mass-spectrometry-congress-2019-posters-abstracts

2 / 12

Page 44
May 20-21, 2019 | Rome, Italy
OF EXCELLENCE
IN INTERNATIONAL
MEETINGS
YEARS
Journal of Chemical Technology and Applications | Volume 3
MASS SPECTROMETRY,
PROTEOMICS AND POLYMER CHEMISTRY
3rd International Conference on
Mass Spectrometry Congress 2019
Ferko M et al., J Chem Tech App 2019, Volume 3
PROTEOMIC ANALYSIS OF MITOCHONDRIAL PERMEABILITY TRANSITION PORES IN RE-
LATION TO CARDIOPROTECTION INDUCED BY METABOLIC PRECONDITIONING
Ferko M 1, Andelová N1, Szeiffová Bačová B 1 and Waczulíková I2
1 Slovak Academy of Sciences, Slovak Republic
2 Comenius University, Slovak Republic
Introduction: Mitochondrial permeability transition pores (mPTPs) are associated with cell death regulation,
but also perform physiological role during calcium homeostasis, bioenergetics and redox signalling of cardiac
mitochondria. Metabolic preconditioning (MPC) is an experimental cardioprotective model that has demon-
strated sufficient protection to compensate for the mitochondrial energy of the heart under pathological con-
ditions.
Aim: The purpose is to clarify regulatory components of the mPTP complex by means of proteomic analysis
and using mass spectrometry. We have focused also on mitochondrial creatine kinase (mtCK) as one of the
proposed mPTP regulators.
Materials & Methods: Proteomic analysis was performed using nano high performance liquid chromatog-
raphy and mass spectrometry (ion mass spectrometer configured with electrospray ionization source (ESI)).
Mitochondrial proteins were separated by 1D gel electrophoresis and in-gel trypsin digestion. Male Wistar
rats were used for this study. Heart mitochondria were isolated by means of differential centrifugation. MPC
was induced for 8-days using single dose of streptozotocin (65 mg/kg b. wt.). At the level of using proteomic
analysis, we have focused on proteins currently considered as structural and regulatory components of mPTP.
The abundance of the investigated proteins as a whole was significantly lower in the MPC affected group (p
= 0.048), expressions of individual proteins expressed by fold change parameter were maintained (analysed
using TREAT (t-tests relative to a threshold) procedure). An important outcome in terms of cardioprotective
regulation is that remaining identified mPTP proteins retained expression at the level of healthy mitochondria
without significant change. MPC has been able to preserve the activity of mtCK, one of the key enzymes in the
energy metabolism.
Results: The results of proteomic analysis under MPC conditions indicate the positive effect of mPTP regulated
mechanisms present in the state of increased calcium influx into the mitochondria, thereby contributing to the
maintenance of the energy of the pathologically affected myocardium.
Ferko M is a researcher who is working at the Department of Biochemistry, Centre of Experimental Medicine SAS as an in charge of
the mass spectrometry and fluorescence spectroscopy laboratory. He has 23 publications on the topics like heart mitochondria and
cardiac adaptation, endogenous cardioprotection and mitochondrial proteomic analysis published in various journals that have
been cited 100 times and his H-index is 11. He is expertise in heart mitochondria proteomic analysis, LC/MS, heart mitochondria
function, bioenergetics, heart failure and cardiovascular physiology.
BIOGRAPHY