Immunogold localization of SP-A in lungs of infants dying from respiratory distress syndrome

D. E. DeMello, S. Heyman, D. S. Phelps, J. Floros

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Prematurely born infants can develop the neonatal respiratory distress syndrome (RDS) because of a deficiency of pulmonary surfactant. This lipoprotein complex synthesized by type II pneumocytes has different ultrastructural forms-intra- and extracellular lamellar bodies, which within the alveoli are transformed into tubular myelin, and this in turn gives rise to the surface monolayer, the functionally active form of surfactant. We have previously shown that at autopsy RDS lungs lack tubular myelin and have decreased immunoreactivity for antisera to surfactant protein A (SP-A), an important component of tubular myelin. Therefore, we proposed a role for SP- A in the conversion of lamellar bodies to tubular myelin and in the pathogenesis of RDS. To explore this possibility further, we compared in 14 RDS and 14 control lungs the distribution of SP-A in ultrathin sections, using affinity-purified rabbit anti-human-SP-A IgG and goat anti-rabbit IgG- conjugated with 10 nm colloidal gold particles. In controls, gold label was present in lamellar bodies, endoplasmic reticulum, on the cytoplasmic membrane of type II cells, and on lamellar bodies and tubular myelin either within alveoli or macrophages. In RDS lungs, reduced label was present in the same intracellular compartments and organelles, except in tubular myelin, which is absent. It is postulated that if SP-A is indeed necessary for the conversion of lamellar bodies to tubular myelin, in RDS either there is a deficiency of adequate amounts of functional SP-A or some other important component of surfactant is missing.

Original languageEnglish (US)
Pages (from-to)1631-1640
Number of pages10
JournalAmerican Journal of Pathology
Volume142
Issue number5
StatePublished - Dec 1 1993

Fingerprint

Pulmonary Surfactant-Associated Protein A
Newborn Respiratory Distress Syndrome
Lung
Surface-Active Agents
Pulmonary Surfactant-Associated Proteins
Rabbits
Alveolar Epithelial Cells
Pulmonary Surfactants
Gold Colloid
tubular myelin
Goats
Gold
Endoplasmic Reticulum
Organelles
Lipoproteins
Immune Sera
Autopsy
Immunoglobulin G
Macrophages
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine

Cite this

@article{b69dcf3dbaf24ec1bb1216b8918abfd0,
title = "Immunogold localization of SP-A in lungs of infants dying from respiratory distress syndrome",
abstract = "Prematurely born infants can develop the neonatal respiratory distress syndrome (RDS) because of a deficiency of pulmonary surfactant. This lipoprotein complex synthesized by type II pneumocytes has different ultrastructural forms-intra- and extracellular lamellar bodies, which within the alveoli are transformed into tubular myelin, and this in turn gives rise to the surface monolayer, the functionally active form of surfactant. We have previously shown that at autopsy RDS lungs lack tubular myelin and have decreased immunoreactivity for antisera to surfactant protein A (SP-A), an important component of tubular myelin. Therefore, we proposed a role for SP- A in the conversion of lamellar bodies to tubular myelin and in the pathogenesis of RDS. To explore this possibility further, we compared in 14 RDS and 14 control lungs the distribution of SP-A in ultrathin sections, using affinity-purified rabbit anti-human-SP-A IgG and goat anti-rabbit IgG- conjugated with 10 nm colloidal gold particles. In controls, gold label was present in lamellar bodies, endoplasmic reticulum, on the cytoplasmic membrane of type II cells, and on lamellar bodies and tubular myelin either within alveoli or macrophages. In RDS lungs, reduced label was present in the same intracellular compartments and organelles, except in tubular myelin, which is absent. It is postulated that if SP-A is indeed necessary for the conversion of lamellar bodies to tubular myelin, in RDS either there is a deficiency of adequate amounts of functional SP-A or some other important component of surfactant is missing.",
author = "DeMello, {D. E.} and S. Heyman and Phelps, {D. S.} and J. Floros",
year = "1993",
month = "12",
day = "1",
language = "English (US)",
volume = "142",
pages = "1631--1640",
journal = "American Journal of Pathology",
issn = "0002-9440",
publisher = "Elsevier Inc.",
number = "5",

}

Immunogold localization of SP-A in lungs of infants dying from respiratory distress syndrome. / DeMello, D. E.; Heyman, S.; Phelps, D. S.; Floros, J.

In: American Journal of Pathology, Vol. 142, No. 5, 01.12.1993, p. 1631-1640.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Immunogold localization of SP-A in lungs of infants dying from respiratory distress syndrome

AU - DeMello, D. E.

AU - Heyman, S.

AU - Phelps, D. S.

AU - Floros, J.

PY - 1993/12/1

Y1 - 1993/12/1

N2 - Prematurely born infants can develop the neonatal respiratory distress syndrome (RDS) because of a deficiency of pulmonary surfactant. This lipoprotein complex synthesized by type II pneumocytes has different ultrastructural forms-intra- and extracellular lamellar bodies, which within the alveoli are transformed into tubular myelin, and this in turn gives rise to the surface monolayer, the functionally active form of surfactant. We have previously shown that at autopsy RDS lungs lack tubular myelin and have decreased immunoreactivity for antisera to surfactant protein A (SP-A), an important component of tubular myelin. Therefore, we proposed a role for SP- A in the conversion of lamellar bodies to tubular myelin and in the pathogenesis of RDS. To explore this possibility further, we compared in 14 RDS and 14 control lungs the distribution of SP-A in ultrathin sections, using affinity-purified rabbit anti-human-SP-A IgG and goat anti-rabbit IgG- conjugated with 10 nm colloidal gold particles. In controls, gold label was present in lamellar bodies, endoplasmic reticulum, on the cytoplasmic membrane of type II cells, and on lamellar bodies and tubular myelin either within alveoli or macrophages. In RDS lungs, reduced label was present in the same intracellular compartments and organelles, except in tubular myelin, which is absent. It is postulated that if SP-A is indeed necessary for the conversion of lamellar bodies to tubular myelin, in RDS either there is a deficiency of adequate amounts of functional SP-A or some other important component of surfactant is missing.

AB - Prematurely born infants can develop the neonatal respiratory distress syndrome (RDS) because of a deficiency of pulmonary surfactant. This lipoprotein complex synthesized by type II pneumocytes has different ultrastructural forms-intra- and extracellular lamellar bodies, which within the alveoli are transformed into tubular myelin, and this in turn gives rise to the surface monolayer, the functionally active form of surfactant. We have previously shown that at autopsy RDS lungs lack tubular myelin and have decreased immunoreactivity for antisera to surfactant protein A (SP-A), an important component of tubular myelin. Therefore, we proposed a role for SP- A in the conversion of lamellar bodies to tubular myelin and in the pathogenesis of RDS. To explore this possibility further, we compared in 14 RDS and 14 control lungs the distribution of SP-A in ultrathin sections, using affinity-purified rabbit anti-human-SP-A IgG and goat anti-rabbit IgG- conjugated with 10 nm colloidal gold particles. In controls, gold label was present in lamellar bodies, endoplasmic reticulum, on the cytoplasmic membrane of type II cells, and on lamellar bodies and tubular myelin either within alveoli or macrophages. In RDS lungs, reduced label was present in the same intracellular compartments and organelles, except in tubular myelin, which is absent. It is postulated that if SP-A is indeed necessary for the conversion of lamellar bodies to tubular myelin, in RDS either there is a deficiency of adequate amounts of functional SP-A or some other important component of surfactant is missing.

UR - http://www.scopus.com/inward/record.url?scp=0027755219&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027755219&partnerID=8YFLogxK

M3 - Article

C2 - 8494055

AN - SCOPUS:0027755219

VL - 142

SP - 1631

EP - 1640

JO - American Journal of Pathology

JF - American Journal of Pathology

SN - 0002-9440

IS - 5

ER -