Advertisement
Journal of Biological Chemistry
Open access logo
Advanced searchSave search
Research Article| Volume 260, ISSUE 20, P10966-10970, September 15, 1985

Download started.

Ok

Leukotriene A3. A poor substrate but a potent inhibitor of rat and human neutrophil leukotriene A4 hydrolase.

Open AccessPublished:September 15, 1985DOI:https://doi.org/10.1016/S0021-9258(17)39131-7
Leukotriene A3. A poor substrate but a potent inhibitor of rat and human neutrophil leukotriene A4 hydrolase.
Previous ArticleForskolin-induced change of the size of adenylate cyclase.
Next ArticleEvidence from chemical degradation studies for a covalent bond from 5-fluoro-2‘-deoxyuridylate to N-5 of tetrahydrofolate in the ternary complex of thymidylate synthetase-5-fluoro-2‘-deoxyuridylate-5,10-methylenetetrahydrofolate.
      This paper is only available as a PDF. To read, Please Download here.
      Analysis of leukotriene B4 production by purified rat and human neutrophil leukotriene (LT) A4 hydrolases in the presence of 5(S)-trans-5,6-oxido-7,9-trans-11-cis-eicosatrienoic acid (leukotriene A3) demonstrated that this epoxide is a potent inhibitor of LTA4 hydrolase. Insignificant amounts of 5(S), 12(R)-dihydroxy-6-cis-8,10-trans-eicosatrienoic acid (leukotriene B3) were formed by incubation of rat neutrophils with leukotriene A3 or by the purified rat and human LTA4 hydrolases incubated with leukotriene A3. Leukotriene A3 was shown to be a potent inhibitor of leukotriene B4 production by rat neutrophils and also by purified rat and human LTA4 hydrolases. Covalent coupling of [3H]leukotriene A4 to both rat and human neutrophil LTA4 hydrolases was shown, and this coupling was inhibited by preincubation of the enzymes with leukotriene A4. Preincubation of rat neutrophils with leukotriene A3 also prevented labeling of LTA4 hydrolase by [3H]leukotriene A4. This result indicates that leukotriene A3 prevents covalent coupling of the substrate leukotriene A4 and inhibits the production of leukotriene B4 by blocking the binding of leukotriene A4 to the enzyme.

      REFERENCES

        • Evans J.F.
        • Dupuis P.
        • Ford-Hutchinson A.W.
        Biochem. Biophys. Acta. 1985; 840: 43-50
        • Rådmark O.
        • Shimizu T.
        • Jörnvall H.
        • Samuelsson B.
        J. Biol. Chem. 1984; 259: 12339-12345
        • Ford-Hutchinson A.W.
        • Bray M.A.
        • Doig M.V.
        • Shipley M.E.
        • Smith M.J.H.
        Nature (Lond.). 1980; 286: 264-265
        • Bray M.A.
        • Cunningham F.M.
        • Ford-Hutchinson A.W.
        • Smith M.J.H.
        Br. J. Pharmacol. 1981; 72: 483-486
        • Bray M.A.
        • Ford-Hutchinson A.W.
        • Smith M.J.H.
        Prostaglandins. 1981; 22: 213-222
        • Rackham A.
        • Ford-Hutchinson A.W.
        Prostaglandins. 1983; 25: 193-203
        • Stenson W.F.
        • Lobos E.
        J. Clin. Invest. 1982; 69: 494-497
        • Grabbe J.
        • Czarnetzki B.M.
        • Rosenbach T.
        • Mardin M.
        J. Invest. Dermatol. 1984; 82: 477-479
        • Klickstein L.B.
        • Shapleigh C.
        • Goetzl E.
        J. Clin. Invest. 1980; 66: 1166-1176
        • Stenson W.F.
        • Prescott S.M.
        • Sprecher H.
        J. Biol. Chem. 1984; 259: 11784-11789
        • Rokach J.
        • Zamboni R.
        • Lau C.K.
        • Guindon Y.
        Tetrahedron Lett. 1981; 22: 2759-2763
        • Cunningham F.M.
        • Smith M.J.H.
        • Ford-Hutchinson A.W.
        • Walker J.R.
        J. Pathol. 1979; 128: 15-20
        • Laemmli U.K.
        Nature (Lond.). 1970; 227: 680-685
        • Bradford M.
        Anal. Biochem. 1976; 72: 248-254
        • Goldman D.W.
        • Pickett W.C.
        • Goetzl E.J.
        Biochem. Biophys. Res. Commun. 1983; 117: 282-288
        • Lee T.H.
        • Mencia-Huerta J.-M.
        • Shih C.
        • Corey E.J.
        • Lewis R.A.
        • Austen K.F.
        J. Biol. Chem. 1984; 259: 2383-2389
        • Prescott S.M.
        J. Biol. Chem. 1984; 259: 7615-7621

      Article info

      Publication history

      Published online: September 15, 1985

      Identification

      DOI: https://doi.org/10.1016/S0021-9258(17)39131-7

      Copyright

      © 1985 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

      User license

      Creative Commons Attribution (CC BY 4.0) |
      How you can reuse Information Icon
      Creative Commons Attribution (CC BY 4.0)

      Permitted

      • Read, print & download
      • Redistribute or republish the final article
      • Text & data mine
      • Translate the article
      • Reuse portions or extracts from the article in other works
      • Sell or re-use for commercial purposes

      Elsevier's open access license policy

      ScienceDirect

      Access this article on ScienceDirect

      ASBMB  ASBMB  ASBMB  ASBMB

      ISSN 0021-9258
      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the for this site.
      Copyright © 2022 Elsevier Inc. except certain content provided by third parties. The content on this site is intended for healthcare professionals.


      RELX