Electromagnetic fields with 217 Hz and 0.2 mT as hazardous factors for tubulin structure and assembly (in vitro study)

Afrasiabi, Ali; Riazi, Gholamhossein; Dadras, Ali; Tavili, Elaheh; Ghalandari, Behafarid; Naghshineh, Ali; Mobasheri, Hamid; Ahmadian, Shahin

doi:10.1007/s13738-013-0398-y

Cited by 5 publications

(9 citation statements)

References 54 publications

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“…Their results on the secondary structure composition of tubulin dimers are presented in the lower portion of Table 4. We find agreement with the results of both analyses reported by de Pereda et al [108] for all secondary structures, as well as with those reported in the study by Afrasiabi et al [109] for α-helices and β-sheets. The discrepancy between our average result for random coil structures and that reported by Afrasiabi et al appears to be due to their analysis not separately quantifying β-turns; integrating our β-turn and random coil results yields no statistically significant difference compared with their random coil result (p = 0.0972).…”

Section: Raman Spectra and Secondary Structures Of Polymerized Unexpo...supporting

confidence: 93%

“…Various studies in the literature also highlight interesting ways in which electromagnetic stimuli can induce conformational changes in proteins [109,[114][115][116][117][118][119]. For instance, using X-ray crystallography, Lundholm et al observed terahertz-radiation-induced (0.4 THz, 62 mW/cm 2 ) steady-state secondary structure changes in lysozymes characterized by α-helix compression, which the authors attributed to resonant interactions [116].…”

Section: Discussionmentioning

confidence: 99%

“…Several other studies in the literature have analyzed the conformation of tubulin dimers using different spectroscopic techniques. We compared our results with three such studies: Ventilla et al [107], which employed far-UV CD spectroscopy; de Pereda et al [108], which included two independent analyses using both far-UV CD spectroscopy and FTIR spectroscopy; and finally, Afrasiabi et al [109], which also utilized far-UV CD spectroscopy. Their results on the secondary structure composition of tubulin dimers are presented in the lower portion of Table 4.…”

Section: Raman Spectra and Secondary Structures Of Polymerized Unexpo...mentioning

confidence: 99%

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Raman Spectroscopy Reveals Photobiomodulation-Induced α-Helix to β-Sheet Transition in Tubulins: Potential Implications for Alzheimer’s and Other Neurodegenerative Diseases

Di Gregorio,

Staelens,

Hosseinkhah

et al. 2024

Nanomaterials

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In small clinical studies, the application of transcranial photobiomodulation (PBM), which typically delivers low-intensity near-infrared (NIR) to treat the brain, has led to some remarkable results in the treatment of dementia and several neurodegenerative diseases. However, despite the extensive literature detailing the mechanisms of action underlying PBM outcomes, the specific mechanisms affecting neurodegenerative diseases are not entirely clear. While large clinical trials are warranted to validate these findings, evidence of the mechanisms can explain and thus provide credible support for PBM as a potential treatment for these diseases. Tubulin and its polymerized state of microtubules have been known to play important roles in the pathology of Alzheimer’s and other neurodegenerative diseases. Thus, we investigated the effects of PBM on these cellular structures in the quest for insights into the underlying therapeutic mechanisms. In this study, we employed a Raman spectroscopic analysis of the amide I band of polymerized samples of tubulin exposed to pulsed low-intensity NIR radiation (810 nm, 10 Hz, 22.5 J/cm2 dose). Peaks in the Raman fingerprint region (300–1900 cm−1)—in particular, in the amide I band (1600–1700 cm−1)—were used to quantify the percentage of protein secondary structures. Under this band, hidden signals of C=O stretching, belonging to different structures, are superimposed, producing a complex signal as a result. An accurate decomposition of the amide I band is therefore required for the reliable analysis of the conformation of proteins, which we achieved through a straightforward method employing a Voigt profile. This approach was validated through secondary structure analyses of unexposed control samples, for which comparisons with other values available in the literature could be conducted. Subsequently, using this validated method, we present novel findings of statistically significant alterations in the secondary structures of polymerized NIR-exposed tubulin, characterized by a notable decrease in α-helix content and a concurrent increase in β-sheets compared to the control samples. This PBM-induced α-helix to β-sheet transition connects to reduced microtubule stability and the introduction of dynamism to allow for the remodeling and, consequently, refreshing of microtubule structures. This newly discovered mechanism could have implications for reducing the risks associated with brain aging, including neurodegenerative diseases like Alzheimer’s disease, through the introduction of an intervention following this transition.

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Section: Raman Spectra and Secondary Structures Of Polymerized Unexpo...supporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Raman Spectra and Secondary Structures Of Polymerized Unexpo...mentioning

confidence: 99%

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Raman Spectroscopy Reveals Photobiomodulation-Induced α-Helix to β-Sheet Transition in Tubulins: Potential Implications for Alzheimer’s and Other Neurodegenerative Diseases

Di Gregorio,

Staelens,

Hosseinkhah

et al. 2024

Nanomaterials

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“…In addition, microwaves could change the conformation of proteins that could take the form of a direct interaction of the electromagnetic fields with the proteins or its water of hydration [49]. As microtubules are key proteins that participate in mitosis, secretion of hormones [12], sperm motility [10], cell division, axonal transportation, and neuronal signal transduction [50], it is interesting to examine the effect of electromagnetic fields on microtubule structure and function.…”

Section: Discussionmentioning

confidence: 99%

“…This phenomenon leads to alter bending angle of α and β tubulin dimers which are necessary for tubulin-tubulin assembly for microtubule establishment [10]. In addition, it is possible that ELEF may affect electron clouds around tubulin dimers by changing the unpaired electrons of hydrophobic regions, and therefore, enhanced microtubule stability [10, 50].…”

Section: Discussionmentioning

confidence: 99%

Comparison of polymerization and structural behavior of microtubules in rat brain and sperm affected by the extremely low-frequency electromagnetic field

Gholami

Riazi

Fathi

et al. 2019

BMC Mol and Cell Biol

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Background: Microtubule proteins are able to produce electromagnetic fields and have an important role in memory formation, and learning. Therefore, microtubules have the potential to be affected by exogenous electromagnetic fields. This study aimed to examine the comparison of microtubule polymerization and its structural behavior in brain and sperm affected by 50 Hz extremely low-frequency electromagnetic field (ELEF). Results: Twenties adult male rats were randomly and equally divided into control and experimental groups, to evaluate the effect of 50 Hz ELEF on the sperm and brain functions. Plus-maze, serum testosterone and corticosterone, and sperm evaluation were performed. Next, the semen and brain samples were obtained, and they were divided into four experimental groups for investigation of microtubule polymerization. There was no significant difference in testosterone and, corticosterone levels, anxiety behaviors, and sperm morphology between control and ELEF-exposure groups. The sperm viability, total and progressive motility were significantly higher in the ELEF-exposed group than that of the control group. The microtubule polymerization in sperm ELEF was significantly higher than in other groups. The secondary and tertiary structures of tubulins were significantly affected in the brain, and sperm ELEF groups. Conclusion: It seems that the polymerization of microtubules and conformational changes of tubulin dimers are improved by ELEF application.

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Variations of Glutamate Concentration Within Synaptic Cleft in the Presence of Electromagnetic Fields: An Artificial Neural Networks Study

et al. 2015

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Glutamate is an excitatory neurotransmitter that is released by the majority of central nervous system synapses and is involved in developmental processes, cognitive functions, learning and memory. Excessive elevated concentrations of Glu in synaptic cleft results in neural cell apoptosis which is called excitotoxicity causing neurodegenerative diseases. Hence, we investigated the possibility of extremely low frequency electromagnetic fields (ELF-EMF) as a risk factor which is able to change Glu concentration in synaptic clef. Synaptosomes as a model of nervous terminal were exposed to ELF-EMF for 15-55 min in flux intensity range from 0.1 to 2 mT and frequency range from 50 to 230 Hz. Finally, all raw data by INForm v4.02 software as an artificial neural network program was analyzed to predict the effect of whole mentioned range spectra. The results showed the tolerance of all effects between the ranges from -35 to +40 % compared to normal state when glutamatergic systems exposed to ELF-EMF. It indicates that glutamatergic system attempts to compensate environmental changes though release or reuptake in order to keep the system safe. Regarding to the wide range of ELF-EMF acquired in this study, the obtained outcomes have potential for developing treatments based on ELF-EMF for some neurological diseases; however, in vivo experiments on the cross linking responses between glutamatergic and cholinergic systems in the presence of ELF-EMF would be needed.

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Electromagnetic fields with 217 Hz and 0.2 mT as hazardous factors for tubulin structure and assembly (in vitro study)

Cited by 5 publications

References 54 publications

Raman Spectroscopy Reveals Photobiomodulation-Induced α-Helix to β-Sheet Transition in Tubulins: Potential Implications for Alzheimer’s and Other Neurodegenerative Diseases

Raman Spectroscopy Reveals Photobiomodulation-Induced α-Helix to β-Sheet Transition in Tubulins: Potential Implications for Alzheimer’s and Other Neurodegenerative Diseases

Comparison of polymerization and structural behavior of microtubules in rat brain and sperm affected by the extremely low-frequency electromagnetic field

Variations of Glutamate Concentration Within Synaptic Cleft in the Presence of Electromagnetic Fields: An Artificial Neural Networks Study

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