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  1. Article: The Synthetic Peptide LyeTx I mn∆K, Derived from

    Vieira, Ana Paula Gonçalves Coelho / de Souza, Amanda Neves / Lima, William Gustavo / Brito, Julio Cesar Moreira / Simião, Daniela Carolina / Gonçalves, Lucas Vinícius Ribeiro / Cordeiro, Lídia Pereira Barbosa / de Oliveira Scoaris, Denise / Fernandes, Simone Odília Antunes / Resende, Jarbas Magalhães / Bechinger, Burkhard / Verly, Rodrigo Moreira / de Lima, Maria Elena

    Antibiotics (Basel, Switzerland)

    2024  Volume 13, Issue 3

    Abstract: The urgent global health challenge posed by methicillin- ... ...

    Abstract The urgent global health challenge posed by methicillin-resistant
    Language English
    Publishing date 2024-03-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2681345-2
    ISSN 2079-6382
    ISSN 2079-6382
    DOI 10.3390/antibiotics13030248
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Peptide fragments of bradykinin show unexpected biological activity not mediated by B

    Souza-Silva, Igor Maciel / de Paula, Cristiane Amorim / Bolais-Ramos, Lucas / Santos, Anderson Kenedy / da Silva, Filipe Alex / de Oliveira, Vívian Louise Soares / da Rocha, Isabella Domingos / Antunes, Maísa Mota / Cordeiro, Lídia Pereira Barbosa / Teixeira, Vanessa Pereira / Scalzo Júnior, Sérgio Ricardo Aluotto / Raabe, Adriana Campezatto / Guimaraes, Pedro Pires Goulart / Amaral, Flávio Almeida / Resende, Jarbas Magalhães / Fontes, Marco Antônio Peliky / Menezes, Gustavo Batista / Guatimosim, Silvia / Santos, Robson Augusto Souza /
    Verano-Braga, Thiago

    British journal of pharmacology

    2022  Volume 179, Issue 12, Page(s) 3061–3077

    Abstract: Background and purpose: Bradykinin (BK-(1-9)) is an endogenous nonapeptide involved in multiple physiological and pathological processes. Peptide fragments of bradykinin are believed to be biologically inactive. We have now tested the two major peptide ... ...

    Abstract Background and purpose: Bradykinin (BK-(1-9)) is an endogenous nonapeptide involved in multiple physiological and pathological processes. Peptide fragments of bradykinin are believed to be biologically inactive. We have now tested the two major peptide fragments of bradykinin in human and animals.
    Experimental approach: BK peptides were quantified by MS in male rats. NO release was quantified from human, mouse and rat cells loaded with DAF-FM. Rat aortic rings were used to measure vascular reactivity. Changes in BP and HR were measured in conscious male rats. To evaluate pro-inflammatory effects both vascular permeability and nociception were measured in adult mice.
    Key results: BK-(1-7) and BK-(1-5) are produced in vivo from BK-(1-9). Both peptides induced NO production in all cell types tested. However, unlike BK-(1-9), NO production elicited by BK-(1-7) or BK-(1-5) was not inhibited by B
    Conclusions and implications: BK-(1-7) and BK-(1-5) are endogenous peptides present in plasma. BK-related peptide fragments show biological activity, not mediated by B
    MeSH term(s) Animals ; Bradykinin/pharmacology ; Male ; Mice ; Peptide Fragments ; Rats ; Receptor, Bradykinin B1 ; Receptor, Bradykinin B2 ; Receptors, Bradykinin/physiology
    Chemical Substances Peptide Fragments ; Receptor, Bradykinin B1 ; Receptor, Bradykinin B2 ; Receptors, Bradykinin ; Bradykinin (S8TIM42R2W)
    Language English
    Publishing date 2022-02-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80081-8
    ISSN 1476-5381 ; 0007-1188
    ISSN (online) 1476-5381
    ISSN 0007-1188
    DOI 10.1111/bph.15790
    Database MEDical Literature Analysis and Retrieval System OnLINE

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