Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides
The kallikrein-kinin system is complex, with several bioactive peptides that are formed in many different compartments. Kinin peptides are implicated in many physiological and pathological processes including the regulation of blood pressure and sodium homeostasis, inflammatory processes, and the ca...
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
2000-06-01
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| Series: | Brazilian Journal of Medical and Biological Research |
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| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000600008 |
| _version_ | 1819169733164924928 |
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| author | D.J. Campbell |
| author_facet | D.J. Campbell |
| author_sort | D.J. Campbell |
| collection | DOAJ |
| description | The kallikrein-kinin system is complex, with several bioactive peptides that are formed in many different compartments. Kinin peptides are implicated in many physiological and pathological processes including the regulation of blood pressure and sodium homeostasis, inflammatory processes, and the cardioprotective effects of preconditioning. We established a methodology for the measurement of individual kinin peptides in order to study the function of the kallikrein-kinin system. The levels of kinin peptides in tissues were higher than in blood, confirming the primary tissue localization of the kallikrein-kinin system. Moreover, the separate measurement of bradykinin and kallidin peptides in man demonstrated the differential regulation of the plasma and tissue kallikrein-kinin systems, respectively. Kinin peptide levels were increased in the heart of rats with myocardial infarction, in tissues of diabetic and spontaneously hypertensive rats, and in urine of patients with interstitial cystitis, suggesting a role for kinin peptides in the pathogenesis of these conditions. By contrast, blood levels of kallidin, but not bradykinin, peptides were suppressed in patients with severe cardiac failure, suggesting that the activity of the tissue kallikrein-kinin system may be suppressed in this condition. Both angiotensin converting enzyme (ACE) and neutral endopeptidase (NEP) inhibitors increased bradykinin peptide levels. ACE and NEP inhibitors had different effects on kinin peptide levels in blood, urine, and tissues, which may be accounted for by the differential contributions of ACE and NEP to kinin peptide metabolism in the multiple compartments in which kinin peptide generation occurs. Measurement of the levels of individual kinin peptides has given important information about the operation of the kallikrein-kinin system and its role in physiology and disease states. |
| first_indexed | 2024-12-22T19:24:11Z |
| format | Article |
| id | doaj.art-394117c83bb84102968a7e54981e8075 |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-12-22T19:24:11Z |
| publishDate | 2000-06-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-394117c83bb84102968a7e54981e80752022-12-21T18:15:17ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2000-06-0133666567710.1590/S0100-879X2000000600008Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptidesD.J. CampbellThe kallikrein-kinin system is complex, with several bioactive peptides that are formed in many different compartments. Kinin peptides are implicated in many physiological and pathological processes including the regulation of blood pressure and sodium homeostasis, inflammatory processes, and the cardioprotective effects of preconditioning. We established a methodology for the measurement of individual kinin peptides in order to study the function of the kallikrein-kinin system. The levels of kinin peptides in tissues were higher than in blood, confirming the primary tissue localization of the kallikrein-kinin system. Moreover, the separate measurement of bradykinin and kallidin peptides in man demonstrated the differential regulation of the plasma and tissue kallikrein-kinin systems, respectively. Kinin peptide levels were increased in the heart of rats with myocardial infarction, in tissues of diabetic and spontaneously hypertensive rats, and in urine of patients with interstitial cystitis, suggesting a role for kinin peptides in the pathogenesis of these conditions. By contrast, blood levels of kallidin, but not bradykinin, peptides were suppressed in patients with severe cardiac failure, suggesting that the activity of the tissue kallikrein-kinin system may be suppressed in this condition. Both angiotensin converting enzyme (ACE) and neutral endopeptidase (NEP) inhibitors increased bradykinin peptide levels. ACE and NEP inhibitors had different effects on kinin peptide levels in blood, urine, and tissues, which may be accounted for by the differential contributions of ACE and NEP to kinin peptide metabolism in the multiple compartments in which kinin peptide generation occurs. Measurement of the levels of individual kinin peptides has given important information about the operation of the kallikrein-kinin system and its role in physiology and disease states.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000600008bradykininkallidinkallikreinkininogen |
| spellingShingle | D.J. Campbell Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides Brazilian Journal of Medical and Biological Research bradykinin kallidin kallikrein kininogen |
| title | Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides |
| title_full | Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides |
| title_fullStr | Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides |
| title_full_unstemmed | Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides |
| title_short | Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides |
| title_sort | towards understanding the kallikrein kinin system insights from measurement of kinin peptides |
| topic | bradykinin kallidin kallikrein kininogen |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000600008 |
| work_keys_str_mv | AT djcampbell towardsunderstandingthekallikreinkininsysteminsightsfrommeasurementofkininpeptides |