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Inactivation of the vascular permeability-increasing activity of bradykinin by mycoplasmas
1Department of Oral Bacteriology, Nagasaki University School of Dentistry, Japan.
Abstract:
Mycoplasma pneumoniae, M. genitalium, M. fermentans, M. hominis, M. salivarium, M. orale, Ureaplasma urealyticum and Acholeplasma laidlawii inactivated the vascular permeability-increasing activity of bradykinin when the mixture of bradykinin and mycoplasma cells was injected after incubation at 37 degrees C for 1 h. Cell components responsible for inactivation of the activity of bradykinin were found to be arginine-specific aminopeptidase and carboxypeptidase.
Insights
Certain Mycoplasma species, including Mycoplasma pneumoniae, inactivate bradykinin's vascular permeability activity through specific enzymes. This inactivation is mediated by arginine-specific aminopeptidase and carboxypeptidase found within the mycoplasma cells.
Area of Science:
- Microbiology
- Biochemistry
- Vascular Biology
Background:
- Mycoplasma species are common human pathogens.
- Bradykinin plays a crucial role in regulating vascular permeability.
- The interaction between Mycoplasma and bradykinin's activity is not fully understood.
Purpose of the Study:
- To investigate the effect of various Mycoplasma species on the vascular permeability-increasing activity of bradykinin.
- To identify the specific cell components responsible for the observed inactivation of bradykinin activity.
Main Methods:
- Incubation of bradykinin with different Mycoplasma species (M. pneumoniae, M. genitalium, M. fermentans, M. hominis, M. salivarium, M. orale, Ureaplasma urealyticum, A. laidlawii) at 37°C for 1 hour.
- Injection of the mixture to assess vascular permeability.
- Analysis of mycoplasma cell components to identify enzymatic activity.
Main Results:
- Several Mycoplasma species inactivated the vascular permeability-enhancing activity of bradykinin.
- The inactivation was attributed to the presence of arginine-specific aminopeptidase and carboxypeptidase within the mycoplasma cells.
- These enzymes likely degrade bradykinin, reducing its biological effect.
Conclusions:
- Mycoplasma species possess enzymatic mechanisms to neutralize bradykinin's vascular effects.
- Arginine-specific aminopeptidase and carboxypeptidase are key enzymes involved in this inactivation process.
- This finding may have implications for understanding Mycoplasma pathogenesis and host-pathogen interactions.