PMID- 2499581
OWN - NLM
STAT- MEDLINE
DCOM- 19890718
LR  - 20210212
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 264
IP  - 18
DP  - 1989 Jun 25
TI  - Activation of hageman factor and prekallikrein and generation of kinin by various 
      microbial proteinases.
PG  - 10589-94
AB  - Activation of the Hageman factor-kallikrein-kinin system by serratial 56-kDa 
      proteinase was previously demonstrated (Matsumoto, K., Yamamoto, T., Kamata, T., 
      and Maeda, H. (1984) J. Biochem. (Tokyo) 96, 739-749; Kamata, R., Yamamoto, T., 
      Matsumoto, K., and Maeda, H. (1985) Infect. Immun. 48, 747-753). To investigate 
      whether the activation of the system is specific for 56-kDa proteinase or is 
      found similarly with other microbial proteinases, 11 proteinases of microbial 
      origins were studied; the 56-kDa proteinase was the control. For in vitro 
      studies, activation of guinea pig Hageman factor and prekallikrein was examined 
      in purified systems as well as in plasma as a zymogen source. Specific antibodies 
      and inhibitors confirmed the activation steps of the cascade. In the in vivo 
      study the enhancement of vascular permeability in guinea pig skin and its 
      sensitivity to inhibitors of activated Hageman factor, plasma kallikrein, or a 
      kininase were examined. The results from the in vivo experiments were consistent 
      with those in vitro. Taking all the data together, we classified the 11 microbial 
      proteinases into three groups as follows: 1) Serratia marcescens 56-, 60-, and 
      73-kDa proteinases, Pseudomonas aeruginosa alkaline proteinase and elastase, and 
      Aspergillus melleus proteinase (this group activated Hageman factor but not 
      prekallikrein); 2) Vibrio vulnificus proteinase, subtilisin from Bacillus 
      subtilis, and thermolysin from Bacillus stearothermophilus (this group activated 
      both Hageman factor and prekallikrein); 3) Streptomyces caespitosus proteinase 
      and V8 proteinase from Staphylococcus aureus (this group activated neither 
      Hageman factor nor prekallikrein, but generated kinin from high molecular weight 
      kininogen directly).
FAU - Molla, A
AU  - Molla A
AD  - Department of Microbiology, Kumamoto University Medical School, Japan.
FAU - Yamamoto, T
AU  - Yamamoto T
FAU - Akaike, T
AU  - Akaike T
FAU - Miyoshi, S
AU  - Miyoshi S
FAU - Maeda, H
AU  - Maeda H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Kinins)
RN  - 9001-30-3 (Factor XII)
RN  - 9055-02-1 (Prekallikrein)
RN  - EC 3.4.- (Peptide Hydrolases)
SB  - IM
MH  - Animals
MH  - Aspergillus/enzymology
MH  - Bacillus/enzymology
MH  - Bacteria/*enzymology
MH  - Enzyme Activation
MH  - Factor XII/*metabolism
MH  - Guinea Pigs
MH  - Kinetics
MH  - Kinins/*metabolism
MH  - Peptide Hydrolases/*metabolism
MH  - Prekallikrein/*metabolism
MH  - Pseudomonas aeruginosa/enzymology
MH  - Serratia marcescens/enzymology
MH  - Staphylococcus aureus/enzymology
MH  - Streptomyces/enzymology
MH  - Vibrio/enzymology
EDAT- 1989/06/25 00:00
MHDA- 1989/06/25 00:01
CRDT- 1989/06/25 00:00
PHST- 1989/06/25 00:00 [pubmed]
PHST- 1989/06/25 00:01 [medline]
PHST- 1989/06/25 00:00 [entrez]
AID - S0021-9258(18)81661-1 [pii]
PST - ppublish
SO  - J Biol Chem. 1989 Jun 25;264(18):10589-94.