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. 2022 Mar 1;6(2):e12673.
doi: 10.1002/rth2.12673. eCollection 2022 Feb.

Bradykinin - An elusive peptide in measuring and understanding

Alessandro S Pinheiro  1 , Sadiq Silbak  1 , Alvin H Schmaier  1   2
Affiliations

Bradykinin - An elusive peptide in measuring and understanding

Alessandro S Pinheiro et al. Res Pract Thromb Haemost. .
No abstract available

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Figures

FIGURE 1
FIGURE 1
Bradykinin formation and degradation. Panel A. Bradykinin (in red lettering) is a 9 amino acid peptide in kininogens. This panel shows where plasma kallikrein (PKa) cleaves kininogen (HK) to liberate bradykinin (BK). The peptidases (kininases) that degrade BK are shown as abbreviations below the red sequence of BK. The peptide bond that each of these kininases cleave are indicated by the thick small arrows. The full name of the abbreviated kininases is shown in Panel C. The BK breakdown products from the various kininases are delineated in red above the sequence of bradykinin. Panel B lists the many human serine and cysteine plasma and tissue proteases that cleave kininogens to liberation BK. Panel C presents the full name and alias of 13 plasma and membrane kininases. The BK degradation peptides produced by these kininases are shown in the table
See this image and copyright information in PMC

References

    1. Gangnus T, Burckhardt BB. Reliable measurement of plasma kinin peptides: Importance of preanalytical variables. Res Pract Thromb Haemost. 2022;6:e12646. doi:10.1002/rth2.12646 - DOI - PMC - PubMed
    1. Rocha E, Silva M, Beraldo WT, Rosenfeld G. Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Am J Physiol. 1949;156:261‐273. - PubMed
    1. Cherry PD, Furchgott RF, Zawadzki JV, Jothianandan D. Role of endothelial cells in relaxation of isolated arteries by bradykinin. Proc Natl Acad Sci U S A. 1982;79:2106‐2110. - PMC - PubMed
    1. Rapoport RM, Murad F. Agonist‐induced endothelium‐dependent relaxation in rat thoracic aorta may be mediated through cGMP. Circ Res. 1983;52:352‐357. - PubMed
    1. Palmer RM, Ferrige AG, Moncada S. Nitric oxide release accounts for the biological activity of endothelium‐derived relaxing factor. Nature. 1987;327:524‐526. - PubMed