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Titolo:
Synergistic neutrophil elastase-cytokine interaction degrades collagen in three-dimensional culture
Autore:
Zhu, YK; Liu, XD; Skold, CM; Umino, T; Wang, HJ; Spurzem, JR; Kohyama, T; Ertl, RF; Rennard, SI;
Indirizzi:
Univ Nebraska, Med Ctr, Nebraska Med Ctr 985125, Omaha, NE 68198 USA Univ Nebraska Omaha NE USA 68198 aska Med Ctr 985125, Omaha, NE 68198 USA Jincheng Hosp, Lanzhou, Peoples R China Jincheng Hosp Lanzhou Peoples R China ng Hosp, Lanzhou, Peoples R China Karolinska Inst, S-17176 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17176 Inst, S-17176 Stockholm, Sweden
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
fascicolo: 4, volume: 281, anno: 2001,
pagine: L868 - L878
SICI:
1040-0605(200110)281:4<L868:SNEIDC>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBROBLAST-MEDIATED CONTRACTION; NECROSIS FACTOR-ALPHA; MATRIX METALLOPROTEINASE; EXTRACELLULAR-MATRIX; PULMONARY-EMPHYSEMA; 92-KDA GELATINASE; TISSUE INHIBITOR; INITIAL COLLAGEN; ACTIVATION; STROMELYSIN;
Keywords:
matrix metalloproteinases; collagen; fibroblasts; interleukin-1; tumor necrosis factor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Rennard, SI Univ Nebraska, Med Ctr, Nebraska Med Ctr 985125, Omaha, NE 68198 USA Univ Nebraska Omaha NE USA 68198 985125, Omaha, NE 68198 USA
Citazione:
Y.K. Zhu et al., "Synergistic neutrophil elastase-cytokine interaction degrades collagen in three-dimensional culture", AM J P-LUNG, 281(4), 2001, pp. L868-L878

Abstract

Proteolytic degradation of extracellular matrix is thought to play an: important role in many lung disorders. In the current study, human lung fibroblasts were cast into type I collagen gels and floated in medium containing elastase, cytomix (combination of tumor necrosis factor-alpha, interleukin-1 beta, and interferon-gamma), or both. After 5 days, gel collagen content was determined by measuring hydroxyproline. Elastase alone did not result in collagen degradation, but in the presence of fibroblasts; elastase reduced hydroxyproline content to 75.2% (P < 0.01), whereas cytomix alone resulted in reduction of hydroxyproline content to 93% (P < 0.05). The combinationof elastase and cytomix reduced hydroxyproline content to 5.2% (P < 0.01).<alpha>(1)-Proteinase inhibitor blocked this synergy. Gelatin zymography and Western blot revealed that matrix metalloproteinase (MMP)-1, -3, and -9 were induced by cytomix and activated in the presence of elastase. Tissue inhibitor of metalloproteinase (TIMP)-1 and -2 were also induced by cytomix but were cleaved by elastase. We conclude that a synergistic interaction between cytomix and elastase, mediated through cytokine induction of MMP production and elastase-induced activation of latent MMPs and degradation of TIMPs, can result in a dramatic augmentation of collagen degradation. These findings support the notion that interaction among inflammatory mediators secreted by mononuclear cells and neutrophils can induce tissue cells to degrade extracellular matrix. Such a mechanism may contribute to the protease-anti-protease imbalance in emphysema.

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Documento generato il 05/04/20 alle ore 12:55:09