{"title":"Carrageenin-Stimulated Peritoneal Macrophages Release In Vitro Collagenase and Gelatinase","authors":"Ricardo López-Escalera, Annie Pardo","doi":"10.1016/S0174-173X(87)80031-6","DOIUrl":null,"url":null,"abstract":"<div><p>Guinea pig macrophages were obtained by intraperitoneal injection of carrageenin, and in contrast with peritoneal cells from non-stimulated animals, release <em>in vitro</em> an active collagenase into the culture medium. Short time trypsin incubations and treatment of enzyme preparations with 4-APMA failed to reveal latent enzyme activity. Metallopeptidases specific for gelatin paralleled the presence of collagenase in the media of stimulated cells. Raw medium was fractionated by affinity chromatography with heparin-sepharose, collagenase activity bound to heparin sepharose while a gelatinase with an apparent molecular weight of 54,800 did not. When macrophages were grown <em>in vitro</em> in the presence of albumin, the gelatinase activity showed affinity for heparin and an apparent molecular weight of 113,000.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 4","pages":"Pages 249-257"},"PeriodicalIF":0.0000,"publicationDate":"1987-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80031-6","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Collagen and related research","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0174173X87800316","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
Guinea pig macrophages were obtained by intraperitoneal injection of carrageenin, and in contrast with peritoneal cells from non-stimulated animals, release in vitro an active collagenase into the culture medium. Short time trypsin incubations and treatment of enzyme preparations with 4-APMA failed to reveal latent enzyme activity. Metallopeptidases specific for gelatin paralleled the presence of collagenase in the media of stimulated cells. Raw medium was fractionated by affinity chromatography with heparin-sepharose, collagenase activity bound to heparin sepharose while a gelatinase with an apparent molecular weight of 54,800 did not. When macrophages were grown in vitro in the presence of albumin, the gelatinase activity showed affinity for heparin and an apparent molecular weight of 113,000.