Literature DB >> 7952653

Elastolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease.

S D Shapiro1.   

Abstract

Mononuclear phagocytes have the capacity to produce an array of MMPs. Several of these proteinases are capable of degrading insoluble elastin, an important component for the structural stability of the lung. Matrilysin is a low molecular weight proteinase with a broad substrate specificity produced at highest levels in in vitro differentiated monocytes. The 92-kD gelatinase is a major product of human alveolar macrophages that is also an elastase. The most newly described member of the MMP family is human macrophage metalloelastase. This enzyme is also expressed in alveolar macrophages derived from cigarette smokers. Determining the contribution of these and other elastolytic proteinases to the pathogenesis of emphysema is a focus of ongoing research.

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Year:  1994        PMID: 7952653     DOI: 10.1164/ajrccm/150.6_Pt_2.S160

Source DB:  PubMed          Journal:  Am J Respir Crit Care Med        ISSN: 1073-449X            Impact factor:   21.405


  34 in total

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Review 8.  alpha1-Antitrypsin deficiency . 6: new and emerging treatments for alpha1-antitrypsin deficiency.

Authors:  R A Sandhaus
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9.  Matrix metalloproteases in bronchoalveolar lavage fluid of patients with type III Pseudomonas aeruginosa pneumonia.

Authors:  Ali A El-Solh; Daniel Amsterdam; Ahmad Alhajhusain; Morohonfolu E Akinnusi; Ranime G Saliba; Susan V Lynch; Jeanine P Wiener-Kronish
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10.  Local lung responses following endobronchial elastase and lipopolysaccharide instillation in sheep.

Authors:  D David S Collie; Nicola McLean; Jean-Michel Sallenave; Alison Baker; Richard Blundell; Elspeth Milne; Susan Rhind; Chris Woodall
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