Tag Archives: myoglobin
The level of inflammatory markers in patients with myocardial infarction after percutaneous coronary intervention
Hadeel S. Abd-Alwahab1, Bayadir Abdul Hussein Mahmeed1,
Nesreen Ahmed Nasser1, Osama A. Mohsein2,3*
1College of Medicine, Al-Nahrain University, Baghdad, Iraq;
2Main Laboratory Unit, Al Habbobi Teaching Hospital,
Thi-Qar Health Directorate, Thi-Qar, Iraq;
3Department of Medical Laboratory Techniques,
Mazaya University College, Thi-Qar, Iraq;
*e-mail: osamaakram889@gmail.com
Received: 04 April 2024; Revised: 20 June 2024;
Accepted: 25 July 2024; Available on-line: 04 September 2024
Cardiovascular diseases are among the most widespread diseases in the world that affect all ages and sometimes can lead to death. Atherosclerosis, coronary syndrome and myocardial infarction are usually associated with artery occlusion and require percutaneous coronary intervention (PCI) as a non-surgical procedure to restore blood flow to the heart. Inflammatory biomarkers, especially interleukins and cardiac biomarkers, have an important role in diagnosing the state of patients with heart damage. The goal of the study was to estimate the serum levels of interleukins and cardiac biomarkers after PCI to reduce the risk of acute coronary syndrome. The study included 100 persons between the ages of 40 and 69 diagnosed with acute coronary syndrome who had successful PCI and a control group consisting of 50 healthy participants of the same age. The levels of interleukins, сreatine kinase MB and myoglobin were measured using an enzyme-linked immunosorbent assay. Troponin and D-dimer levels were measured using immunoassay. It was found that patients before PCI had significantly higher levels of IL-1β, IL-6, IL-8, cardiac troponin I, D-dimer, creatine kinase-MB and myoglobin compared to the control group. One day after PCI, the levels of IL -6, IL-8, cardiac troponin I and D-dimer remained elevated. One week after PCI, the levels of IL-1β, IL-6, IL-8, CK-MB and myoglobin did not show significant differences compared to the control group, while the levels of cardiac troponin I and D-dimer remained higher. Results obtained indicate that in patients after PCI, the levels of interleukins decreased, indicating the reduction of inflammatory processes, but cardiac damage persists to a certain degree, even a week after PCI.
The contribution of Nobel prize laureates to research of the protein structure: J. Sumner, J. Northrop, W. Stanley, L. Pauling, F. Sanger, M. Perutz, J. Kendrew
V. M. Danilova, R. P. Vynogradova, S. V. Komisarenko
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: valdan@biochem.kiev.ua
Received: 11 Match 2020; Accepted: 15 May 2020
The second half of the 20th century was marked by remarkable discoveries in the chemistry and biochemistry of proteins, in particular, in establishing the protein structure. James Sumner, John Northrop, and Wendell Stanley, the Nobel Laureates in chemistry in 1946, were the first to isolate individual enzymes and viruses in a pure crystalline form and prove their protein nature, thereby making an invaluable scientific contribution to the development of important biological disciplines such as biochemistry, enzymology, virology, and molecular biology. A significant contribution to understanding chemical bonding in the formation of the different levels of a protein structure was made by Linus Pauling – a prominent American scientist of the 20th century. He was awarded the Nobel Prize in Chemistry in 1954 “for his research into the nature of the chemical bond and its application to the elucidation of the structure of complex substances”. Biochemists know him well as the author of the secondary structure of proteins – the α-helix and the β-sheet. Frederick Sanger, a two-time Nobel Prize winner (1958 and 1980), was the first among researchers who determined the primary amino acid sequence of a protein, for example, of two insulin polypeptide chains A and B. F. Sanger proved that the sequence nature of proteins’ structures is analogous to that of gene sequences in the DNA, and thus, the same principles may be applied. The difficult question of how a protein molecule is arranged in space was answered by the English biochemists Max F. Perutz and John C. Kendrew. They determined the three-dimensional structure of hemoglobin and myoglobin proteins by X-ray diffraction and were awarded the Nobel Prize in Chemistry in 1962 “for their studies of the structures of globular proteins”.