Thermal heliox proteome. High-temperature heliox does not cause destruction of human respiratory system cells

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Abstract


Aim. Conducting a pilot study to assess the effect of thermal heliox on the state of the respiratory tract by studying of the exhaled breath condensate protein composition before the thermal heliox procedure, immediately after and after three hours of relaxation

Materials and methods. A comparative study of the exhaled breath condensates (EBC) protein composition of five non-smoking healthy donors was carried out. The EBC was taken before the respiratory procedure, immediately after a 20-minute inhalation by mixture of He/O2 gases (70/30) heated to 70°C and 3 hours later. The protein composition was determined by chromatography-mass spectrometric analysis after selective tryptic hydrolysis. The results were processed using the Mascot program and the UniProt database.

Results. After the heliox procedure, the volume of the collected condensate (1–1.5 ml) decreases by an average of 32% and is practically restored after three hours of relaxation. Most proteins were consistent for all samples, regardless of the thermal heliox procedure. These are keratins, several proteins of the immune system (immunoglobulins, compliment proteins), tubulin. In samples after thermal heliox, the appearance of small amounts of additional proteins is observed. These are proteins of muscle metabolism (actin and calmodulin), fibrinogen, traces of hemoglobin, apolipoprotein, type B creatine kinase. After three hours of relaxation, tubulin disappears in the EBC.

Conclusion. Most exhaled proteins are the same before, after the procedure, and for three hours of relaxation. The results obtained demonstrate the relative safety of the use of high temperature heliox as a therapeutic agent.


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About the authors

Sergey D. Varfolomeev

Lomonosov Moscow State University; Emanuel Institute of Biochemical Physics

Email: amryabokon@gmail.com

Russian Federation, Moscow

чл.-кор. РАН, д.х.н., проф., дир. Института физико-химических основ функционирования сети нейронов и искусственного интеллекта; науч. рук.

Aleksander A. Panin

Medtechinnovations

Email: amryabokon@gmail.com

Russian Federation, Moscow

д.э.н, ген. дир.

Anna M. Ryabokon

Lomonosov Moscow State University; Emanuel Institute of Biochemical Physics

Author for correspondence.
Email: amryabokon@gmail.com
ORCID iD: 0000-0001-9043-9129

Russian Federation, Moscow

к.х.н., науч. сотр. каф. химической энзимологии химического фак-та; ст. науч. сотр.

Anna S. Kozyr

Emanuel Institute of Biochemical Physics

Email: amryabokon@gmail.com
ORCID iD: 0000-0001-6723-2963

Russian Federation, Moscow

аспирант

Aleksey S. Kononikhin

Emanuel Institute of Biochemical Physics

Email: amryabokon@gmail.com
ORCID iD: 0000-0002-2238-3458

Russian Federation, Moscow

к.ф.-м.н., ст. науч. сотр

Lyudmila V. Shogenova

Pirogov Russian National Research Medical University; Pletnev City Clinical Hospital

Email: amryabokon@gmail.com

Russian Federation, Moscow

к.м.н., доц. каф. госпитальной терапии педиатрического фак-та; врач анестезиолог-реаниматолог отд-ния реанимации и интенсивной терапии

 

Aleksander G. Chuchalin

Pirogov Russian National Research Medical University

Email: amryabokon@gmail.com
ORCID iD: 0000-0002-5070-5450

Russian Federation, Moscow

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