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...
Uloženo v:
| Vydáno v: | Biomeditsinskaia khimiia Ročník 71; číslo 2; s. 103 |
|---|---|
| Hlavní autoři: | , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
Russia (Federation)
01.03.2025
|
| Témata: | |
| ISSN: | 2310-6972 |
| On-line přístup: | Zjistit podrobnosti o přístupu |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | 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. |
|---|---|
| AbstractList | 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.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. 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. |
| Author | Fedchenko, V I Medvedev, A E Kaloshina, S A Zavyalova, M G Buneeva, O A Zgoda, V G |
| Author_xml | – sequence: 1 givenname: O A surname: Buneeva fullname: Buneeva, O A organization: Institute of Biomedical Chemistry, Moscow, Russia – sequence: 2 givenname: V I surname: Fedchenko fullname: Fedchenko, V I organization: Institute of Biomedical Chemistry, Moscow, Russia – sequence: 3 givenname: S A surname: Kaloshina fullname: Kaloshina, S A organization: Institute of Biomedical Chemistry, Moscow, Russia – sequence: 4 givenname: M G surname: Zavyalova fullname: Zavyalova, M G organization: Institute of Biomedical Chemistry, Moscow, Russia – sequence: 5 givenname: V G surname: Zgoda fullname: Zgoda, V G organization: Institute of Biomedical Chemistry, Moscow, Russia – sequence: 6 givenname: A E surname: Medvedev fullname: Medvedev, A E organization: Institute of Biomedical Chemistry, Moscow, Russia |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/40326017$$D View this record in MEDLINE/PubMed |
| BookMark | eNo1kL1OwzAYRT0U0VK68ADII0vAduzYHqHip1IRVQVz5MRfWovECbYL6ttToExXujq60j1naOR7DwhdUHJNFdHyZnX3PF9TUcgRmrCckqzQko3RLEZXEcapFlzpUzTmJGcFoXKCNgufIJg6ud7jvsHvznrY4yH0CZyPP5XvQ2dabLzF2_0AIYGP7hNwMCniL5e2uAlm04FPv3gAb1oTAQ8wJGcBr1eMkXN00pg2wuyYU_T2cP86f8qWL4-L-e0yq6nWMsurhhhJgLCm5jQXBVOacNCacWMU5VqAUrqqZWG5FQUIDblqtKyAgLC2YlN09bd7ePCxg5jKzsUa2tZ46HexzBkhisqDjAN6eUR3VQe2HILrTNiX_3LYN8HAZok |
| ContentType | Journal Article |
| DBID | CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.18097/PBMCR1567 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | no_fulltext_linktorsrc |
| ExternalDocumentID | 40326017 |
| Genre | Journal Article |
| GroupedDBID | 53G CGR CUY CVF ECM EIF NPM 7X8 |
| ID | FETCH-LOGICAL-c1997-3bf0a70e02fc4135628904e9924aa81495e889bc76d4d56e59e38f97be0e5ddb2 |
| IEDL.DBID | 7X8 |
| ISSN | 2310-6972 |
| IngestDate | Wed May 07 05:46:08 EDT 2025 Wed May 07 07:46:20 EDT 2025 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 2 |
| Keywords | arterial hypertension renalase WKY and SHR rats and RP233-239 proteomic profiling of kidney tissue renalase peptides RP220 RP224-232 |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c1997-3bf0a70e02fc4135628904e9924aa81495e889bc76d4d56e59e38f97be0e5ddb2 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | http://pbmc.ibmc.msk.ru/pdf/PBMC-2025-71-2-103 |
| PMID | 40326017 |
| PQID | 3200817024 |
| PQPubID | 23479 |
| ParticipantIDs | proquest_miscellaneous_3200817024 pubmed_primary_40326017 |
| PublicationCentury | 2000 |
| PublicationDate | 2025-Mar |
| PublicationDateYYYYMMDD | 2025-03-01 |
| PublicationDate_xml | – month: 03 year: 2025 text: 2025-Mar |
| PublicationDecade | 2020 |
| PublicationPlace | Russia (Federation) |
| PublicationPlace_xml | – name: Russia (Federation) |
| PublicationTitle | Biomeditsinskaia khimiia |
| PublicationTitleAlternate | Biomed Khim |
| PublicationYear | 2025 |
| SSID | ssib024195489 ssib040281610 ssib025541122 |
| Score | 2.3120499 |
| Snippet | Renalase (RNLS) is a protein involved in the regulation of blood pressure; it has various functions inside and outside cells. The twenty-membered peptide... |
| SourceID | proquest pubmed |
| SourceType | Aggregation Database Index Database |
| StartPage | 103 |
| SubjectTerms | 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 |
| Title | Interaction of kidney proteins of normal and hypertensive rats with fragments of renalase peptide RP220 |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/40326017 https://www.proquest.com/docview/3200817024 |
| Volume | 71 |
| hasFullText | |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LS8NAEF7UevDiA1_1xQpeg2s26e6eRIviwZZSVHorye6kFmVTGxX8985s03oSBC85hATCZHbmm9c3jJ1lMm3p1IkotdZECdq_KM9BRBBnIKVMEhm2KDzdq25XDwamVyfcqrqtcm4Tg6F2paUc-bmkQv2FQpdyOXmLaGsUVVfrFRrLrCERypBWq8FCn9A5EZ3Zwl0jek4QXizcOYZOGgGPCPvn0By1jIprBlNNxI696067j_GN-h19Bi90u_Hf799k6zX-5FczhdliS-C32SjkBWcjDrws-MvYefjigcNh7Cu65QnbvvLMO_6Moeu0bnznqEAVp2QuL6bZKMzL0eNT8DSgCXxCXTMOeL8Xx2KHPd7ePLTvonoDQ2QDTavMC5EpASIuLHo7xEraiAQMBm1Zpim4Aq1NblXLJS5tQWpA6sIo_NuQOpfHu2zFlx72GScoRkw2sULB2zzHg6-UU9Lp1IIpZJOdzuU2RA2nskXmofyohj-Sa7K9mfCHkxkVxzARkjjR1MEf3j5kazEt7w0NZEesUeD5hmO2aj_fx9X0JKgOXru9zjeAecpN |
| linkProvider | ProQuest |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Interaction+of+kidney+proteins+of+normal+and+hypertensive+rats+with+fragments+of+renalase+peptide+RP220&rft.jtitle=Biomeditsinskaia+khimiia&rft.au=Buneeva%2C+O+A&rft.au=Fedchenko%2C+V+I&rft.au=Kaloshina%2C+S+A&rft.au=Zavyalova%2C+M+G&rft.date=2025-03-01&rft.issn=2310-6972&rft.volume=71&rft.issue=2&rft.spage=103&rft_id=info:doi/10.18097%2FPBMCR1567&rft_id=info%3Apmid%2F40326017&rft_id=info%3Apmid%2F40326017&rft.externalDocID=40326017 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2310-6972&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2310-6972&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2310-6972&client=summon |