In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways

Antonella Alberti, Franco Ravenna, Daniela Quaglino, Maurizio Luisetti, Maurizio Muraca, Lorenzo Previato, Goretta Baldo Enzi, Roberta Bruni, Aldo Baritussio

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Serum lipoproteins may enter the airways and appear in sputum (chyloptysis) when the lymphatic circulation is impaired by inflammation, neoplasia, or an abnormal proliferation of smooth muscle cells. While analyzing the bronchoalveolar lavage fluid of a patient with chyloptysis, we noticed that surfactant could not be separated from contaminating serum lipoproteins and speculated that lipoproteins might interact with surfactant components. To clarify this point we immobilized surfactant protein (SP) A on microtiter wells and incubated it with 125I-labeled very low density lipoproteins (VLDLs), low-density lipoproteins, and high-density lipoproteins. We found that SP-A binds lipoproteins. Studying in greater detail the interaction of SP-A with VLDLs, we found that the binding is time and concentration dependent; is inhibited by unlabeled lipoproteins, phospholipids, and antibodies to SP-A; is increased by Ca2+; and is unaffected by methyl α-D-mannopyranoside. Whole surfactant is a potent inhibitor of binding. Furthermore, we found that SP-A increases the degradation of VLDLs by alveolar macrophages and favors the association of VLDLs with alveolar surfactant. We conclude that SP-A influences the disposal of serum lipoproteins entering the airways and speculate that binding to alveolar surfactant might represent an important step in the interaction between exogenous substances and the lung.

Original languageEnglish
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Volume274
Issue number5 18-5
Publication statusPublished - May 1998

Fingerprint

Pulmonary Surfactant-Associated Protein A
Lipoproteins
Surface-Active Agents
VLDL Lipoproteins
Serum
Immobilized Proteins
Bronchoalveolar Lavage Fluid
Alveolar Macrophages
HDL Lipoproteins
Sputum
LDL Lipoproteins
Smooth Muscle Myocytes
Phospholipids
Inflammation
Lung
Antibodies
Neoplasms

Keywords

  • Alveolar macrophages
  • Lung surfactant
  • Lymphangioleiomyomatosis
  • Surfactant protein A

ASJC Scopus subject areas

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

Cite this

Alberti, A., Ravenna, F., Quaglino, D., Luisetti, M., Muraca, M., Previato, L., ... Baritussio, A. (1998). In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways. American Journal of Physiology - Lung Cellular and Molecular Physiology, 274(5 18-5).

In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways. / Alberti, Antonella; Ravenna, Franco; Quaglino, Daniela; Luisetti, Maurizio; Muraca, Maurizio; Previato, Lorenzo; Enzi, Goretta Baldo; Bruni, Roberta; Baritussio, Aldo.

In: American Journal of Physiology - Lung Cellular and Molecular Physiology, Vol. 274, No. 5 18-5, 05.1998.

Research output: Contribution to journalArticle

Alberti, A, Ravenna, F, Quaglino, D, Luisetti, M, Muraca, M, Previato, L, Enzi, GB, Bruni, R & Baritussio, A 1998, 'In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways', American Journal of Physiology - Lung Cellular and Molecular Physiology, vol. 274, no. 5 18-5.
Alberti, Antonella ; Ravenna, Franco ; Quaglino, Daniela ; Luisetti, Maurizio ; Muraca, Maurizio ; Previato, Lorenzo ; Enzi, Goretta Baldo ; Bruni, Roberta ; Baritussio, Aldo. / In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways. In: American Journal of Physiology - Lung Cellular and Molecular Physiology. 1998 ; Vol. 274, No. 5 18-5.
@article{3ee91cf380ca4be9b1e329fe57deba60,
title = "In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways",
abstract = "Serum lipoproteins may enter the airways and appear in sputum (chyloptysis) when the lymphatic circulation is impaired by inflammation, neoplasia, or an abnormal proliferation of smooth muscle cells. While analyzing the bronchoalveolar lavage fluid of a patient with chyloptysis, we noticed that surfactant could not be separated from contaminating serum lipoproteins and speculated that lipoproteins might interact with surfactant components. To clarify this point we immobilized surfactant protein (SP) A on microtiter wells and incubated it with 125I-labeled very low density lipoproteins (VLDLs), low-density lipoproteins, and high-density lipoproteins. We found that SP-A binds lipoproteins. Studying in greater detail the interaction of SP-A with VLDLs, we found that the binding is time and concentration dependent; is inhibited by unlabeled lipoproteins, phospholipids, and antibodies to SP-A; is increased by Ca2+; and is unaffected by methyl α-D-mannopyranoside. Whole surfactant is a potent inhibitor of binding. Furthermore, we found that SP-A increases the degradation of VLDLs by alveolar macrophages and favors the association of VLDLs with alveolar surfactant. We conclude that SP-A influences the disposal of serum lipoproteins entering the airways and speculate that binding to alveolar surfactant might represent an important step in the interaction between exogenous substances and the lung.",
keywords = "Alveolar macrophages, Lung surfactant, Lymphangioleiomyomatosis, Surfactant protein A",
author = "Antonella Alberti and Franco Ravenna and Daniela Quaglino and Maurizio Luisetti and Maurizio Muraca and Lorenzo Previato and Enzi, {Goretta Baldo} and Roberta Bruni and Aldo Baritussio",
year = "1998",
month = "5",
language = "English",
volume = "274",
journal = "American Journal of Physiology",
issn = "0363-6119",
publisher = "American Physiological Society",
number = "5 18-5",

}

TY - JOUR

T1 - In chyloptysis, SP-A affects the clearance of serum lipoproteins entering the airways

AU - Alberti, Antonella

AU - Ravenna, Franco

AU - Quaglino, Daniela

AU - Luisetti, Maurizio

AU - Muraca, Maurizio

AU - Previato, Lorenzo

AU - Enzi, Goretta Baldo

AU - Bruni, Roberta

AU - Baritussio, Aldo

PY - 1998/5

Y1 - 1998/5

N2 - Serum lipoproteins may enter the airways and appear in sputum (chyloptysis) when the lymphatic circulation is impaired by inflammation, neoplasia, or an abnormal proliferation of smooth muscle cells. While analyzing the bronchoalveolar lavage fluid of a patient with chyloptysis, we noticed that surfactant could not be separated from contaminating serum lipoproteins and speculated that lipoproteins might interact with surfactant components. To clarify this point we immobilized surfactant protein (SP) A on microtiter wells and incubated it with 125I-labeled very low density lipoproteins (VLDLs), low-density lipoproteins, and high-density lipoproteins. We found that SP-A binds lipoproteins. Studying in greater detail the interaction of SP-A with VLDLs, we found that the binding is time and concentration dependent; is inhibited by unlabeled lipoproteins, phospholipids, and antibodies to SP-A; is increased by Ca2+; and is unaffected by methyl α-D-mannopyranoside. Whole surfactant is a potent inhibitor of binding. Furthermore, we found that SP-A increases the degradation of VLDLs by alveolar macrophages and favors the association of VLDLs with alveolar surfactant. We conclude that SP-A influences the disposal of serum lipoproteins entering the airways and speculate that binding to alveolar surfactant might represent an important step in the interaction between exogenous substances and the lung.

AB - Serum lipoproteins may enter the airways and appear in sputum (chyloptysis) when the lymphatic circulation is impaired by inflammation, neoplasia, or an abnormal proliferation of smooth muscle cells. While analyzing the bronchoalveolar lavage fluid of a patient with chyloptysis, we noticed that surfactant could not be separated from contaminating serum lipoproteins and speculated that lipoproteins might interact with surfactant components. To clarify this point we immobilized surfactant protein (SP) A on microtiter wells and incubated it with 125I-labeled very low density lipoproteins (VLDLs), low-density lipoproteins, and high-density lipoproteins. We found that SP-A binds lipoproteins. Studying in greater detail the interaction of SP-A with VLDLs, we found that the binding is time and concentration dependent; is inhibited by unlabeled lipoproteins, phospholipids, and antibodies to SP-A; is increased by Ca2+; and is unaffected by methyl α-D-mannopyranoside. Whole surfactant is a potent inhibitor of binding. Furthermore, we found that SP-A increases the degradation of VLDLs by alveolar macrophages and favors the association of VLDLs with alveolar surfactant. We conclude that SP-A influences the disposal of serum lipoproteins entering the airways and speculate that binding to alveolar surfactant might represent an important step in the interaction between exogenous substances and the lung.

KW - Alveolar macrophages

KW - Lung surfactant

KW - Lymphangioleiomyomatosis

KW - Surfactant protein A

UR - http://www.scopus.com/inward/record.url?scp=0031836711&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031836711&partnerID=8YFLogxK

M3 - Article

C2 - 9612289

AN - SCOPUS:0031836711

VL - 274

JO - American Journal of Physiology

JF - American Journal of Physiology

SN - 0363-6119

IS - 5 18-5

ER -