J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kang, L.-T.
Right arrow Articles by Vanderhoek, J. Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kang, L.-T.
Right arrow Articles by Vanderhoek, J. Y.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The Journal of Lipid Research, Vol. 39, 1476-1482, July 1998
Copyright © 1998 by Lipid Research, Inc.


Original Article

Mono (S) hydroxy fatty acids: novel ligands for cytosolic actin

Li-Ta Kanga and Jack Y. Vanderhoeka
a Department of Biochemistry and Molecular Biology, The George Washington University Medical Center, 2300 Eye Street, N.W., Washington, DC 20037

Correspondence to: Jack Y. Vanderhoek.

The ubiquitous hydroxylated fatty acids derived from arachidonic acid (HETEs) or linoleic acid (HODEs) exhibit diverse biological effects including chemotaxis, cell proliferation, and modulation of several enzymatic pathways, including the 5-lipoxygenase leading to the inflammatory leukotrienes. It was observed that 12(S)- and 15(S)-HETE and 13(S)-HODE (12- and 15-lipoxygenase-derived metabolites, respectively) inhibited the 5-lipoxygenase present in rat basophilic leukemia (RBL -1) cell homogenates whereas the 15(R) chiral enantiomer and the nonhydroxylated linoleic, oleic, and stearic acids were either less potent or ineffective. In examining the mechanism of this inhibition, the relative effectiveness of several fatty acids in displacing [3H]15-HETE bound to cytosol preparations were compared and the results indicated that these (S) hydroxy fatty acids and 5(S)-HETE were significantly more potent than either the 15(R) enantiomer, 15(S)-HETE methyl ester, arachidonic acid, or prostaglandin F2{alpha}. In order to identify the protein(s) that specifically binds HETEs, 15(S)-HETE biotin hydrazide was used as a probe to detect any HETE–protein complexes as this compound both inhibited the 5-lipoxygenase and interfered with the binding of [3H]15-HETE to cytosol preparations. SDS-PAGE analysis and chemiluminescent detection revealed that the major cytosolic proteins that bound this biotinylated probe had molecular masses of 43 and 51 kD. Fatty acid competition experiments indicated that the order of effectiveness in displacing this probe from these proteins was 13(S)-HODE > 5(S)-HETE {approx}15(S)-HETE > > stearic acid {approx}arachidonic acid {approx}15(R)-HETE. Amino acid sequence analysis showed that the 43 kD protein was actin.

These findings suggest the possibility that actin may play a major role in the biological effects of monohydroxylated metabolites derived from cellular 5-, 12-, and 15-lipoxygenases.—Kang, L-T., and J. Y. Vanderhoek. Mono (S) hydroxy fatty acids: novel ligands for cytosolic actin. J. Lipid Res. 1998. 39: 1476–1482.

Supplementary key words: 5-lipoxygenase, inhibition, binding, chemiluminescence


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
American MineralogistHome page
R. M. Hazen
Presidential Address to the Mineralogical Society of America, Salt Lake City, October 18, 2005: Mineral surfaces and the prebiotic selection and organization of biomolecules
American Mineralogist, November 1, 2006; 91(11-12): 1715 - 1729.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Pathol.Home page
T. Arnould, R. Thibaut-Vercruyssen, N. Bouaziz, M. Dieu, J. Remacle, and C. Michiels
PGF2{{alpha}}, a Prostanoid Released by Endothelial Cells Activated by Hypoxia, Is a Chemoattractant Candidate for Neutrophil Recruitment
Am. J. Pathol., July 1, 2001; 159(1): 345 - 357.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
P. Provost, B. Samuelsson, and O. Radmark
Interaction of 5-lipoxygenase with cellular proteins
PNAS, March 2, 1999; 96(5): 1881 - 1885.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Provost, J. Doucet, T. Hammarberg, G. Gerisch, B. Samuelsson, and O. Radmark
5-Lipoxygenase Interacts with Coactosin-like Protein
J. Biol. Chem., May 4, 2001; 276(19): 16520 - 16527.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
O. Werz, J. Klemm, B. Samuelsson, and O. Radmark
5-Lipoxygenase is phosphorylated by p38 kinase-dependent MAPKAP kinases
PNAS, May 9, 2000; 97(10): 5261 - 5266.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.