Therapeutic Perspectives of Adenosine Deaminase Inhibition in Cardiovascular Diseases
Department of Biochemistry, Medical University of Gdansk, Debinki 1 St., 80-211 Gdansk, Poland
*
Authors to whom correspondence should be addressed.
Academic Editors: Luigi A. Agrofoglio, Vincent Roy and Cyril Nicolas
Molecules 2020, 25(20), 4652; https://doi.org/10.3390/molecules25204652
Received: 31 August 2020
/
Revised: 2 October 2020
/
Accepted: 7 October 2020
/
Published: 12 October 2020
(This article belongs to the Special Issue Nucleosides – Nucleotides – Oligonucleotides)
Adenosine deaminase (ADA) is an enzyme of purine metabolism that irreversibly converts adenosine to inosine or 2′deoxyadenosine to 2′deoxyinosine. ADA is active both inside the cell and on the cell surface where it was found to interact with membrane proteins, such as CD26 and adenosine receptors, forming ecto-ADA (eADA). In addition to adenosine uptake, the activity of eADA is an essential mechanism that terminates adenosine signaling. This is particularly important in cardiovascular system, where adenosine protects against endothelial dysfunction, vascular inflammation, or thrombosis. Besides enzymatic function, ADA protein mediates cell-to-cell interactions involved in lymphocyte co-stimulation or endothelial activation. Furthermore, alteration in ADA activity was demonstrated in many cardiovascular pathologies such as atherosclerosis, myocardial ischemia-reperfusion injury, hypertension, thrombosis, or diabetes. Modulation of ADA activity could be an important therapeutic target. This work provides a systematic review of ADA activity and anchoring inhibitors as well as summarizes the perspectives of their therapeutic use in cardiovascular pathologies associated with increased activity of ADA.
View Full-Text
Keywords:
adenosine deaminase; ADA; inhibition; therapy; inflammation; atherosclerosis; myocardial infarction; thrombosis; hypertension; type II diabetes mellitus
▼
Show Figures
Figure 1
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited
MDPI and ACS Style
Kutryb-Zajac, B.; Mierzejewska, P.; Slominska, E.M.; Smolenski, R.T. Therapeutic Perspectives of Adenosine Deaminase Inhibition in Cardiovascular Diseases. Molecules 2020, 25, 4652. https://doi.org/10.3390/molecules25204652
AMA Style
Kutryb-Zajac B, Mierzejewska P, Slominska EM, Smolenski RT. Therapeutic Perspectives of Adenosine Deaminase Inhibition in Cardiovascular Diseases. Molecules. 2020; 25(20):4652. https://doi.org/10.3390/molecules25204652
Chicago/Turabian StyleKutryb-Zajac, Barbara, Paulina Mierzejewska, Ewa M. Slominska, and Ryszard T. Smolenski. 2020. "Therapeutic Perspectives of Adenosine Deaminase Inhibition in Cardiovascular Diseases" Molecules 25, no. 20: 4652. https://doi.org/10.3390/molecules25204652
Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.
