Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema

G. W. Hunninghake, J. M. Davidson, S. Rennard, S. Szapiel, J. E. Gadek, Ronald Crystal

Research output: Contribution to journalArticle

148 Citations (Scopus)

Abstract

This study suggests one mechanism by which alveolar macrophages accumulate in the lung in pulmonary emphysema: elastin fragments generated at the diseased sites are potent chemoattractants for monocytes, the precursors of the macrophages. The most chemotactic elastin fragments have a molecular weight between 10,000 and 50,000 and are active at concentrations as low as 3 nanograms per milliliter. By comparison, elastin fragments with higher molecular weights and desmosines are active only at concentrations greater than 0.3 microgram per milliliter. In addition, preincubation of monocytes with the 10,000- to 50,000-dalton elastin impairs the ability of the cells to migrate toward elastin fragments but not toward activated serum. Fragments of tropoelastin are not chemotactic for monocytes. Because elastin, but not tropoelastin, contains lysyl-derived cross-links, these structures may be the active chemotactic site on the elastin fragments.

Original languageEnglish
Pages (from-to)925-927
Number of pages3
JournalScience
Volume212
Issue number4497
Publication statusPublished - 1 Jan 1981
Externally publishedYes

Fingerprint

Pulmonary Emphysema
Elastin
Macrophages
Tropoelastin
Monocytes
Desmosine
Molecular Weight
Chemotactic Factors
Alveolar Macrophages
Catalytic Domain
Lung
Serum

ASJC Scopus subject areas

  • Medicine(all)
  • General

Cite this

Hunninghake, G. W., Davidson, J. M., Rennard, S., Szapiel, S., Gadek, J. E., & Crystal, R. (1981). Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema. Science, 212(4497), 925-927.

Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema. / Hunninghake, G. W.; Davidson, J. M.; Rennard, S.; Szapiel, S.; Gadek, J. E.; Crystal, Ronald.

In: Science, Vol. 212, No. 4497, 01.01.1981, p. 925-927.

Research output: Contribution to journalArticle

Hunninghake, GW, Davidson, JM, Rennard, S, Szapiel, S, Gadek, JE & Crystal, R 1981, 'Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema', Science, vol. 212, no. 4497, pp. 925-927.
Hunninghake GW, Davidson JM, Rennard S, Szapiel S, Gadek JE, Crystal R. Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema. Science. 1981 Jan 1;212(4497):925-927.
Hunninghake, G. W. ; Davidson, J. M. ; Rennard, S. ; Szapiel, S. ; Gadek, J. E. ; Crystal, Ronald. / Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema. In: Science. 1981 ; Vol. 212, No. 4497. pp. 925-927.
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N2 - This study suggests one mechanism by which alveolar macrophages accumulate in the lung in pulmonary emphysema: elastin fragments generated at the diseased sites are potent chemoattractants for monocytes, the precursors of the macrophages. The most chemotactic elastin fragments have a molecular weight between 10,000 and 50,000 and are active at concentrations as low as 3 nanograms per milliliter. By comparison, elastin fragments with higher molecular weights and desmosines are active only at concentrations greater than 0.3 microgram per milliliter. In addition, preincubation of monocytes with the 10,000- to 50,000-dalton elastin impairs the ability of the cells to migrate toward elastin fragments but not toward activated serum. Fragments of tropoelastin are not chemotactic for monocytes. Because elastin, but not tropoelastin, contains lysyl-derived cross-links, these structures may be the active chemotactic site on the elastin fragments.

AB - This study suggests one mechanism by which alveolar macrophages accumulate in the lung in pulmonary emphysema: elastin fragments generated at the diseased sites are potent chemoattractants for monocytes, the precursors of the macrophages. The most chemotactic elastin fragments have a molecular weight between 10,000 and 50,000 and are active at concentrations as low as 3 nanograms per milliliter. By comparison, elastin fragments with higher molecular weights and desmosines are active only at concentrations greater than 0.3 microgram per milliliter. In addition, preincubation of monocytes with the 10,000- to 50,000-dalton elastin impairs the ability of the cells to migrate toward elastin fragments but not toward activated serum. Fragments of tropoelastin are not chemotactic for monocytes. Because elastin, but not tropoelastin, contains lysyl-derived cross-links, these structures may be the active chemotactic site on the elastin fragments.

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