The search for potential hypotensive peptides in the amino acid sequence of human renalase and their identification in proteolytic fragments of this protein

  
Fedchenko V.I.1, Veselovsky A.V.1, .Kopylov A.T1, Medvedev A.E.1

1. Institute of Biomedical Chemistry, Moscow, Russia
Section: Experimental Study
DOI: 10.18097/PBMC20236906403      PubMed Id: 38153055
Year: 2023  Volume: 69  Issue: 6  Pages: 403-408
Renalase (RNLS) is a secretory protein discovered in 2005. It plays an important role in the regulation of blood pressure. Studies by two independent laboratories have shown that administration of purified recombinant RNLS reduced blood pressure in experimental animals. However, the mechanisms of the antihypertensive effect of RNLS still remain unclear, especially in the context of the shift in the catalytic paradigm of this protein. In addition, there is growing evidence that endogenous plasma/serum RNLS, detected by enzyme immunoassay, is not an intact protein secreted into the extracellular space, and exogenous recombinant RNLS is effectively cleaved during short-term incubation with human plasma samples. This suggests that the antihypertensive effect of RNLS may be due to peptides formed during proteolytic processing. Based on the results of a bioinformatics analysis of potential RNLS cleavage sites (Fedchenko et al., Medical Hypotheses, 2022; DOI: 10.1016/j.mehy.2022.110895), a number of short peptides have been identified in the RNLS sequence that show similarity to fragments of known peptide inhibitors of angiotensin-converting enzyme. Some of them were found as a part of larger RNLS peptides, formed during RNLS cleavage by chymotrypsin and, and to a lesser extent, by trypsin.
Download PDF:  
Keywords: renalase, proteolytic processing, renalase peptides, biological activity, peptide inhibitors of angiotensin-converting enzyme
Supplementary materials:
Citation:

Fedchenko, V. I., Veselovsky, A. V., . Kopylov, A. T,, Medvedev, A. E. (2023). The search for potential hypotensive peptides in the amino acid sequence of human renalase and their identification in proteolytic fragments of this protein. Biomeditsinskaya Khimiya, 69(6), 403-408.
References  
 2024 (vol 70)
 2023 (vol 69)
 2022 (vol 68)
 2021 (vol 67)
 2020 (vol 66)
 2019 (vol 65)
 2018 (vol 64)
 2017 (vol 63)
 2016 (vol 62)
 2015 (vol 61)
 2014 (vol 60)
 2013 (vol 59)
 2012 (vol 58)
 2011 (vol 57)
 2010 (vol 56)
 2009 (vol 55)
 2008 (vol 54)
 2007 (vol 53)
 2006 (vol 52)
 2005 (vol 51)
 2004 (vol 50)
 2003 (vol 49)