02035nas a2200325 4500000000100000008004100001260001300042653001200055653002400067653003300091653001400124653001700138653001500155653000900170653002300179653002100202653002900223653003100252653002400283653002400307100001200331700001200343700001300355700001200368245008400380300001000464490000700474520121400481022001401695 1986 d c1986 Aug10aAnimals10aChromatography, Gel10aChromatography, Ion Exchange10aGranuloma10aInflammation10aIsoenzymes10aMice10aMice, Inbred C57BL10aMolecular Weight10aMycobacterium Infections10aMycobacterium lepraemurium10aPancreatic Elastase10aProtease Inhibitors1 aHsu P S1 aIzaki S1 aHibino T1 aIzaki M00aElastase activity in granulomatous inflammation in experimental murine leprosy. a84-920 v453 a

Proteolytic activity for [3H]elastin, pyro-Glu-Pro-Val-pNA(S-2484), and Suc-(Ala)3-pNA(AAApNA) was demonstrated in the bound fraction extracted with 2 M KSCN + 0.1% Triton X-100 from hypersensitivity-type murine lepromas in C57BL/6N mice, while elastase-inhibitor activity was separately observed in the soluble fraction extracted with a Tris-saline buffer. Sephacryl S-200 gel chromatography showed a peak of elastolytic activity with approximately 20,000 in molecular weight. The following DEAE-Sepharose chromatography demonstrated three fractions of elastolytic activity (E-I, II, III). The inhibitory profile showed that E-I is a thiol proteinase, while E-II and E-III belong to serine proteinase-type elastases. Both E-II and E-III showed different properties with neutrophil elastase or elastase secreted from cultured macrophages, but identical characteristics to membrane bound-type elastase of monocytes. A lower level of elastolytic activity was detected in the bound fraction of nonhypersensitivity-type murine lepromas in CBA/N mice, suggesting a more involvement of membrane bound-type elastase from monocytes/macrophages during the tissue remodelings of hypersensitivity-type granulomas.

 a0014-4800