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Title: 12S-lipoxygenase protein associates with {alpha}-actin fibers in human umbilical artery vascular smooth muscle cells

Abstract

The current study sets out to characterize the intracellular localization of the platelet-type 12S-lipoxygenase (12-LO), an enzyme involved in angiotensin-II induced signaling in vascular smooth muscle cells (VSMC). Immunohistochemical analysis of VSMC in vitro or human umbilical arteries in vivo showed a clear cytoplasmic localization. On immunogold electron microscopy, 12-LO was found primarily associated with cytoplasmic VSMC muscle fibrils. Upon angiotensin-II treatment of cultured VSMC, immunoprecipitated 12-LO was found bound to {alpha}-actin, a component of the cytoplasmic myofilaments. 12-LO/{alpha}-actin binding was blocked by VSMC pretreatment with the 12-LO inhibitors, baicalien or esculetine and the protein synthesis inhibitor, cycloheximide. Moreover, the binding of 12-LO to {alpha}-actin was not associated with 12-LO serine or tyrosine phosphorylation. These observations suggest a previously unrecognized angiotensin-II dependent protein interaction in VSMC through which 12-LO protein may be trafficked, for yet undiscovered purposes towards the much more abundantly expressed cytoskeletal protein {alpha}-actin.

Authors:
 [1];  [2];  [2];  [2];  [3];  [4];  [5];  [2]
  1. Institute of Endocrinology, Metabolism and Hypertension, Tel Aviv Sourasky Medical Center, 6 Weizman Street 64239 Tel Aviv, and the Sackler Faculty of Medicine, Tel Aviv University (Israel). E-mail: gary_w@tasmc.health.gov.il
  2. Institute of Endocrinology, Metabolism and Hypertension, Tel Aviv Sourasky Medical Center, 6 Weizman Street 64239 Tel Aviv, and the Sackler Faculty of Medicine, Tel Aviv University (Israel)
  3. Department of Biological Regulation, Weizman Institute, Rehovot (Israel)
  4. EM Unit, Weizman Institute, Rehovot (Israel)
  5. Department of Chemical Engineering and Biotechnology, College of Judea and Sameria, Ariel (Israel)
Publication Date:
OSTI Identifier:
20991332
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 356; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2007.03.012; PII: S0006-291X(07)00463-9; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ACTIN; ANGIOTENSIN; ARTERIES; CYCLOHEXIMIDE; ELECTRON MICROSCOPY; ENZYMES; FIBERS; HUMAN POPULATIONS; IN VITRO; IN VIVO; MUSCLES; PHOSPHORYLATION; SERINE; TYROSINE

Citation Formats

Weisinger, Gary, Limor, Rona, Marcus-Perlman, Yonit, Knoll, Esther, Kohen, Fortune, Schinder, Vera, Firer, Michael, and Stern, Naftali. 12S-lipoxygenase protein associates with {alpha}-actin fibers in human umbilical artery vascular smooth muscle cells. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.03.012.
Weisinger, Gary, Limor, Rona, Marcus-Perlman, Yonit, Knoll, Esther, Kohen, Fortune, Schinder, Vera, Firer, Michael, & Stern, Naftali. 12S-lipoxygenase protein associates with {alpha}-actin fibers in human umbilical artery vascular smooth muscle cells. United States. doi:10.1016/j.bbrc.2007.03.012.
Weisinger, Gary, Limor, Rona, Marcus-Perlman, Yonit, Knoll, Esther, Kohen, Fortune, Schinder, Vera, Firer, Michael, and Stern, Naftali. Fri . "12S-lipoxygenase protein associates with {alpha}-actin fibers in human umbilical artery vascular smooth muscle cells". United States. doi:10.1016/j.bbrc.2007.03.012.
@article{osti_20991332,
title = {12S-lipoxygenase protein associates with {alpha}-actin fibers in human umbilical artery vascular smooth muscle cells},
author = {Weisinger, Gary and Limor, Rona and Marcus-Perlman, Yonit and Knoll, Esther and Kohen, Fortune and Schinder, Vera and Firer, Michael and Stern, Naftali},
abstractNote = {The current study sets out to characterize the intracellular localization of the platelet-type 12S-lipoxygenase (12-LO), an enzyme involved in angiotensin-II induced signaling in vascular smooth muscle cells (VSMC). Immunohistochemical analysis of VSMC in vitro or human umbilical arteries in vivo showed a clear cytoplasmic localization. On immunogold electron microscopy, 12-LO was found primarily associated with cytoplasmic VSMC muscle fibrils. Upon angiotensin-II treatment of cultured VSMC, immunoprecipitated 12-LO was found bound to {alpha}-actin, a component of the cytoplasmic myofilaments. 12-LO/{alpha}-actin binding was blocked by VSMC pretreatment with the 12-LO inhibitors, baicalien or esculetine and the protein synthesis inhibitor, cycloheximide. Moreover, the binding of 12-LO to {alpha}-actin was not associated with 12-LO serine or tyrosine phosphorylation. These observations suggest a previously unrecognized angiotensin-II dependent protein interaction in VSMC through which 12-LO protein may be trafficked, for yet undiscovered purposes towards the much more abundantly expressed cytoskeletal protein {alpha}-actin.},
doi = {10.1016/j.bbrc.2007.03.012},
journal = {Biochemical and Biophysical Research Communications},
number = 3,
volume = 356,
place = {United States},
year = {Fri May 11 00:00:00 EDT 2007},
month = {Fri May 11 00:00:00 EDT 2007}
}