Lipopolysaccharide induces release of a metallo-protease from hemocytes of the ascidian, Halocynthia roretzi.
Hemocytes of the solitary ascidian, Halocynthia roretzi, released a succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide hydrolyzing enzyme in response to lipopolysaccharide treatment. The response was dependent on the temperature for incubating hemocytes. The protease release reaction was not triggered by beta 1-3 glucan. The protease released showed strict substrate specificity and its activity was inhibited by EDTA and o-phenanthroline, but not by phosphoramidon, diisopropylfluorophosphate, N-ethylmaleimide, or p-chloromercuribenzoic acid. Thus, the enzyme was characterized as a phosphoramidon-insensitive metallo-protease. Calcium ionophore, phorbol myristate acetate, concanavalin A, and thrombin also induced the release of the same protease from H. roretzi hemocytes.
Azumi
K
K
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Yokosawa
H
H
Ishii
S
S
D000595:Amino Acid Sequence; D000818:Animals; D006434:Hemocytes / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000494:pharmacology*; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D014561:Urochordata / Q000502:physiology*
D008070:Lipopolysaccharides; D008666:Metalloendopeptidases