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Eur.J.Biochem.198,391-398(1991)
3;FEBS1991
0014295691003504
Purificationandidentificationof91-kDaneutrophilgelatinase
Releasebytheactivatingpeptideinterleukin-8
StefanMASURE,PaulPROOST,JoVANDAMMEandGhislainOPDENAKKER
RegaInstituteforMedicalResearch,UniversityofLeuven,Belgium
(ReceivedDecember17,1990/February11,1991)-EJB901502
Humanneutrophilswerefoundtoreleasea91-kDagelatinasethatisserologicallyrelatedtotumor-derived
gelatinolyticenzymes,asevidencedbyimmunoprecipitation.Inordertoidentifytheneutrophilgelatinase,the
activityinconditionedmediumfromhumanneutrophilsuspensionswaspurifiedbyaffinitychromatographyon
agelatinsubstrate.The91-kDaactiveenzymewasfurtherseparatedfromotherstainableproteinbandsby
classicalSDSjPAGEandblottingtoasolidsupport.Amino-terminalsequenceanalysisofblottedproteinsshowed
thatthe91-kDaenzymeisatruncatedformoftumor-derived92-kDagelatinase(typeIVcollagenase),lacking
eightresiduesattheNH2-terminus.Sequenceanalysisofenzymaticallyinactivecleavageproductsofthis
neutrophilgelatinasedemonstratedthatthegelatin-bindingpartofthemoleculeisrestrictedtotheamino-terminal
third.
Exocytosisofgelatinase-containinggranulesfromneutrophilsoccurredspontaneouslywithin6hafter
neutrophilplating.Whenthecellsweretriggeredwiththephorbolesterphorbol12-myristate13-acetate,astrong
secretagogue,rapidgelatinasereleasewasobserved.Whengranulocyteswerestimulatedwiththeneutrophil-
activatingpeptideinterleukin-8,maximalexocytosisoccurredwithin
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