKOVITS (Semmelweis University, Budapest, Hungary)
  • Gyula PAPP (University of Szeged, Hungary)
  • Gábor PAVLIK (University of Physical Education, Budapest, Hungary)
  • András SPÄT (Semmelweis University, Budapest, Hungary)
  • Gyula SZABÓ (University of Szeged, Hungary)
  • Zoltán SZELÉNYI (University of Pécs, Hungary)
  • Lajos SZOLLÁR (Semmelweis University, Budapest, Hungary)
  • Gyula TELEGDY (MTA-SZTE, Neuroscience Research Group and University of Szeged, Hungary)
  • József TOLDI (MTA-SZTE Neuroscience Research Group and University of Szeged, Hungary)
  • Árpád TÓSAKI (University of Debrecen, Hungary)

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  • Helmut G. HINGHOFER-SZALKAY (Medical University of Graz, Austria)
  • Tibor HORTOBÁGYI (University of Groningen, Netherlands)
  • George KUNOS (National Institutes of Health, Bethesda, USA)
  • Massoud MAHMOUDIAN (Iran University of Medical Sciences, Tehran, Iran)
  • Tadaaki MANO (Gifu University of Medical Science, Japan)
  • Luis Gabriel NAVAR (Tulane University School of Medicine, New Orleans, USA)
  • Hitoo NISHINO (Nagoya City University, Japan)
  • Ole H. PETERSEN (Cardiff University, UK)
  • Ulrich POHL (German Centre for Cardiovascular Research and Ludwig-Maximilians-University, Planegg, Germany)
  • Andrej A. ROMANOVSKY (University of Arizona, USA)
  • Anwar Ali SIDDIQUI (Aga Khan University, Karachi, Pakistan)
  • Csaba SZABÓ (University of Fribourg, Switzerland)
  • Eric VICAUT (Université de Paris, UMRS 942 INSERM, France)
  • Nico WESTERHOF (Vrije Universiteit Amsterdam, The Netherlands)

 

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2022  
Web of Science  
Total Cites
WoS
335
Journal Impact Factor 1.4
Rank by Impact Factor

Physiology (Q4)

Impact Factor
without
Journal Self Cites
1.4
5 Year
Impact Factor
1.6
Journal Citation Indicator 0.42
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Physiology (Q4)

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Physiology (medical) (Q3)
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Scopus
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Physiology 68/102 (33rd PCTL)
Scopus
SNIP
0.508

2021  
Web of Science  
Total Cites
WoS
330
Journal Impact Factor 1,697
Rank by Impact Factor

Physiology 73/81

Impact Factor
without
Journal Self Cites
1,697
5 Year
Impact Factor
1,806
Journal Citation Indicator 0,47
Rank by Journal Citation Indicator

Physiology 69/86

Scimago  
Scimago
H-index
31
Scimago
Journal Rank
0,32
Scimago Quartile Score Medicine (miscellaneous) (Q3)
Physiology (medical) (Q3)
Scopus  
Scopus
Cite Score
2,7
Scopus
CIte Score Rank
Physiology (medical) 69/101 (Q3)
Scopus
SNIP
0,591

 

2020  
Total Cites 245
WoS
Journal
Impact Factor
2,090
Rank by Physiology 62/81 (Q4)
Impact Factor  
Impact Factor 1,866
without
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5 Year 1,703
Impact Factor
Journal  0,51
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Rank by Journal  Physiology 67/84 (Q4)
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Citable 42
Items
Total 42
Articles
Total 0
Reviews
Scimago 29
H-index
Scimago 0,417
Journal Rank
Scimago Physiology (medical) Q3
Quartile Score  
Scopus 270/1140=1,9
Scite Score  
Scopus Physiology (medical) 71/98 (Q3)
Scite Score Rank  
Scopus 0,528
SNIP  
Days from  172
submission  
to acceptance  
Days from  106
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2019  
Total Cites
WoS
137
Impact Factor 1,410
Impact Factor
without
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1,361
5 Year
Impact Factor
1,221
Immediacy
Index
0,294
Citable
Items
34
Total
Articles
33
Total
Reviews
1
Cited
Half-Life
2,1
Citing
Half-Life
9,3
Eigenfactor
Score
0,00028
Article Influence
Score
0,215
% Articles
in
Citable Items
97,06
Normalized
Eigenfactor
0,03445
Average
IF
Percentile
12,963
Scimago
H-index
27
Scimago
Journal Rank
0,267
Scopus
Scite Score
235/157=1,5
Scopus
Scite Score Rank
Physiology (medical) 73/99 (Q3)
Scopus
SNIP
0,38

 

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Physiology International
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