Interaction of kidney proteins of normal and hypertensive rats with fragments of renalase peptide RP220

Renalase (RNLS) is a protein involved in the regulation of blood pressure; it has various functions inside and outside cells. The twenty-membered peptide RP220, corresponding to the amino acid sequence of human RNLS 220-239, reproduces a number of effects of extracellular RNLS and can bind to many i...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:Biomeditsinskaia khimiia Ročník 71; číslo 2; s. 103
Hlavní autoři: Buneeva, O A, Fedchenko, V I, Kaloshina, S A, Zavyalova, M G, Zgoda, V G, Medvedev, A E
Médium: Journal Article
Jazyk:angličtina
Vydáno: Russia (Federation) 01.03.2025
Témata:
Amino Acid Sequence
Animals
Humans
Hypertension - metabolism
Hypertension - pathology
Kidney - metabolism
Kidney - pathology
Male
Monoamine Oxidase
Neprilysin - chemistry
Neprilysin - metabolism
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Proteomics
Rats
Rats, Inbred SHR
Rats, Inbred WKY
arterial hypertension
renalase
WKY and SHR rats
and RP233-239
proteomic profiling of kidney tissue
renalase peptides RP220
RP224-232
ISSN:2310-6972
On-line přístup:Zjistit podrobnosti o přístupu
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
Popis
Shrnutí:Renalase (RNLS) is a protein involved in the regulation of blood pressure; it has various functions inside and outside cells. The twenty-membered peptide RP220, corresponding to the amino acid sequence of human RNLS 220-239, reproduces a number of effects of extracellular RNLS and can bind to many intracellular proteins in the kidney. The RP220 sequence contains several cleavage sites for extracellular proteases, which could potentially produce RP224-232 and RP233-239 peptides. The aim of this work was to perform proteomic profiling of kidney tissue from normotensive Wistar Kyoto (WKY) rats and spontaneously hypertensive rats (SHR) derived from WKY, using potential proteolytic fragments (RP224-232 and RP233-239) of the RP220 peptide as affinity ligands, and to compare these proteomic profiles with the profiles obtained using the parent RP220 peptide. The obtained results indicate that the relative content of proteins bound to the RNLS peptides in SHR, compared to that in WKY rats, changes most significantly in the case of the RP224-232 peptide. Almost all of these proteins, with a few exceptions, are associated with cardiovascular pathology, many with hypertension. The results of our work indicate that proteolytic processing of RP220 does not lead to the inactivation of this peptide, but to a change in its ligand/regulatory properties, as well as the repertoire of potential protein partners and, consequently, protein-protein interactions that may have possible pharmacological application.
Bibliografie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:2310-6972
DOI:10.18097/PBMCR1567