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Surfactant protein A accumulating in the alveoli of patients with pulmonary alveolar proteinosis: oligomeric structure and interaction with lipids. Paper-573330. APP-I failed to form tubular myelin structures.
These populations of APP showed almost identical amino acid compositions. Paper-573330.
They also induced phospholipid vesicle aggregation in a concentration-dependent manner.
In contrast, APP-II formed well-formed lattice structures seen in tubular myelin.
The population seen for APP-II was similar to that seen for SP-A from healthy individuals. Paper-573330.
Both APP-I and APP-II retained the abilities to bind dipalmitoylphosphatidylcholine ( DPPC). Paper-573330.
In contrast, APP-I was observed as multimerized larger aggregates whose diameter appeared to be about 70 to 90 nm.
The maximal turbidity for light scattering induced by APP-I and APP-II was almost equivalent when analyzed as a function of molar concentration.
Its major pathologic manifestations are a small number of normal tubular myelin structures and an unusual abundance of multilamellated structures.
Electron microscopic observations of APP molecules using the rotary shadow technique revealed that APP-II was observed as hexameric particles, presumably consisting mainly of octadecamers whose diameter was approximately 30 nm. Paper-573330.
Pulmonary alveolar proteinosis ( PAP) is a diffuse lung disease of unknown etiology in which the alveoli and terminal bronchioles of the lung fill with large amounts of surfactant-rich lipoproteinaceous materials. Paper-573330.
In vitro reconstitution experiments with porcine surfactant protein B ( SP-B) and phospholipids revealed that the multilamellated membranes in structures formed from APP-I consisted of several layers of doubled unit membranes. Paper-573330.
Analysis of APP by Bio Gel A15m column chromatography revealed that it was composed of two protein peaks, one of which (APP-I) eluted at the position near that of blue dextran whereas the other (APP-II) eluted far behind blue dextran but ahead of thyroglobulin. Paper-573330.
From these data we conclude that there exists an abnormal multimerized form of SP-A oligomer in the alveoli of patients with PAP, and that this unusual subpopulation of SP-A oligomer exhibits abnormal function on phospholipid membrane organization. Paper-573330.
Since surfactant protein A ( SP-A) plays an important role in surfactant phospholipid homeostasis, we investigated the structural features of SP-A oligomers ( alveolar proteinosis protein, APP) accumulating in the alveoli of individuals with PAP, and examined the abilities of APP to interact with lipids. Paper-573330.
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