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Related Experiment Videos

Mouse procollagen IV. Characterization and supramolecular association

H P Bächinger, L I Fessler, J H Fessler

    The Journal of Biological Chemistry
    |August 25, 1982
    PubMed
    Summary

    Procollagen IV molecules self-assemble into basement membrane networks. This study visualizes procollagen IV structure and noncovalent associations, supporting a network model for these crucial extracellular matrix components.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Extracellular Matrix Research

    Background:

    • The endodermal cell line PF-HR9, derived from murine teratocarcinoma, was cultured as monolayers and embryoid bodies.
    • Procollagen IV and laminin were isolated from culture media, and their presence near cells and in media was confirmed via specific antibodies.

    Purpose of the Study:

    • To characterize the structure and assembly of procollagen IV molecules.
    • To investigate the noncovalent associations of procollagen IV, supporting basement membrane network models.

    Main Methods:

    • Isolation and characterization of procollagen IV and laminin.
    • Circular dichroism spectroscopy and thermal transition analysis.
    • Electron microscopy (rotary shadowing) and velocity sedimentation.

    Main Results:

    • Procollagen IV consists of pro alpha 1 IV and pro alpha 2 IV chains with helical characteristics and thermal transitions.
    • Electron microscopy revealed a 434 nm linear thread of procollagen IV with a carboxyl-terminal knob.
    • Noncovalent associations of procollagen IV molecules (dimers, tetramers) were observed via amino-terminal and carboxyl-terminal linkages.

    Conclusions:

    • Procollagen IV molecules associate noncovalently to form components found in basement membranes.
    • The findings strongly support a network model for basement membrane supramolecular assembly.

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