Document Detail


Lysyl oxidase oxidizes cell membrane proteins and enhances the chemotactic response of vascular smooth muscle cells.
MedLine Citation:
PMID:  18586678     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lysyl oxidase (LOX) is a potent chemokine inducing the migration of varied cell types. Here we demonstrate that inhibition of LOX activity by beta-aminopropionitrile (BAPN) in cultured rat aortic smooth muscle cells (SMCs) reduced the chemotactic response and sensitivity of these cells toward LOX and toward PDGF-BB. The chemotactic activity of PDGF-BB was significantly enhanced in the presence of a non-chemotactic concentration of LOX. We considered the possibility that extracellular LOX may oxidize cell surface proteins, including the PDGF receptor-beta (PDGFR-beta), to affect PDGF-BB-induced chemotaxis. Plasma membranes purified from control SMC contained oxidized PDGFR-beta. The oxidation of this receptor and other membrane proteins was largely prevented in cells preincubated with BAPN. Addition of purified LOX to these cells restored the profile of oxidized proteins toward that of control cells. The high affinity and capacity for the binding of PDGF-BB by cells containing oxidized PDGFR-beta was diminished by approximately 2-fold when compared with cells in which oxidation by LOX was prevented by BAPN. Phosphorylated members of the PDGFR-beta-dependent signal transduction pathway, including PDGFR-beta, SHP2, AKT1, and ERK1/ERK2 (p44/42 MAPK), turned over faster in BAPN-treated than in control SMCs. LOX knock-out mouse embryonic fibroblasts mirrored the effect obtained with SMCs treated with BAPN. These novel findings suggest that LOX activity is essential to generate optimal chemotactic sensitivity of cells to chemoattractants by oxidizing specific cell surface proteins, such as PDGFR-beta.
Authors:
Héctor A Lucero; Katya Ravid; Jessica L Grimsby; Celeste B Rich; Sandra J DiCamillo; Joni M Mäki; Johanna Myllyharju; Herbert M Kagan
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2008-06-27
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  283     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2008 Aug 
Date Detail:
Created Date:  2008-08-25     Completed Date:  2008-10-03     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  24103-17     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA. hlucero@bu.edu
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MeSH Terms
Descriptor/Qualifier:
Aminopropionitrile / pharmacology
Animals
Aorta / cytology,  enzymology*
Cells, Cultured
Chemotaxis / drug effects,  physiology*
Embryo, Mammalian / cytology,  enzymology
Fibroblasts / cytology,  enzymology
MAP Kinase Signaling System / physiology
Mice
Mice, Knockout
Muscle, Smooth, Vascular / cytology,  enzymology*
Myocytes, Smooth Muscle / cytology,  enzymology*
Oxidation-Reduction
Platelet-Derived Growth Factor / pharmacology
Protein-Lysine 6-Oxidase / antagonists & inhibitors,  metabolism*
Proto-Oncogene Proteins c-sis
Rats
Receptor, Platelet-Derived Growth Factor beta / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
HL 13262-31/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Platelet-Derived Growth Factor; 0/Proto-Oncogene Proteins c-sis; 0/platelet-derived growth factor BB; 151-18-8/Aminopropionitrile; EC 1.4.3.13/Protein-Lysine 6-Oxidase; EC 2.7.10.1/Receptor, Platelet-Derived Growth Factor beta
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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