Stabilization of lung surfactant particles against conversion by a cycling interface

Stephen (Steve) Hall, R. W. Hyde, M. C. Kahn

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The large active particles of pulmonary surfactant are depleted in patients with acute respiratory distress syndrome and in animal models of this disorder. We studied in vitro conversion of large to small particles, separated by differential sedimentation, to determine how factors lavaged from rabbits injured by intravenous oleic acid would affect conversion. In half-filled test tubes rotated end over end, samples from injured animals increased the recovery of large particles from 40 ± 6% of uncycled samples for controls to 62 ± 21%. We hypothesized that proteins in the injured samples, and perhaps also the proteinase inhibitors used previously to block conversion (N.J. Gross and R. M. Schultz. Biochim. Biophys. Acta 1044: 222- 230, 1990), stabilized surfactant particles by limiting access to the cycling interface. Hemoglobin, neutrophil elastase, and α1-antiproteinase (α1- PI) oxidized to eliminate its antiproteinase activity all stabilized large particles against conversion. Hemoglobin was most effective, increasing recovery from 18 ± 5% for controls to 86 ± 5% with 0.4 mg/ml hemoglobin. Native α1-PI had no effect on conversion. Our results suggest that acceleration of normal conversion is unlikely to explain the depletion of large particles in injured lungs. They also suggest that conversion of surfactant particles separated by differential sedimentation requires no proteinase susceptible to inhibition by α1-PI. They provide an alternate hypothesis related to interfacial effects rather than proteinase inhibition for the previously reported effect of α1-PI on conversion of particles separated according to density.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Volume272
Issue number2 16-2
StatePublished - Feb 1997

Fingerprint

Surface-Active Agents
Hemoglobins
Peptide Hydrolases
Lung
Pulmonary Surfactants
Leukocyte Elastase
Adult Respiratory Distress Syndrome
Oleic Acid
Animal Models
Rabbits
Proteins
In Vitro Techniques

Keywords

  • free fatty acid
  • oleic acid
  • pulmonary surfactant
  • surfactant cycling
  • surfactant metabolism
  • surfactant subfractions

ASJC Scopus subject areas

  • Pulmonary and Respiratory Medicine
  • Cell Biology
  • Physiology
  • Physiology (medical)

Cite this

Stabilization of lung surfactant particles against conversion by a cycling interface. / Hall, Stephen (Steve); Hyde, R. W.; Kahn, M. C.

In: American Journal of Physiology - Lung Cellular and Molecular Physiology, Vol. 272, No. 2 16-2, 02.1997.

Research output: Contribution to journalArticle

@article{f8a45d1ddb7b4746895da07a0e736dfa,
title = "Stabilization of lung surfactant particles against conversion by a cycling interface",
abstract = "The large active particles of pulmonary surfactant are depleted in patients with acute respiratory distress syndrome and in animal models of this disorder. We studied in vitro conversion of large to small particles, separated by differential sedimentation, to determine how factors lavaged from rabbits injured by intravenous oleic acid would affect conversion. In half-filled test tubes rotated end over end, samples from injured animals increased the recovery of large particles from 40 ± 6{\%} of uncycled samples for controls to 62 ± 21{\%}. We hypothesized that proteins in the injured samples, and perhaps also the proteinase inhibitors used previously to block conversion (N.J. Gross and R. M. Schultz. Biochim. Biophys. Acta 1044: 222- 230, 1990), stabilized surfactant particles by limiting access to the cycling interface. Hemoglobin, neutrophil elastase, and α1-antiproteinase (α1- PI) oxidized to eliminate its antiproteinase activity all stabilized large particles against conversion. Hemoglobin was most effective, increasing recovery from 18 ± 5{\%} for controls to 86 ± 5{\%} with 0.4 mg/ml hemoglobin. Native α1-PI had no effect on conversion. Our results suggest that acceleration of normal conversion is unlikely to explain the depletion of large particles in injured lungs. They also suggest that conversion of surfactant particles separated by differential sedimentation requires no proteinase susceptible to inhibition by α1-PI. They provide an alternate hypothesis related to interfacial effects rather than proteinase inhibition for the previously reported effect of α1-PI on conversion of particles separated according to density.",
keywords = "free fatty acid, oleic acid, pulmonary surfactant, surfactant cycling, surfactant metabolism, surfactant subfractions",
author = "Hall, {Stephen (Steve)} and Hyde, {R. W.} and Kahn, {M. C.}",
year = "1997",
month = "2",
language = "English (US)",
volume = "272",
journal = "American Journal of Physiology - Renal Fluid and Electrolyte Physiology",
issn = "1931-857X",
publisher = "American Physiological Society",
number = "2 16-2",

}

TY - JOUR

T1 - Stabilization of lung surfactant particles against conversion by a cycling interface

AU - Hall, Stephen (Steve)

AU - Hyde, R. W.

AU - Kahn, M. C.

PY - 1997/2

Y1 - 1997/2

N2 - The large active particles of pulmonary surfactant are depleted in patients with acute respiratory distress syndrome and in animal models of this disorder. We studied in vitro conversion of large to small particles, separated by differential sedimentation, to determine how factors lavaged from rabbits injured by intravenous oleic acid would affect conversion. In half-filled test tubes rotated end over end, samples from injured animals increased the recovery of large particles from 40 ± 6% of uncycled samples for controls to 62 ± 21%. We hypothesized that proteins in the injured samples, and perhaps also the proteinase inhibitors used previously to block conversion (N.J. Gross and R. M. Schultz. Biochim. Biophys. Acta 1044: 222- 230, 1990), stabilized surfactant particles by limiting access to the cycling interface. Hemoglobin, neutrophil elastase, and α1-antiproteinase (α1- PI) oxidized to eliminate its antiproteinase activity all stabilized large particles against conversion. Hemoglobin was most effective, increasing recovery from 18 ± 5% for controls to 86 ± 5% with 0.4 mg/ml hemoglobin. Native α1-PI had no effect on conversion. Our results suggest that acceleration of normal conversion is unlikely to explain the depletion of large particles in injured lungs. They also suggest that conversion of surfactant particles separated by differential sedimentation requires no proteinase susceptible to inhibition by α1-PI. They provide an alternate hypothesis related to interfacial effects rather than proteinase inhibition for the previously reported effect of α1-PI on conversion of particles separated according to density.

AB - The large active particles of pulmonary surfactant are depleted in patients with acute respiratory distress syndrome and in animal models of this disorder. We studied in vitro conversion of large to small particles, separated by differential sedimentation, to determine how factors lavaged from rabbits injured by intravenous oleic acid would affect conversion. In half-filled test tubes rotated end over end, samples from injured animals increased the recovery of large particles from 40 ± 6% of uncycled samples for controls to 62 ± 21%. We hypothesized that proteins in the injured samples, and perhaps also the proteinase inhibitors used previously to block conversion (N.J. Gross and R. M. Schultz. Biochim. Biophys. Acta 1044: 222- 230, 1990), stabilized surfactant particles by limiting access to the cycling interface. Hemoglobin, neutrophil elastase, and α1-antiproteinase (α1- PI) oxidized to eliminate its antiproteinase activity all stabilized large particles against conversion. Hemoglobin was most effective, increasing recovery from 18 ± 5% for controls to 86 ± 5% with 0.4 mg/ml hemoglobin. Native α1-PI had no effect on conversion. Our results suggest that acceleration of normal conversion is unlikely to explain the depletion of large particles in injured lungs. They also suggest that conversion of surfactant particles separated by differential sedimentation requires no proteinase susceptible to inhibition by α1-PI. They provide an alternate hypothesis related to interfacial effects rather than proteinase inhibition for the previously reported effect of α1-PI on conversion of particles separated according to density.

KW - free fatty acid

KW - oleic acid

KW - pulmonary surfactant

KW - surfactant cycling

KW - surfactant metabolism

KW - surfactant subfractions

UR - http://www.scopus.com/inward/record.url?scp=0030956408&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030956408&partnerID=8YFLogxK

M3 - Article

VL - 272

JO - American Journal of Physiology - Renal Fluid and Electrolyte Physiology

JF - American Journal of Physiology - Renal Fluid and Electrolyte Physiology

SN - 1931-857X

IS - 2 16-2

ER -