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pulmonary alveolar proteinosis/carbohydrate
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Isolation, characterization and localization of a 45 000 molecular weight, soluble glycoprotein from the lung in pulmonary alveolar proteinosis.
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A carbohydrate-rich, water-soluble glycoprotein has been isolated in pure form from delipidated lung lavage fluid from a patient with pulmonary alveolar proteinosis, in a three-step procedure involving ion-exchange and gel filtration chromatography. The molecular weight of the glycoprotein was
Elevation of tumour markers in serum and bronchoalveolar lavage fluid in pulmonary alveolar proteinosis.
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It is unclear whether tumour markers are generally increased in the serum and bronchoalveolar lavage fluid (BALF) of patients with pulmonary alveolar proteinosis (PAP). To clarify this point, levels of tumour markers were measured in the serum and BALF of patients with PAP. Squamous cell carcinoma
Accumulation of surfactant protein D in human pulmonary alveolar proteinosis.
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Surfactant protein D (SP-D) is a collagenous calcium-dependent carbohydrate-binding protein that is structurally related to the serum mannose-binding proteins and pulmonary surfactant protein A. SP-D was initially characterized as a biosynthetic product of freshly isolated rat type II cells and
Ultrastructural, histochemical, and freeze-fracture evaluation of multilamellated structures in human pulmonary alveolar proteinosis.
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Ultrastructural, histochemical, and freeze-fracture studies of material recovered by bronchoalveolar lavage from patients with pulmonary alveolar proteinosis revealed four types (A, B, C, and D) of multilamellated structures (MS). Type A, the major component, consisted of concentric, trilaminar
Isolation and characterization of a mucin-type glycoprotein from the lung lavage of a patient with alveolar proteinosis.
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A high molecular weight glycoprotein was isolated from the lavage fluid of a patient with alveolar proteinosis by gel chromatography with Sepharose CL-4B. The glycoprotein gave a single band stainable with alcian blue and with periodate-Schiff reagent on the cellulose acetate membrane
Human lung surfactant protein A exists in several different oligomeric states: oligomer size distribution varies between patient groups.
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BACKGROUND
Lung surfactant protein A (SP-A) is a complex molecule composed of up to 18 polypeptide chains. In vivo, SP-A probably binds to a wide range of inhaled materials via the interaction of surface carbohydrates with the lectin domains of SP-A and mediates their interaction with cells as part
Structure and activity of human surfactant protein D from different natural sources
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Surfactant protein D (SP-D) is a C-type lectin that participates in the innate immune defense of lungs. It binds pathogens through its carbohydrate recognition domain in a calcium-dependent manner. Human surfactant protein D (hSP-D) has been routinely obtained from bronchoalveolar lavage of patients
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