Inhibition of the growth and cysteine proteinase activity of Porphyromonas gingivalis by human salivary cystatin S and chicken cystatin.
The mutual effects of P. gingivalis and several cystatin species has been investigated. After incubation with P. gingivalis culture supernatant, cystatin S, cystatin C and chicken cystatin were truncated from a 14 kDa protein into a polypeptide of approximately 13 kDa. Amino acid sequence analysis of the truncated cystatin S polypeptide revealed that cystatin S was cleaved after Arg-8. All three types of truncated cystatins fully retained their inhibitory activity toward papain. Cystatin S and chicken cystatin partially inhibited proteolytic activity in the culture supernatant of P. gingivalis. Furthermore, cystatin S and chicken cystatin inhibited the growth of P. gingivalis in culture to 50% at approximately 1 microM.
Blankenvoorde
M F
MF
Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), The Netherlands.
Henskens
Y M
YM
van't Hof
W
W
Veerman
E C
EC
Nieuw Amerongen
A V
AV
D000595:Amino Acid Sequence; D000818:Animals; D001587:Benzoylarginine-2-Naphthylamide / Q000494:pharmacology; D015891:Cystatins / Q000494:pharmacology*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D012463:Saliva / Q000737:chemistry*; D055333:Salivary Cystatins
C525173:CST4 protein, human; D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D055333:Salivary Cystatins; C100158:cystatin, egg-white; D001587:Benzoylarginine-2-Naphthylamide; D003546:Cysteine Endopeptidases