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Elastin degradation by mononuclear phagocytes.

S D Shapiro¹, E J Campbell, H G Welgus

¹Division of Respiratory and Critical Care, Jewish Hospital, Washington University Medical Center, St. Louis, Missouri 63110.

Annals of the New York Academy of Sciences

|January 1, 1991

Summary

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Mononuclear phagocytes release proteinases that degrade extracellular matrix, including elastin. These enzymes, particularly metalloelastase and cysteine proteinases, play a role in lung tissue remodeling and may contribute to emphysema pathogenesis.

Area of Science:

Biochemistry
Cell Biology
Pulmonary Medicine

Background:

Mononuclear phagocytes exhibit dynamic proteinase expression during development.
Neutrophil elastase is present in immature cells but not synthesized by mature macrophages.

Purpose of the Study:

To investigate the role of proteinases, particularly elastolytic enzymes, in extracellular matrix degradation by mononuclear phagocytes.
To explore the contribution of these enzymes to lung pathologies like emphysema.

Main Methods:

Analysis of proteinase profiles in developing mononuclear phagocytes.
Characterization of elastolytic enzymes such as metalloelastase and cysteine proteinases.
Investigation of enzyme secretion and activity in macrophages.

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Main Results:

Immature mononuclear phagocytes produce neutrophil elastase; mature macrophages internalize and secrete it.
Human alveolar macrophages synthesize cathepsin L (cysteine proteinase) with acidic pH elastolytic activity.
Animal macrophages secrete metalloelastase that degrades elastin and alpha 1-antiproteinase.
Human macrophage elastolytic activity is primarily mediated by metalloproteinases.

Conclusions:

Extracellular matrix degradation involves multiple proteinases acting synergistically.
Proteinase activity is often localized pericellularly for protection and concentration.
Mononuclear phagocytes accumulating in the lung due to smoking may contribute to emphysema through matrix injury.