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Time‐lapse imaging of extracellular matrix assembly
Author(s) -
Wagenseil Jessica E,
Kozel Beth A,
Czirok Andras,
Rongish Brenda J,
Mecham Robert P
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.101.1
Subject(s) - tropoelastin , elastin , fibulin , extracellular matrix , fibronectin , fibrillin , elastic fiber , biophysics , chemistry , fiber , extracellular , matrix (chemical analysis) , fibril , microbiology and biotechnology , materials science , composite material , biochemistry , biology , genetics , organic chemistry , chromatography
The extracellular matrix (ECM) is a composite polymer made up of many different components. The cell takes an active role in ECM assembly through targeted secretion of ECM components and through the active participation of matrix‐organizing binding proteins on the cell surface. To learn more about how the cell organizes ECM, we studied elastic fiber formation using time‐lapse imaging microscopy. Elastic fibers are formed from soluble elastin monomers, tropoelastin, which are crosslinked to form fibers of mature elastin. The initial step in elastic fiber assembly is the formation of tropoelastin aggregates on the cell surface (microassembly). Over several hours, these aggregates coalesce to become larger and are eventually transferred onto microfibrils, which serve to structure the growing fiber in the extracellular space (macroassembly). The assembly of microfibrils also occurs in a defined spatial and temporal sequence. Fibronectin, fibrillin‐1 and MAGP‐1 start as fibers, while fibulin‐5 and tropoelastin start as a combination of fibers and aggregates. Many of the fibulin‐5 aggregates co‐localize with the subsequent tropoelastin aggregates suggesting that fibulin‐5 may play a role in elastic fiber microassembly.