Expression and subcellular distribution of filamin isotypes in endothelial cells and pericytes

Electrophoresis
N ShojaeeD Shepro

Abstract

Two principal forms of the actin binding protein, filamin, are expressed in mammalian cells: nonmuscle and muscle isotypes (FLN-1 and FLN-2). A protein that copurifies with an alpha-naphthyl acetate hydrolyzing esterase from human omentum microvessel endothelial cells (EC) is isolated by nondenaturing electrophoresis, sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and electroblotting. The purified protein is subjected to in situ trypsin cleavage, reversed-phase high performance liquid chromatography (HPLC) and automated Edman degradation. Six peptide fragments from the protein are identified to have 60-66% identity with nonmuscle filamin (ABP-280). Two of these peptides are 100% identical to a previously sequenced human muscle filamin fragment. Polyclonal antibody is produced using a 16-residue synthetic peptide corresponding to a structural beta-sheet region of muscle filamin. Compared with a variety of vascular cells evaluated, retinal pericytes express an abundance of both muscle and non-muscle filamin isotypes. Pericytes contain at least 10 times more muscle filamin than human umbilical vein EC and at least three times the amount expressed in human omentum microvessel and bovine pulmonary artery EC. Differe...Continue Reading

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Jan 1, 1990·Methods in Enzymology·B Storrie, E A Madden
Sep 1, 1990·The Journal of Cell Biology·J B GorlinJ H Hartwig
Oct 1, 1988·The Journal of Cell Biology·J D Cortese, C Frieden
Dec 16, 1985·European Journal of Biochemistry·T OhtakiA Asano
Nov 1, 1971·Analytical Biochemistry·C Beauchamp, I Fridovich
Jan 1, 1983·Cell Motility·P H Mangeat, K Burridge
Jan 1, 1984·Cell Motility·M A RockwellD L Taylor
Feb 1, 1983·The Journal of Cell Biology·R H Gomer, E Lazarides
Dec 1, 1980·The Journal of Cell Biology·J H HartwigT P Stossel
Dec 10, 1981·Nature·K Burridge, J R Feramisco
Feb 1, 1995·Current Opinion in Cell Biology·P A Janmey, C Chaponnier
Feb 1, 1994·Current Opinion in Cell Biology·A L Hitt, E J Luna
Jul 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·P J LeedmanL C Harrison
Aug 1, 1993·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·D Shepro, N M Morel
Nov 1, 1995·In Vitro Cellular & Developmental Biology. Animal·C GalustianJ A Firth
Jan 1, 1997·Free Radical Biology & Medicine·L E HastieD Shepro
Dec 28, 1964·Annals of the New York Academy of Sciences·L ORNSTEIN
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS

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Citations

Feb 19, 2000·Developmental Dynamics : an Official Publication of the American Association of Anatomists·W ChiangG E Lyons
Aug 27, 1999·Journal of Cellular Biochemistry·N ShojaeeD Shepro
Jan 12, 2010·Trends in Cell Biology·Alex-Xianghua ZhouLevent M Akyürek
Nov 6, 2007·Journal of Cellular and Molecular Medicine·Chunfa Huang, R Tyler Miller
Mar 12, 2005·Health Physics·J Kenneth Shultis, Richard E Faw

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