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Titolo:
HUMAN NEUTROPHIL COLLAGENASE (MMP-8), IDENTIFIED IN BRONCHIECTASIS BAL FLUID, CORRELATES WITH SEVERITY OF DISEASE
Autore:
SEPPER R; KONTTINEN YT; DING YL; TAKAGI M; SORSA T;
Indirizzi:
HELSINKI UNIV,DEPT ANAT,MOLEC BIOL LAB HELSINKI FINLAND HELSINKI UNIV,DEPT PERIODONTOL HELSINKI FINLAND TARTU STATE UNIV,LUNG CLIN TARTU ESTONIA
Titolo Testata:
Chest
fascicolo: 6, volume: 107, anno: 1995,
pagine: 1641 - 1647
SICI:
0012-3692(1995)107:6<1641:HNC(II>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN FIBROBLAST COLLAGENASE; HUMAN MONONUCLEAR PHAGOCYTES; GINGIVAL CREVICULAR FLUID; LATENT COLLAGENASE; MATRIX METALLOPROTEINASES; TETRACYCLINE-INHIBITION; BACTEROIDES-GINGIVALIS; MAMMALIAN COLLAGENASE; PARTIAL-PURIFICATION; ACTIVATION;
Keywords:
BAL; BRONCHIECTASIS; COLLAGENOLYTIC PROTEINASES; MMP-8;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
R. Sepper et al., "HUMAN NEUTROPHIL COLLAGENASE (MMP-8), IDENTIFIED IN BRONCHIECTASIS BAL FLUID, CORRELATES WITH SEVERITY OF DISEASE", Chest, 107(6), 1995, pp. 1641-1647

Abstract

Collagenases in bronchoalveolar lavage fluid (BALF) of patients with bronchiectasis and healthy subjects were characterized using specific functional and immunologic assays. The BAL fluid contained interstitial collagenase and collagenolytic proteinases of bacterial origin. Collagenase activities, obtained after organomercurial activation, correlated with the severity of bronchiectasis. In severe cases, collagenase activities were 3.5x10(-7) IU/L/48 h or 4.8x10(-6) IU/g/48 h (p<0.01),in moderate ones 1.74x10(-7) IU/L/48 h or 3.35x10(-6) IU/g/48 h (p<0.05), and in mild cases 0.32x10(-7) IU/L/48 h or 0.7x10(-6) IU/g/48 h (p<0.05). The corresponding activities in healthy control subjects were0.08x10(-7) IU/L/48 h or 0.13x10(-6) IU/g/48 h. The cellular origin of interstitial collagenase was assessed with doxycycline inhibition test utilizing the differential sensitivity of fibroblast-type collagenase/MMP-1 (IC50=280 mu M) and neutrophil-type collagenase/MMP-8 (IC50=26 mu M) to the anticollagenolytic, nonantimicrobial doxycycline action. Interstitial collagenase, contained in BALF, was totally inhibited by 100 mu M of doxycycline. It can therefore be concluded that most of mammalian collagenase presented in inflamed fluid of bronchiectasis originated from neutrophils. The molecular forms of neutrophil-type collagenase/MMP-8 were confirmed and analyzed by Western-blot, which showed evidence of the proteolytic conversion of the latent 85-kD MMP-8 proenzyme species into active 65-kD molecular weight species. These findings strongly suggest involvement of proteolytic activation pathway of proMMP-8, especially in severe and moderate forms of bronchiectasis. Furthermore, collagenolytic proteases of bacterial origins may also participate in tissue destruction of the lung.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 01:11:00