elastin and tetraethylenepentamine

elastin has been researched along with tetraethylenepentamine* in 1 studies

Other Studies

1 other study(ies) available for elastin and tetraethylenepentamine

ArticleYear
Inhibitors and specificity of Pseudomonas aeruginosa LasA.
    The Journal of biological chemistry, 1997, Apr-11, Volume: 272, Issue:15

    LasA is an extracellular protease of Pseudomonas aeruginosa that enhances the elastolytic activity of Pseudomonas elastase and other proteases by cleaving elastin at unknown sites. LasA is also a staphylolytic protease, an enzyme that lyses Staphylococcus aureus cells by cleaving the peptidoglycan pentaglycine interpeptides. Here we showed that the staphylolytic activity of LasA is inhibited by tetraethylenepentamine and 1,10-phenanthroline (zinc chelators) as well as excess Zn2+ and dithiothreitol. However, LasA was not inhibited by several serine or cysteine proteinase inhibitors including diisopropyl fluorophosphate, phenylmethylsulfonyl fluoride, leupeptin, and N-ethylmaleimide. LasA staphylolytic activity was also insensitive to Nalpha-p-tosyl-L-lysine chloromethyl ketone or phosphoramidon. EDTA and EGTA were inhibitory only at concentrations greater than 20 mM. Without added inhibitors, LasA obtained by DEAE-cellulose fractionation was active toward beta-casein, but the same cleavage patterns were observed with column fractions containing little or no LasA. The beta-casein cleaving activity was fully blocked in the presence of inhibitors that did not affect staphylolytic activity. In the presence of such inhibitors, purified LasA was inactive toward acetyl-Ala4 and benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala, but it degraded soluble recombinant human elastin as well as insoluble elastin. N-terminal amino acid sequencing of two fragments derived from soluble elastin indicated that both resulted from cleavages of Gly-Ala peptide bonds located within similar sequences, Pro-Gly-Val-Gly-Gly-Ala-Xaa (where Xaa is Phe or Gly). In addition, Ala was identified as the predominant N-terminal residue in fragments released by LasA from insoluble elastin. A dose-dependence study of elastase stimulation by LasA indicated that a high molar ratio of LasA to elastase was required for significant enhancement of elastolysis. The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Substrates that contain no Gly-Gly peptide bonds such as beta-casein appear to be resistant to LasA.

    Topics: Bacterial Proteins; Caseins; Chelating Agents; Dithiothreitol; Elastin; Electrophoresis, Polyacrylamide Gel; Ethylenediamines; Glycine; Humans; Metalloendopeptidases; Pancreatic Elastase; Peptide Fragments; Phenanthrolines; Protease Inhibitors; Serine Proteinase Inhibitors; Substrate Specificity; Tosyllysine Chloromethyl Ketone; Zinc

1997