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Complex protein composition of isolated focal adhesions: A two‐dimensional gel and database analysis
Author(s) -
Niederreiter Markus,
Gimona Mario,
Streichsbier Franz,
Celis Julio E.,
Small J. Victor
Publication year - 1994
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150150169
Subject(s) - focal adhesion , gelsolin , vinculin , adhesion , gel electrophoresis , paxillin , chemistry , actin , biology , microbiology and biotechnology , biochemistry , signal transduction , organic chemistry
Current ideas about the composition of the focal adhesion complexes in cultured cells are based mainly on indirect immunocytochemical data. We here report a two‐dimensional (2‐D) gel electrophoresis analysis of the focal adhesion associated‐structures that remain in the growth substrate after removal of cells by mechanical shearing. Many proteins additional to the known adhesion proteins, and in higher abundance, could be identified. Using selective extraction procedures, employing detergent or gelsolin, these could be classified as either membrane‐associated, actin‐associated or both. Cross correlation of these polypeptode patterns with a 2‐D gel database allowed identification of some proteins, not previously considered as resident of focal adhesions. The data point to a more complex make up of focal adhesions than formerly supposed.