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Related Experiment Videos

Alveolyn--structure and source: a review.

W S Lynn

    Experimental Lung Research
    |January 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Alveolyn, a large pulmonary glycoprotein, and its smaller fragments are found in lung secretions and amniotic fluid. These fragments contain collagenous domains and bind phospholipids, aiding lipid transfer.

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    Area of Science:

    • Pulmonary Medicine
    • Biochemistry
    • Glycoprotein Research

    Background:

    • Alveolyn is a large secretory glycoprotein (250,000 MW) identified in distal pulmonary secretions.
    • Other glycoproteins (130,000–36,000 MW) found in alveolar secretions are proteolytic fragments of Alveolyn.
    • Alveolyn is also a major protein in human amniotic fluid, likely originating from alveolar secretions.

    Purpose of the Study:

    • To characterize Alveolyn and its proteolytic fragments.
    • To investigate the structural and functional properties of these glycoproteins.

    Main Methods:

    • Identification and molecular weight determination of glycoproteins in pulmonary secretions.
    • Analysis of proteolytic fragments.
    • Collagenase digestion assays.

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  • Peptide sequence analysis (Gly-Pro-Hyp-Gly-type).

    • Main Results:

    • Alveolyn (250,000 MW) and its fragments (130,000, 80,000, 62,000, 36,000 MW) were identified in alveolar secretions.
    • Fragments of 62,000 MW and 36,000 MW possess both collagenous and noncollagenous domains.
    • Collagenous nature confirmed by collagenase susceptibility and specific amino acid sequences.
    • Alveolyn fragments bind phospholipids, potentially facilitating lipid transfer to air-water interfaces.

    Conclusions:

    • Alveolyn is a complex glycoprotein secreted by fetal type II pulmonary cells.
    • Its fragments exhibit unique structural features, including collagenous domains.
    • These glycoproteins play a role in lung surfactant function through phospholipid binding.