Surfactant Protein-A Concentration in Bronchoalveolar Lavage Fluids of Patients With Pulmonary Alveolar Proteinosis

CHEST Journal ◽  
1993 ◽  
Vol 103 (2) ◽  
pp. 496-499 ◽  
Author(s):  
Yasuhito Honda ◽  
Hiroki Takahashi ◽  
Noriharu Shijubo ◽  
Yoshio Kuroki ◽  
Toyoaki Akino
Keyword(s):  
Bronchoalveolar Lavage ◽  
Pulmonary Alveolar Proteinosis ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Alveolar Proteinosis

Alveolar Proteinosis and Phospholipidoses of the Lungs

1991 ◽  
Vol 19 (4_part_1) ◽  
pp. 482-513 ◽  
Author(s):  
Gary E. R. Hook
Keyword(s):  
Pulmonary Alveolar Proteinosis ◽  
Protein A ◽  
Surfactant Protein ◽  
Phospholipid Metabolism ◽  
Therapeutic Agents ◽  
Human Condition ◽  
Surfactant Protein A ◽  
The Status ◽  
Alveolar Proteinosis ◽  
Surfactant Phospholipids

Three pulmonary disease conditions result from the accumulation of phospholipids in the lung. These conditions are the human lung disease known as pulmonary alveolar proteinosis, the lipoproteinosis that arises in the lungs of rats during acute silicosis, and the phospholipidoses induced by numerous cationic amphiphilic therapeutic agents. In this paper, the status of phospholipid metabolism in the lungs during the process of each of these lung conditions has been reviewed and possible mechanisms for their establishment are discussed. Pulmonary alveolar proteinosis is characterized by the accumulation of tubular myelin-like multilamellated structures in the alveoli and distal airways of patients. These structures appear to be formed by a process of spontaneous assembly involving surfactant protein A and surfactant phospholipids. Structures similar to tubular myelin-like multilamellated structures can be seen in the alveoli of rats during acute silicosis and, as with the human condition, both surfactant protein A and surfactant phospholipids accumulate in the alveoli. Excessive accumulation of surfactant protein A and surfactant phospholipids in the alveoli could arise from their overproduction and hypersecretion by a subpopulation of Type II cells that are activated by silica, and possibly other agents. Phospholipidoses caused by cationic amphiphilic therapeutic agents arise as a result of their inhibition of phospholipid catabolism. Inhibition of phospholipases results in the accumulation of phospholipids in the cytoplasm of alveolar macrophages and other cells. While inhibition of phospholipases by these agents undoubtedly occurs, there are many anomalous features, such as the accumulation of extracellular phospholipids and surfactant protein A, that cannot be accounted for by this simplistic hypothesis.

scholarly journals A novel procedure for the rapid isolation of surfactant protein A with retention of its alveolar-macrophage-stimulating properties

1995 ◽  
Vol 309 (2) ◽  
pp. 551-555 ◽  
Author(s):  
J F van Iwaarden ◽  
F Teding van Berkhout ◽  
J A Whitsett ◽  
R S Oosting ◽  
L M G van Golde
Keyword(s):  
Alveolar Macrophage ◽  
Alveolar Macrophages ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Normal Rat ◽  
Normal Human ◽  
Novel Method ◽  
Alveolar Proteinosis ◽  
Simplex Virus

Previous studies have shown that surfactant protein A (SP-A) derived from alveolar-proteinosis patients activates rat alveolar macrophages. However, it is not known if normal rat, dog and human SP-A can also stimulate alveolar macrophages. As alveolar-proteinosis SP-A has a slightly different structure from ordinary SP-A, it would be possible that the ascribed alveolar-macrophage-stimulating properties of SP-A are restricted to alveolar-proteinosis SP-A. To clarify this issue, we isolated SP-A from normal rat and dog pulmonary surfactants, using the same isolation technique commonly used for the isolation of alveolar-proteinosis SP-A, i.e. by butanol precipitation. In contrast with human alveolar-proteinosis SP-A, rat and dog SP-A obtained thus could not activate rat alveolar macrophages to produce oxygen radicals or enhance the phagocytosis of fluorescein isothiocyanate-labelled herpes simplex virus. However, rat, dog and normal human SP-A isolated by a novel method, involving extraction from pulmonary surfactant by using n-octyl beta-D-glucopyranoside and subsequent purification by cation-exchange chromatography, were able to elicit an oxidative burst in rat as well as normal human alveolar macrophages. In addition, dog and rat SP-A obtained thus stimulated the phagocytosis of herpes simplex virus by rat alveolar macrophages. These findings indicate that normal human, rat and dog SP-A have the same alveolar-macrophage-stimulating properties as human alveolar proteinosis SP-A. Dog and rat SP-A isolated by this novel method had the same Ca(2+)-dependent self-aggregation and lipid-aggregation properties as SP-A isolated by butanol precipitation. The new and milder isolation procedure yielded SP-A of high purity, as judged by SDS/PAGE and ELISA.

SURFACTANT PROTEIN A IN BRONCHOALVEOLAR LAVAGE FLUID OF CHILDREN WITH CYSTIC FIBROSIS

2004 ◽  
Vol 32 (Supplement) ◽  
pp. A115
Author(s):  
Neal J Thomas ◽  
Gavin R Graff ◽  
Todd M Umstead ◽  
David S Phelps ◽  
Joanna Floros
Keyword(s):  
Cystic Fibrosis ◽  
Bronchoalveolar Lavage ◽  
Bronchoalveolar Lavage Fluid ◽  
Protein A ◽  
Lavage Fluid ◽  
Surfactant Protein ◽  
Surfactant Protein A
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