Degradation of bradykinin by a metalloendopeptidase from Streptococcus pyogenes
| Autor: | Takaaki Akaike, Shigetada Kawabata, Shigeyuki Hamada, Fusao Ota, Teruo Akuta, Yoichi Miyamoto, Hideo Igarashi, Jun Yoshitake, Ryutaro Kamijo, Kentaro Yoshimura, Chiho Taruki, Hiroshi Maeda |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
education Medicine (miscellaneous) Bradykinin Biology medicine.disease_cause General Biochemistry Genetics and Molecular Biology Microbiology law.invention 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine law medicine Immunoadsorption General Dentistry chemistry.chemical_classification Kininogen 030206 dentistry Angiotensin II 030104 developmental biology Enzyme chemistry Streptococcus pyogenes cardiovascular system Recombinant DNA Metalloendopeptidase circulatory and respiratory physiology |
| Zdroj: | Journal of oral biosciences. 58(4) |
| ISSN: | 1880-3865 |
| Popis: | Objectives Streptococcus pyogenes secretes streptococcal pyrogenic exotoxin B (SpeB), which cleaves kininogen to liberate bradykinin. In addition, this bacterium also has cell-associated bradykinin-degrading activity. Here, we characterized the bradykinin-degrading enzyme produced by S. pyogenes . Methods The effects of various peptidase inhibitors on bradykinin degradation by intact S. pyogenes and cell lysates were assessed. Cleavage of bradykinin and other peptides by a recombinant putative metalloendopeptidase (Sp-Pep) from S. pyogenes was analyzed by mass spectrometry. The enhancement of vascular permeability induced by bradykinin (before and after treatment with Sp-Pep) was evaluated in guinea pig skin. Results Various S. pyogenes strains expressed Sp-Pep. Immunoadsorption of S. pyogenes with an anti-Sp-Pep antibody showed that 80% of the bradykinin-degrading activity in S. pyogenes was due to Sp-Pep. Recombinant Sp-Pep cleaved bradykinin, and cleavage caused a loss of its extravasation-inducing potential. Sp-Pep-mediated degradation of bradykinin was 40 times more efficient than degradation of substance P and angiotensin II. While S. pyogenes secreted mature SpeB in stationary phase, this bacterium produced Sp-Pep during all tested growth phases. Conclusions S. pyogenes produces a cell-associated metalloendopeptidase that degrades bradykinin. |
| Databáze: | OpenAIRE |
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